PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2615188-2 1989 Tubule fluid iron is determined by the magnitude of the glomerular leak for transferrin and the iron saturation of transferrin. Iron 13-17 transferrin Rattus norvegicus 76-87 2608449-10 1989 Since transferrin is indispensible for the utilization of iron by the heme-synthesizing red cell precursors, transferrin concentration in the blood is the limiting factor for the utilization of iron in hemoglobin synthesis. Iron 58-62 transferrin Rattus norvegicus 6-17 2608449-10 1989 Since transferrin is indispensible for the utilization of iron by the heme-synthesizing red cell precursors, transferrin concentration in the blood is the limiting factor for the utilization of iron in hemoglobin synthesis. Iron 58-62 transferrin Rattus norvegicus 109-120 2608449-10 1989 Since transferrin is indispensible for the utilization of iron by the heme-synthesizing red cell precursors, transferrin concentration in the blood is the limiting factor for the utilization of iron in hemoglobin synthesis. Iron 194-198 transferrin Rattus norvegicus 109-120 2615188-2 1989 Tubule fluid iron is determined by the magnitude of the glomerular leak for transferrin and the iron saturation of transferrin. Iron 13-17 transferrin Rattus norvegicus 115-126 2615188-2 1989 Tubule fluid iron is determined by the magnitude of the glomerular leak for transferrin and the iron saturation of transferrin. Iron 96-100 transferrin Rattus norvegicus 115-126 2584367-0 1989 [Regulation of ferritin and transferrin synthesis in hepatocytes depending on iron status of rats]. Iron 78-82 transferrin Rattus norvegicus 28-39 2679134-6 1989 The uptake of non-transferrin-bound iron was also increased in HD and LD hepatocytes at 24 h but only in HD cells at 1 h. Transferrin binding was not altered in LPS-treated cells from ND rats but was depressed in cells from LPS-treated rats both at 1 h and at 24 h after injection. Iron 36-40 transferrin Rattus norvegicus 18-29 2679134-6 1989 The uptake of non-transferrin-bound iron was also increased in HD and LD hepatocytes at 24 h but only in HD cells at 1 h. Transferrin binding was not altered in LPS-treated cells from ND rats but was depressed in cells from LPS-treated rats both at 1 h and at 24 h after injection. Iron 36-40 transferrin Rattus norvegicus 122-133 2478317-3 1989 Because of the importance of iron in basic cell metabolism we have hypothesized that iron (mobilized by Tf) may be a permissive agent in the process of myelination. Iron 29-33 transferrin Rattus norvegicus 104-106 2478317-3 1989 Because of the importance of iron in basic cell metabolism we have hypothesized that iron (mobilized by Tf) may be a permissive agent in the process of myelination. Iron 85-89 transferrin Rattus norvegicus 104-106 2478317-13 1989 The temporal association of Tf and myelin production suggests that further study is warranted regarding the possibility that the Tf-iron system supports or perhaps even permits the initiation of the process of myelination. Iron 132-136 transferrin Rattus norvegicus 28-30 2478317-13 1989 The temporal association of Tf and myelin production suggests that further study is warranted regarding the possibility that the Tf-iron system supports or perhaps even permits the initiation of the process of myelination. Iron 132-136 transferrin Rattus norvegicus 129-131 2795208-9 1989 In contrast, the iron-transferrin complex may be useful for measuring and imaging transferrin-specific receptors in brain and tumor tissue. Iron 17-21 transferrin Rattus norvegicus 22-33 2795208-9 1989 In contrast, the iron-transferrin complex may be useful for measuring and imaging transferrin-specific receptors in brain and tumor tissue. Iron 17-21 transferrin Rattus norvegicus 82-93 2912502-2 1989 Uptake of iron from ferritin by the cells is partially inhibited by including apotransferrin in the culture medium, but not by inclusion of diferric transferrin. Iron 10-14 transferrin Rattus norvegicus 81-92 2758037-9 1989 Under normal conditions, there is no significant intracellular or intramitochondrial iron pool in reticulocytes, which are therefore dependent upon continuous delivery of transferrin-bound iron to maintain heme synthesis. Iron 189-193 transferrin Rattus norvegicus 171-182 2735408-5 1989 When livers were perfused with increasing concentrations of transferrin the uptake into the different peaks of transferrin and iron increased in a curvilinear fashion, which indicated that uptake occurred by saturable and nonsaturable processes, both of which increased in iron deficiency. Iron 127-131 transferrin Rattus norvegicus 60-71 2926242-3 1989 Iron 55-labeled rat transferrin was injected at the same time as the 59Fe-labeled compound, and storage iron release was calculated from the cumulative incorporation of the two isotopes in the red cell mass over 2 weeks. Iron 0-4 transferrin Rattus norvegicus 20-31 2926242-7 1989 A strong correlation between hepatocyte iron release and plasma transferrin receptor levels was observed (p less than 0.001), suggesting that plasma transferrin receptors could mediate the regulation of hepatocyte iron mobilization in rats. Iron 40-44 transferrin Rattus norvegicus 64-75 2926242-7 1989 A strong correlation between hepatocyte iron release and plasma transferrin receptor levels was observed (p less than 0.001), suggesting that plasma transferrin receptors could mediate the regulation of hepatocyte iron mobilization in rats. Iron 40-44 transferrin Rattus norvegicus 149-160 2926242-7 1989 A strong correlation between hepatocyte iron release and plasma transferrin receptor levels was observed (p less than 0.001), suggesting that plasma transferrin receptors could mediate the regulation of hepatocyte iron mobilization in rats. Iron 214-218 transferrin Rattus norvegicus 64-75 2926242-7 1989 A strong correlation between hepatocyte iron release and plasma transferrin receptor levels was observed (p less than 0.001), suggesting that plasma transferrin receptors could mediate the regulation of hepatocyte iron mobilization in rats. Iron 214-218 transferrin Rattus norvegicus 149-160 2546742-1 1989 Transferrin, a serum iron-binding protein, delivers iron to the cell after binding to specific receptors on the cell surface and is an important component of culture medium for virtually all cell lines, including the FRTL5 line of rat thyroid follicular cells. Iron 21-25 transferrin Rattus norvegicus 0-11 2546742-1 1989 Transferrin, a serum iron-binding protein, delivers iron to the cell after binding to specific receptors on the cell surface and is an important component of culture medium for virtually all cell lines, including the FRTL5 line of rat thyroid follicular cells. Iron 52-56 transferrin Rattus norvegicus 0-11 2719657-3 1989 Purified rat transferrin was radiolabelled either with 125I (protein moiety) or with 3H (sialyl residues), and subsequently saturated with iron. Iron 139-143 transferrin Rattus norvegicus 13-24 2468292-12 1989 According to the same technique, intraperitoneally administered diferric transferrin retained its iron during passage into the circulation. Iron 98-102 transferrin Rattus norvegicus 73-84 2732309-0 1989 [Detection of transferrin in the digestive juices of rat and its possible role in iron absorption from the small intestine]. Iron 82-86 transferrin Rattus norvegicus 14-25 2732309-1 1989 Presence of transferrin in digestive juices and its possible role in iron absorption of rats were examined. Iron 69-73 transferrin Rattus norvegicus 12-23 2732309-3 1989 Transferrin concentration in pancreas juice was the highest (approximately 0.28 mg/ml) in the collected digestive juices and the concentration in iron deficient rats was 4 times higher than that of normal rats. Iron 146-150 transferrin Rattus norvegicus 0-11 2732309-4 1989 The iron saturation rate of transferrin in pancreas juice was approximately 40%. Iron 4-8 transferrin Rattus norvegicus 28-39 2732309-5 1989 The participation of transferrin in iron absorption was investigated by the absorption through the intestinal segment of rats, into which 59Fe labeled diferric transferrin was injected. Iron 36-40 transferrin Rattus norvegicus 21-32 2732309-8 1989 Iron absorption from diferric transferrin in the duodenal segment was inhibited by 1 mM monodansylcadaverine, the inhibitor of endocytosis, or addition of 20 times the normal amounts of nonradioactive transferrin in the test material. Iron 0-4 transferrin Rattus norvegicus 30-41 2732309-8 1989 Iron absorption from diferric transferrin in the duodenal segment was inhibited by 1 mM monodansylcadaverine, the inhibitor of endocytosis, or addition of 20 times the normal amounts of nonradioactive transferrin in the test material. Iron 0-4 transferrin Rattus norvegicus 201-212 2732309-9 1989 These data indicated that the process of iron absorption through diferric transferrin was not a passive phenomenon. Iron 41-45 transferrin Rattus norvegicus 74-85 2666983-4 1989 We found that beta-cell proliferation is stimulated by iron-saturated transferrin, interleukin-1-alpha, fetal calf serum, and glucose. Iron 55-59 transferrin Rattus norvegicus 70-81 2492027-9 1989 It is suggested that this effect of lactic acid is mediated by increased dissociation of catalytic iron from proteins of the transferrin type. Iron 99-103 transferrin Rattus norvegicus 125-136 2752211-0 1989 Effects of iron overload on transferrin secretion by cultured fetal rat hepatocytes. Iron 11-15 transferrin Rattus norvegicus 28-39 2752211-4 1989 The present data demonstrate that iron overload decreases transferrin secretion; this effect appears not to be specific, since albumin production is affected in a similar manner. Iron 34-38 transferrin Rattus norvegicus 58-69 2752211-6 1989 Since the corresponding mRNA is unaffected, it may be postulated that iron overload decreases transferrin secretion at some post-transcriptional level. Iron 70-74 transferrin Rattus norvegicus 94-105 2850162-5 1988 Pretreatment of the cells with the weak base primaquine had no influence on this distribution while at the same time uptake of iron via the transferrin receptor was inhibited. Iron 127-131 transferrin Rattus norvegicus 140-151 3182815-0 1988 Hepatocytes and reticulocytes have different mechanisms for the uptake of iron from transferrin. Iron 74-78 transferrin Rattus norvegicus 84-95 3182815-1 1988 The uptake of iron from transferrin by isolated rat hepatocytes and rat reticulocytes has been compared. Iron 14-18 transferrin Rattus norvegicus 24-35 3182815-5 1988 2) Hepatocyte plasma membrane NADH:ferricyanide oxidoreductase activity and uptake of iron from transferrin are stimulated by low oxygen concentration and inhibited by iodoacetate. Iron 86-90 transferrin Rattus norvegicus 96-107 3182815-7 1988 3) Ferricyanide inhibits the uptake of iron from transferrin by hepatocytes, but has no effect on iron uptake by reticulocytes. Iron 39-43 transferrin Rattus norvegicus 49-60 3182815-12 1988 The results are compatible with hepatocyte uptake of iron from transferrin by a reductive process at the cell surface and reticulocyte iron uptake by receptor-mediated endocytosis. Iron 53-57 transferrin Rattus norvegicus 63-74 3350861-6 1988 The results suggest that nicotine acts by blocking uptake, probably by acting as a weak base inhibiting iron release from transferrin, and inhibiting exocytosis with a resultant block of endocytosis. Iron 104-108 transferrin Rattus norvegicus 122-133 3415986-6 1988 At a low incubation concentration of transferrin (0.5 microM), the presence of both rat albumin and the antibody decreased the rate of iron uptake by the cells to about 15% of the value found in their absence, but to only 40% when the diferric transferrin concentration was 5 microM. Iron 135-139 transferrin Rattus norvegicus 37-48 3415986-6 1988 At a low incubation concentration of transferrin (0.5 microM), the presence of both rat albumin and the antibody decreased the rate of iron uptake by the cells to about 15% of the value found in their absence, but to only 40% when the diferric transferrin concentration was 5 microM. Iron 135-139 transferrin Rattus norvegicus 244-255 3415986-7 1988 These results confirm that the uptake of transferrin-bound iron by both fetal and adult rat hepatocytes in culture occurs by a specific, receptor-mediated process and a low-affinity, non-saturable process. Iron 59-63 transferrin Rattus norvegicus 41-52 3407805-5 1988 Erythron iron uptake was increased in proportion to the increased receptor number in phenylhydrazine-treated animals but was reduced in iron deficiency because of the limited amount of iron-bearing transferrin. Iron 9-13 transferrin Rattus norvegicus 198-209 3169492-6 1988 In normal rats, DFO injections also significantly blocked absorption of inorganic iron and transferrin iron. Iron 103-107 transferrin Rattus norvegicus 91-102 3046665-2 1988 The serum transferrin contaminating mucosal preparations, even when fully saturated with iron and in the presence of proteinase inhibitors, also acquires the properties of the mucosal transferrin when the mucosa is homogenised. Iron 89-93 transferrin Rattus norvegicus 10-21 3183569-4 1988 It is concluded that germ cells normally located within the adluminal compartment of the seminiferous tubules may be capable of controlling their own supply of iron via their influence upon transferrin secretion by the Sertoli cells. Iron 160-164 transferrin Rattus norvegicus 190-201 3294334-4 1988 Dietary iron depletion resulted in anemia (hematocrit 25 vs. 46%), microcytosis (MCV 54 vs. 60 fl), and reduced transferrin saturation (17 vs. 96%) without any effect on infection (peak parasitemia 30 vs. 36%). Iron 8-12 transferrin Rattus norvegicus 112-123 3379048-0 1988 Uptake of iron from transferrin by isolated rat hepatocytes. Iron 10-14 transferrin Rattus norvegicus 20-31 3379048-2 1988 The uptake of iron from transferrin by isolated rat hepatocytes varies in parallel with plasma membrane NADH:ferricyanide oxidoreductase activity, is inhibited by ferricyanide, ferric, and ferrous iron chelators, divalent transition metal cations, and depends on calcium ions. Iron 14-18 transferrin Rattus norvegicus 24-35 3379048-2 1988 The uptake of iron from transferrin by isolated rat hepatocytes varies in parallel with plasma membrane NADH:ferricyanide oxidoreductase activity, is inhibited by ferricyanide, ferric, and ferrous iron chelators, divalent transition metal cations, and depends on calcium ions. Iron 197-201 transferrin Rattus norvegicus 24-35 3379048-4 1988 The results are compatible with a model in which iron, at transferrin concentrations above that needed to saturate the transferrin receptor, is taken up from transferrin predominantly by mechanisms located to or contiguous with the plasma membrane. Iron 49-53 transferrin Rattus norvegicus 58-69 3379048-4 1988 The results are compatible with a model in which iron, at transferrin concentrations above that needed to saturate the transferrin receptor, is taken up from transferrin predominantly by mechanisms located to or contiguous with the plasma membrane. Iron 49-53 transferrin Rattus norvegicus 119-130 3379048-5 1988 The process involves labilization and reduction of transferrin-bound iron by cooperative proton and electron fluxes. Iron 69-73 transferrin Rattus norvegicus 51-62 3408780-6 1988 Iron-saturated (holo-) transferrin was a more potent stimulator of rat placental cell DNA synthesis than was iron-free (apo-) transferrin. Iron 0-4 transferrin Rattus norvegicus 23-34 3401541-2 1988 Double-labeled [( 59Fe125I]) transferrin has been used to study the fate of transferrin and iron. Iron 92-96 transferrin Rattus norvegicus 29-40 3180141-4 1988 Malignant cells requiring more iron modulate a transferrin receptor and the iron transporting protein transferrin delivers iron to the cell. Iron 31-35 transferrin Rattus norvegicus 47-58 3338996-0 1988 Non-transferrin-bound iron uptake by rat liver. Iron 22-26 transferrin Rattus norvegicus 4-15 3338996-2 1988 Non-transferrin-bound iron is efficiently cleared from serum by the liver and may be primarily responsible for the hepatic damage seen in iron-overload states. Iron 22-26 transferrin Rattus norvegicus 4-15 3338996-2 1988 Non-transferrin-bound iron is efficiently cleared from serum by the liver and may be primarily responsible for the hepatic damage seen in iron-overload states. Iron 138-142 transferrin Rattus norvegicus 4-15 3338996-12 1988 These findings are consistent with an electrogenic transport mechanism for uptake of non-transferrin-bound iron that is driven by the transmembrane potential difference. Iron 107-111 transferrin Rattus norvegicus 89-100 3337844-6 1988 (3) In the presence of apotransferrin in the culture medium, part of the iron was found as transferrin iron. Iron 73-77 transferrin Rattus norvegicus 26-37 3337844-6 1988 (3) In the presence of apotransferrin in the culture medium, part of the iron was found as transferrin iron. Iron 103-107 transferrin Rattus norvegicus 26-37 3291685-2 1988 Iron and the iron-binding proteins can act as regulators of immune function, and not only as a result of a nutritional dependence of lymphoid cells on transferrin and transferrin-iron. Iron 0-4 transferrin Rattus norvegicus 151-162 3291685-2 1988 Iron and the iron-binding proteins can act as regulators of immune function, and not only as a result of a nutritional dependence of lymphoid cells on transferrin and transferrin-iron. Iron 0-4 transferrin Rattus norvegicus 167-178 3291685-2 1988 Iron and the iron-binding proteins can act as regulators of immune function, and not only as a result of a nutritional dependence of lymphoid cells on transferrin and transferrin-iron. Iron 13-17 transferrin Rattus norvegicus 151-162 3291685-2 1988 Iron and the iron-binding proteins can act as regulators of immune function, and not only as a result of a nutritional dependence of lymphoid cells on transferrin and transferrin-iron. Iron 13-17 transferrin Rattus norvegicus 167-178 3291685-2 1988 Iron and the iron-binding proteins can act as regulators of immune function, and not only as a result of a nutritional dependence of lymphoid cells on transferrin and transferrin-iron. Iron 179-183 transferrin Rattus norvegicus 167-178 3291685-15 1988 Transient increases in serum iron concentration above the full saturation of transferrin, reproducing the clinical situation frequently seen in hereditary hemochromatosis, are followed by a series of cellular changes in the synovium that can be correlated to changes in the course of an experimental model of arthritis in the rat. Iron 29-33 transferrin Rattus norvegicus 77-88 3422446-2 1988 Plasma transferrin receptors were measured by ELISA in rats of different age and sex, of different iron status, with different degrees of erythropoiesis, and with inflammation. Iron 99-103 transferrin Rattus norvegicus 7-18 3053498-8 1988 The Sertoli cells have developed a system to move serum-derived iron through their own cytoplasm and to secrete it bound to newly synthesized testicular transferrin molecules which can deliver it to specific receptors on the germinal cell surface (Huggenvik et al., 1984). Iron 64-68 transferrin Rattus norvegicus 153-164 3433005-7 1987 The results are consistent with receptor-mediated endocytosis as one mechanism for hepatocyte uptake of iron from transferrin but also suggest an alternative route by which transferrin can donate its iron to the cells and rapidly be released to the extracellular environment without undergoing a complete transferrin cycle. Iron 104-108 transferrin Rattus norvegicus 114-125 3452592-0 1987 Mobilization of iron from serum transferrin following lead acetate administration in rats. Iron 16-20 transferrin Rattus norvegicus 32-43 3680232-11 1987 Because the transmembrane electron transport has been shown to stimulate cell growth, the reduction of diferric transferrin at the cell surface may be an important function for diferric transferrin in stimulation of cell growth, in addition to its role in iron transport. Iron 256-260 transferrin Rattus norvegicus 112-123 3429053-0 1987 Transport of transferrin-bound iron into rat Sertoli cells and spermatids. Iron 31-35 transferrin Rattus norvegicus 13-24 3429053-1 1987 Transferrin (Tf), a major secretory protein of Sertoli cells, may transport iron to spermatogenic cells. Iron 76-80 transferrin Rattus norvegicus 0-11 3429053-1 1987 Transferrin (Tf), a major secretory protein of Sertoli cells, may transport iron to spermatogenic cells. Iron 76-80 transferrin Rattus norvegicus 13-15 3429053-2 1987 This was assessed by measuring the uptake of Fe from 59Fe-125I-labelled rat Tf by Sertoli cells and round spermatids in vitro. Iron 45-47 transferrin Rattus norvegicus 76-78 3429053-3 1987 Uptake of Fe from labelled Tf by Sertoli cells after a 72-h pre-incubation period was linear for 20 h (approximately 18 pmol/10(6) cells/20 h), whereas the uptake of Fe from labelled Tf by round spermatids after a 16-h pre-incubation period reached a plateau by 2 h (approximately 5 pmol/10(6) cells/2 h). Iron 10-12 transferrin Rattus norvegicus 27-29 3429053-3 1987 Uptake of Fe from labelled Tf by Sertoli cells after a 72-h pre-incubation period was linear for 20 h (approximately 18 pmol/10(6) cells/20 h), whereas the uptake of Fe from labelled Tf by round spermatids after a 16-h pre-incubation period reached a plateau by 2 h (approximately 5 pmol/10(6) cells/2 h). Iron 166-168 transferrin Rattus norvegicus 183-185 3429053-8 1987 It is concluded that iron from exogenous Tf is transported into Sertoli cells and round spermatids in vitro, and is complexed to intracellular ferritin. Iron 21-25 transferrin Rattus norvegicus 41-43 3433005-0 1987 Uptake of iron from transferrin by isolated hepatocytes. Iron 10-14 transferrin Rattus norvegicus 20-31 3433005-2 1987 The subcellular distribution of iron and transferrin has been studied in isolated rat hepatocytes during uptake of transferrin iron. Iron 32-36 transferrin Rattus norvegicus 115-126 3433005-2 1987 The subcellular distribution of iron and transferrin has been studied in isolated rat hepatocytes during uptake of transferrin iron. Iron 127-131 transferrin Rattus norvegicus 115-126 3433005-3 1987 Iron and transferrin are both rapidly transferred from an extracellular to an intracellular compartment in a process which is slowed down when the cells are deprived of ATP and completely blocked when the cells are incubated at 4 degrees C. The transfer of iron occurs at a higher rate than transferrin. Iron 0-4 transferrin Rattus norvegicus 291-302 3433005-7 1987 The results are consistent with receptor-mediated endocytosis as one mechanism for hepatocyte uptake of iron from transferrin but also suggest an alternative route by which transferrin can donate its iron to the cells and rapidly be released to the extracellular environment without undergoing a complete transferrin cycle. Iron 200-204 transferrin Rattus norvegicus 173-184 3433005-3 1987 Iron and transferrin are both rapidly transferred from an extracellular to an intracellular compartment in a process which is slowed down when the cells are deprived of ATP and completely blocked when the cells are incubated at 4 degrees C. The transfer of iron occurs at a higher rate than transferrin. Iron 257-261 transferrin Rattus norvegicus 9-20 3433005-3 1987 Iron and transferrin are both rapidly transferred from an extracellular to an intracellular compartment in a process which is slowed down when the cells are deprived of ATP and completely blocked when the cells are incubated at 4 degrees C. The transfer of iron occurs at a higher rate than transferrin. Iron 257-261 transferrin Rattus norvegicus 291-302 3433005-7 1987 The results are consistent with receptor-mediated endocytosis as one mechanism for hepatocyte uptake of iron from transferrin but also suggest an alternative route by which transferrin can donate its iron to the cells and rapidly be released to the extracellular environment without undergoing a complete transferrin cycle. Iron 200-204 transferrin Rattus norvegicus 173-184 3689862-9 1987 Thus, our results demonstrated a unidirectional system of iron transport from the basal compartment of the seminiferous epithelium to the germ cells in the adluminal compartment involving two distinct transferrins, i.e., a serum transferrin and a testicular transferrin synthesized by the seminiferous epithelium. Iron 58-62 transferrin Rattus norvegicus 201-212 3312497-1 1987 Transferrin (Tf), the iron mobilization protein, is synthesized mainly in the liver. Iron 22-26 transferrin Rattus norvegicus 0-11 3312497-1 1987 Transferrin (Tf), the iron mobilization protein, is synthesized mainly in the liver. Iron 22-26 transferrin Rattus norvegicus 13-15 3312497-7 1987 Regional variation in the amount of Tf was in general agreement with published reports on the variation of iron and Tf receptor levels in the CNS. Iron 107-111 transferrin Rattus norvegicus 36-38 3125486-4 1987 Iron absorption from 59Fe-labelled transferrin was inhibited by the addition of rat plasma. Iron 0-4 transferrin Rattus norvegicus 35-46 3689862-9 1987 Thus, our results demonstrated a unidirectional system of iron transport from the basal compartment of the seminiferous epithelium to the germ cells in the adluminal compartment involving two distinct transferrins, i.e., a serum transferrin and a testicular transferrin synthesized by the seminiferous epithelium. Iron 58-62 transferrin Rattus norvegicus 229-240 3578500-7 1987 The mechanism involved was further investigated by studying the effect of the chelators on uptake of transferrin-bound iron by placental cells in culture. Iron 119-123 transferrin Rattus norvegicus 101-112 3593971-1 1987 The mechanisms underlying the impaired utilization of transferrin-bound iron by erythroid cells in the anemia of the Belgrade laboratory rat were investigated using reticulocytes from homozygous anemic animals and transferrin labeled with 59Fe and 125I. Iron 72-76 transferrin Rattus norvegicus 54-65 3305046-5 1987 A lipophilic iron chelator, ferric pyridoxal isonicotinoyl hydrazone (FePIH), can fully mimic the effect of transferrin on the proliferation of WB-F344 cells, but the molar concentration of transferrin. Iron 13-17 transferrin Rattus norvegicus 108-119 3305046-5 1987 A lipophilic iron chelator, ferric pyridoxal isonicotinoyl hydrazone (FePIH), can fully mimic the effect of transferrin on the proliferation of WB-F344 cells, but the molar concentration of transferrin. Iron 13-17 transferrin Rattus norvegicus 190-201 3305046-6 1987 These results suggest that the critical function of transferrin in the proliferation of WB-F344 cells may be in the delivery of iron to the cells. Iron 128-132 transferrin Rattus norvegicus 52-63 3619079-3 1987 The presence of large amounts of ferritin in the cytoplasm of these cells suggests that they receive iron, presumably from circulating transferrin. Iron 101-105 transferrin Rattus norvegicus 135-146 3619079-8 1987 It is postulated that the iron responsible for enamel pigmentation is transported by transferrin to maturation ameloblasts and is bound to specific transferrin receptors found mostly on RAs and that the modulation of these cells into SAs results in a loss of most of these receptors. Iron 26-30 transferrin Rattus norvegicus 85-96 3619079-8 1987 It is postulated that the iron responsible for enamel pigmentation is transported by transferrin to maturation ameloblasts and is bound to specific transferrin receptors found mostly on RAs and that the modulation of these cells into SAs results in a loss of most of these receptors. Iron 26-30 transferrin Rattus norvegicus 148-159 3578091-4 1987 A greater reduction in iron absorption occurred in iron-deficient rats when transferrin iron was injected into gut loops. Iron 23-27 transferrin Rattus norvegicus 76-87 3578091-4 1987 A greater reduction in iron absorption occurred in iron-deficient rats when transferrin iron was injected into gut loops. Iron 51-55 transferrin Rattus norvegicus 76-87 3578091-4 1987 A greater reduction in iron absorption occurred in iron-deficient rats when transferrin iron was injected into gut loops. Iron 51-55 transferrin Rattus norvegicus 76-87 3578500-10 1987 The results can be explained if the iron is released from the transferrin in intracellular vesicles in the ferrous form, where it may be chelated by bipyridine and prevented from passing to the fetus or converted to the ferric form once it is inside the cell matrix. Iron 36-40 transferrin Rattus norvegicus 62-73 3578091-5 1987 Mucosal radioiron content in animals given cadmium with either iron salts or transferrin iron was increased. Iron 13-17 transferrin Rattus norvegicus 77-88 3578091-6 1987 The primary effect of cadmium was on intracellular processing of iron salts and transferrin iron. Iron 92-96 transferrin Rattus norvegicus 80-91 3539227-7 1987 These findings support the concept that the hepatocyte has a central role in the uptake and storage of transferrin iron. Iron 115-119 transferrin Rattus norvegicus 103-114 2440461-0 1987 Biological effect of transferrin on mast cell mediator release during the passive cutaneous anaphylaxis reaction: a possible inhibition mechanism involving iron. Iron 156-160 transferrin Rattus norvegicus 21-32 2440461-6 1987 Iron and iron-saturated transferrin could play a role in the mechanism of desensitization by modulating the responsiveness of mast cells. Iron 9-13 transferrin Rattus norvegicus 24-35 2437773-0 1987 Inhibition of histamine release in vitro by a blocking factor from human serum: comparison with the iron binding proteins transferrin and lactoferrin. Iron 100-104 transferrin Rattus norvegicus 122-133 2437773-5 1987 BF (DEAE-peak 1) and the iron binding proteins transferrin and lactoferrin (LF) are shown to inhibit the histamine release in vitro. Iron 25-29 transferrin Rattus norvegicus 47-58 2444207-5 1987 In all three cell types iron delivery occurs, as concluded from the increase in cellular 59Fe/125I ratio at prolonged circulation times of transferrin. Iron 24-28 transferrin Rattus norvegicus 139-150 3697729-1 1986 Recent studies have demonstrated receptors in the nervous system for transferrin, the iron binding and transport protein in the blood. Iron 86-90 transferrin Rattus norvegicus 69-80 3828435-3 1986 Iron-saturated and iron-free (apo-) transferrin use the same binding sites on the surface of the tubules, but the dissociation constant is about two times higher for apotransferrin than for iron-saturated transferrin. Iron 0-4 transferrin Rattus norvegicus 36-47 3828435-3 1986 Iron-saturated and iron-free (apo-) transferrin use the same binding sites on the surface of the tubules, but the dissociation constant is about two times higher for apotransferrin than for iron-saturated transferrin. Iron 0-4 transferrin Rattus norvegicus 169-180 3828435-3 1986 Iron-saturated and iron-free (apo-) transferrin use the same binding sites on the surface of the tubules, but the dissociation constant is about two times higher for apotransferrin than for iron-saturated transferrin. Iron 19-23 transferrin Rattus norvegicus 36-47 3828435-3 1986 Iron-saturated and iron-free (apo-) transferrin use the same binding sites on the surface of the tubules, but the dissociation constant is about two times higher for apotransferrin than for iron-saturated transferrin. Iron 19-23 transferrin Rattus norvegicus 169-180 3828435-3 1986 Iron-saturated and iron-free (apo-) transferrin use the same binding sites on the surface of the tubules, but the dissociation constant is about two times higher for apotransferrin than for iron-saturated transferrin. Iron 190-194 transferrin Rattus norvegicus 36-47 3828435-3 1986 Iron-saturated and iron-free (apo-) transferrin use the same binding sites on the surface of the tubules, but the dissociation constant is about two times higher for apotransferrin than for iron-saturated transferrin. Iron 190-194 transferrin Rattus norvegicus 169-180 3779112-9 1986 As iron transfer cumulated linearly while transferrin release cumulated in an asymptotic manner, the capacity of transferrin to bind iron ions is exceeded roughly 100 times by molar equivalents of iron in the last absorbate fractions. Iron 3-7 transferrin Rattus norvegicus 113-124 3779112-9 1986 As iron transfer cumulated linearly while transferrin release cumulated in an asymptotic manner, the capacity of transferrin to bind iron ions is exceeded roughly 100 times by molar equivalents of iron in the last absorbate fractions. Iron 133-137 transferrin Rattus norvegicus 42-53 3779112-9 1986 As iron transfer cumulated linearly while transferrin release cumulated in an asymptotic manner, the capacity of transferrin to bind iron ions is exceeded roughly 100 times by molar equivalents of iron in the last absorbate fractions. Iron 133-137 transferrin Rattus norvegicus 113-124 3779112-9 1986 As iron transfer cumulated linearly while transferrin release cumulated in an asymptotic manner, the capacity of transferrin to bind iron ions is exceeded roughly 100 times by molar equivalents of iron in the last absorbate fractions. Iron 133-137 transferrin Rattus norvegicus 42-53 3779112-9 1986 As iron transfer cumulated linearly while transferrin release cumulated in an asymptotic manner, the capacity of transferrin to bind iron ions is exceeded roughly 100 times by molar equivalents of iron in the last absorbate fractions. Iron 133-137 transferrin Rattus norvegicus 113-124 3019155-2 1986 In experiments lasting 60-90 min, rat asialotransferrin delivered a three to four times larger fraction of the Fe dose to the liver than rat transferrin. Iron 111-113 transferrin Rattus norvegicus 44-55 3019155-5 1986 In all cases, rat asialotransferrin delivered Fe to the liver at rates comparable with those seen with rat transferrin. Iron 46-48 transferrin Rattus norvegicus 24-35 3019155-7 1986 These findings suggest that the enhanced hepatic uptake of Fe from rat asialotransferrin is mediated by simultaneous binding of the ligand both through its glycan and transferrin receptor affinity site. Iron 59-61 transferrin Rattus norvegicus 77-88 3019155-9 1986 The data suggest that deposition of a significant fraction of Fe in rat liver from rat transferrin is likely to take place by a mechanism not involving transferrin receptors. Iron 62-64 transferrin Rattus norvegicus 87-98 3758939-7 1986 Chase experiments showed that the internalized transferrin donated all of its iron to the cell and was then released in a biphasic manner which was dependent on the time of preincubation with radiolabeled transferrin. Iron 78-82 transferrin Rattus norvegicus 47-58 3758939-11 1986 The second process is nonsaturable up to a transferrin concentration of at least 6 microM but like the specific process, also leads to accumulation of iron in excess of transferrin. Iron 151-155 transferrin Rattus norvegicus 43-54 3733737-9 1986 Because clearance is highly efficient, increased levels of non-transferrin-bound iron in plasma may present the liver with an obligatory iron load resulting in progressive accumulation and toxicity. Iron 137-141 transferrin Rattus norvegicus 63-74 3800875-8 1986 When livers were perfused with various concentrations of transferrin the total uptakes of both iron and transferrin and incorporation into their subcellular fractions were curvilinear, increasing with transferrin concentrations up to at least 10 microM. Iron 95-99 transferrin Rattus norvegicus 57-68 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 53-57 transferrin Rattus norvegicus 35-46 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 53-57 transferrin Rattus norvegicus 134-145 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 53-57 transferrin Rattus norvegicus 134-145 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 53-57 transferrin Rattus norvegicus 134-145 3459151-4 1986 This increase in transferrin gene expression resulted in a corresponding increase in serum total-iron-binding capacity. Iron 97-101 transferrin Rattus norvegicus 17-28 3459151-7 1986 The small intestine had no detectable transferrin mRNA in either normal or iron-deficient rats; however, transferrin protein was present, and its level was 2-fold higher in the iron-deficient group. Iron 177-181 transferrin Rattus norvegicus 105-116 3573080-1 1987 Transferrin is the second most abundant plasma protein and functions to transport iron. Iron 82-86 transferrin Rattus norvegicus 0-11 3694713-3 1987 The receptor-mediated movement of transferrin across the blood-brain barrier suggests that the brain may derive its iron through the transcytosis of iron-loaded transferrin across the brain microvasculature. Iron 116-120 transferrin Rattus norvegicus 34-45 3694713-3 1987 The receptor-mediated movement of transferrin across the blood-brain barrier suggests that the brain may derive its iron through the transcytosis of iron-loaded transferrin across the brain microvasculature. Iron 116-120 transferrin Rattus norvegicus 161-172 3694713-3 1987 The receptor-mediated movement of transferrin across the blood-brain barrier suggests that the brain may derive its iron through the transcytosis of iron-loaded transferrin across the brain microvasculature. Iron 149-153 transferrin Rattus norvegicus 34-45 3694713-3 1987 The receptor-mediated movement of transferrin across the blood-brain barrier suggests that the brain may derive its iron through the transcytosis of iron-loaded transferrin across the brain microvasculature. Iron 149-153 transferrin Rattus norvegicus 161-172 3733737-0 1986 Characterization of non-transferrin-bound iron clearance by rat liver. Iron 42-46 transferrin Rattus norvegicus 24-35 3733737-1 1986 Recent evidence suggests that the hepatic iron-loading characteristic of hemochromatosis may result in part from efficient hepatic clearance of non-transferrin-bound iron, which is increased in this disorder. Iron 42-46 transferrin Rattus norvegicus 148-159 3733737-1 1986 Recent evidence suggests that the hepatic iron-loading characteristic of hemochromatosis may result in part from efficient hepatic clearance of non-transferrin-bound iron, which is increased in this disorder. Iron 166-170 transferrin Rattus norvegicus 148-159 3733737-3 1986 We therefore studied hepatic uptake of non-transferrin-bound iron in the single-pass perfused rat liver under varying conditions. Iron 61-65 transferrin Rattus norvegicus 43-54 3733737-9 1986 Because clearance is highly efficient, increased levels of non-transferrin-bound iron in plasma may present the liver with an obligatory iron load resulting in progressive accumulation and toxicity. Iron 81-85 transferrin Rattus norvegicus 63-74 3530028-0 1986 Depression of iron uptake from transferrin by isolated hepatocytes in the presence of ethanol is a pH-dependent consequence of ethanol metabolism. Iron 14-18 transferrin Rattus norvegicus 31-42 3530028-1 1986 Incubation of freshly isolated rat hepatocytes with highly purified radiolabeled rat transferrin in weakly buffered medium in the presence of 10 mM ethanol resulted in a marked diminution of iron uptake by these cells, associated with a greater pH depression than in ethanol-free control studies. Iron 191-195 transferrin Rattus norvegicus 85-96 3530028-2 1986 This effect on iron uptake persisted, even when the cells were preincubated for 90 min with ethanol before the addition of transferrin. Iron 15-19 transferrin Rattus norvegicus 123-134 3530028-7 1986 It is suggested that, in the light of current understanding of transferrin recycling by other cell types, the disturbances of iron homeostasis observed in alcoholics can be partially accounted for by alterations in their acid-base metabolism. Iron 126-130 transferrin Rattus norvegicus 63-74 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 35-46 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 134-145 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 134-145 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 134-145 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 35-46 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 134-145 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 134-145 3800875-15 1986 It is concluded that the uptake of transferrin-bound iron by the liver of the rat results from endocytosis by hepatocytes of the iron-transferrin complex into low-density vesicles followed by release of iron from the transferrin and recycling of the transferrin to the extracellular medium. Iron 129-133 transferrin Rattus norvegicus 134-145 3459151-2 1986 We quantitated transferrin mRNA in a variety of tissues from normal and iron-deficient rats and found that the level of transferrin mRNA in normal rat liver was about 6500 molecules per cell, while the level in iron-deficient animals was 2.4-fold higher. Iron 72-76 transferrin Rattus norvegicus 120-131 3459151-2 1986 We quantitated transferrin mRNA in a variety of tissues from normal and iron-deficient rats and found that the level of transferrin mRNA in normal rat liver was about 6500 molecules per cell, while the level in iron-deficient animals was 2.4-fold higher. Iron 211-215 transferrin Rattus norvegicus 120-131 3755593-3 1986 It has the ability to catalyse the oxidative incorporation of iron into transferrin at very low Fe2+ and O2 concentrations. Iron 62-66 transferrin Rattus norvegicus 72-83 3715363-0 1986 Uptake of iron from transferrin by isolated hepatocytes. Iron 10-14 transferrin Rattus norvegicus 20-31 3715363-2 1986 The mechanism by which utilization of transferrin-bound iron is linked with cellular metabolism has been studied in isolated rat hepatocytes. Iron 56-60 transferrin Rattus norvegicus 38-49 3697729-9 1986 The presence of Tf in oligodendrocytes implies that these neuroglia are involved in iron mobilization and storage in the CNS. Iron 84-88 transferrin Rattus norvegicus 16-18 3697729-10 1986 Stored quantities of iron and the ability to mobilize the iron through stored transferrin may be the reason for the extreme dietary restrictions necessary to induce iron-deficient CNS disorders. Iron 21-25 transferrin Rattus norvegicus 78-89 3697729-10 1986 Stored quantities of iron and the ability to mobilize the iron through stored transferrin may be the reason for the extreme dietary restrictions necessary to induce iron-deficient CNS disorders. Iron 58-62 transferrin Rattus norvegicus 78-89 3738220-2 1986 In the plasma as well as in the bile there is a decrease of iron and an increase of transferrin due to iron depletion, whereas the albumin level remains constant. Iron 103-107 transferrin Rattus norvegicus 84-95 3081063-7 1986 Reticulocyte incubation studies demonstrated an unimpaired uptake of the transferrin-iron-receptor complex but a marked reduction in iron accumulation. Iron 85-89 transferrin Rattus norvegicus 73-84 3081063-8 1986 The diferric transferrin molecule, when it did give up iron within the cell, released both of its iron atoms so that only apotransferrin was returned to the media. Iron 55-59 transferrin Rattus norvegicus 13-24 3081063-8 1986 The diferric transferrin molecule, when it did give up iron within the cell, released both of its iron atoms so that only apotransferrin was returned to the media. Iron 98-102 transferrin Rattus norvegicus 13-24 3948880-11 1986 On the basis of our results we suggest that, at low extracellular transferrin concentration, iron uptake by the liver involves endocytosis of the transferrin protein. Iron 93-97 transferrin Rattus norvegicus 66-77 3948880-11 1986 On the basis of our results we suggest that, at low extracellular transferrin concentration, iron uptake by the liver involves endocytosis of the transferrin protein. Iron 93-97 transferrin Rattus norvegicus 146-157 3948880-14 1986 The iron-depleted transferrin molecule would then be returned to the extracellular medium during the recycling of the plasma membrane. Iron 4-8 transferrin Rattus norvegicus 18-29 3947549-0 1986 Interaction of transferrin with iron-loaded rat peritoneal macrophages. Iron 32-36 transferrin Rattus norvegicus 15-26 3942693-0 1986 Fluorescence probe measurement of the pH of the transferrin microenvironment during iron uptake by rat bone marrow erythroid cells. Iron 68-72 transferrin Rattus norvegicus 48-59 3942693-1 1986 Fluorescence probe measurements of the transferrin micro-environment during iron uptake by rat erythroid cells revealed that part of the transferrin is taken up in an acidic environment. Iron 60-64 transferrin Rattus norvegicus 39-50 3942693-1 1986 Fluorescence probe measurements of the transferrin micro-environment during iron uptake by rat erythroid cells revealed that part of the transferrin is taken up in an acidic environment. Iron 60-64 transferrin Rattus norvegicus 137-148 4020242-2 1985 Radioactive iron uptake per 2 X 10(6) cells/24 hr was 3.8% for 59Fe-transferrin, 15.8% for 59Fe-ferric ammonium citrate (FeAC) at 20 micrograms Fe/ml in 20% serum, and 37.1% for 59FeAC at 20 micrograms Fe/ml in serum-free medium. Iron 12-16 transferrin Rattus norvegicus 68-79 4091824-3 1985 Iron entering the cells on transferrin was subsequently found in a number of intracellular components: transferrin, haem, ferritin and a residual fraction. Iron 0-4 transferrin Rattus norvegicus 27-38 4091824-3 1985 Iron entering the cells on transferrin was subsequently found in a number of intracellular components: transferrin, haem, ferritin and a residual fraction. Iron 0-4 transferrin Rattus norvegicus 103-114 4091824-4 1985 After 2 h incubation with 59Fe-transferrin almost 70% of the iron was in ferritin, and this proportion increased to 80% during a "chase" experiment. Iron 61-65 transferrin Rattus norvegicus 31-42 4063390-5 1985 Previously we had shown that iron uptake into cells and onto cellular transferrin was virtually the same throughout the small intestine, irrespective of the iron-absorbing capacity of the region. Iron 29-33 transferrin Rattus norvegicus 70-81 4063390-6 1985 The results of this study therefore suggest that iron absorption depends on an intact cytoskeletal system and that ferritin in the iron-absorbing cell is able to load from the pool of iron committed to transcellular movement onto plasma transferrin. Iron 131-135 transferrin Rattus norvegicus 237-248 4063390-6 1985 The results of this study therefore suggest that iron absorption depends on an intact cytoskeletal system and that ferritin in the iron-absorbing cell is able to load from the pool of iron committed to transcellular movement onto plasma transferrin. Iron 131-135 transferrin Rattus norvegicus 237-248 2996611-2 1985 Isolated rat liver mitochondria accumulate iron from fully saturated transferrin at neutral pH. Iron 43-47 transferrin Rattus norvegicus 69-80 2996611-3 1985 With 5 microM iron as diferric transferrin, accumulation at 30 degrees C amounts to approx. Iron 14-18 transferrin Rattus norvegicus 31-42 2996611-6 1985 Vacant iron-binding sites on mono- and apotransferrin compete with the mitochondria for iron mobilized from transferrin. Iron 7-11 transferrin Rattus norvegicus 42-53 2996611-6 1985 Vacant iron-binding sites on mono- and apotransferrin compete with the mitochondria for iron mobilized from transferrin. Iron 88-92 transferrin Rattus norvegicus 42-53 4044661-1 1985 The mechanism of iron uptake from transferrin by the rat placenta in culture has been studied. Iron 17-21 transferrin Rattus norvegicus 34-45 4044661-2 1985 Transferrin endocytosis preceded iron accumulation by the cells. Iron 33-37 transferrin Rattus norvegicus 0-11 4044661-4 1985 Transferrin endocytosis was less susceptible to the effects of metabolic inhibitors such as sodium fluoroacetate, potassium cyanide, 2,4, dinitrophenol or carbonylcyanide M-chlorophenyl hydrazone (CCCP) than was iron uptake. Iron 212-216 transferrin Rattus norvegicus 0-11 4044661-6 1985 These results suggest that, following internalisation, the vesicles containing the transferrin and iron became acidified, and that this acidification was a necessary prerequisite for the accumulation of iron by the cell. Iron 203-207 transferrin Rattus norvegicus 83-94 4044661-8 1985 The importance of the permeability properties of the vesicle membrane in the iron uptake process was investigated by incubating the cells with labelled transferrin and iron in the presence of different cation and anion ionophores. Iron 77-81 transferrin Rattus norvegicus 152-163 4084303-1 1985 Short-term alterations in the amount of iron in the diets of rats caused substantial differences in the distribution of a test dose of radioiron between mucosal transferrin and mucosal ferritin, and also caused a change in the relative amounts of these two proteins in mucosal tissue without resulting in any detectable change in liver iron stores. Iron 40-44 transferrin Rattus norvegicus 161-172 4084303-1 1985 Short-term alterations in the amount of iron in the diets of rats caused substantial differences in the distribution of a test dose of radioiron between mucosal transferrin and mucosal ferritin, and also caused a change in the relative amounts of these two proteins in mucosal tissue without resulting in any detectable change in liver iron stores. Iron 140-144 transferrin Rattus norvegicus 161-172 3877057-10 1985 The ability of rough microsomal transferrin to bind and deliver iron through interaction with transferrin receptors on reticulocytes suggests that considerable tertiary structure is present. Iron 64-68 transferrin Rattus norvegicus 32-43 3877057-10 1985 The ability of rough microsomal transferrin to bind and deliver iron through interaction with transferrin receptors on reticulocytes suggests that considerable tertiary structure is present. Iron 64-68 transferrin Rattus norvegicus 94-105 4056038-0 1985 Efficient clearance of non-transferrin-bound iron by rat liver. Iron 45-49 transferrin Rattus norvegicus 27-38 4056038-10 1985 These findings suggest that high levels of non-transferrin-bound iron in plasma may be an important cause of hepatic iron loading in iron overload states. Iron 65-69 transferrin Rattus norvegicus 47-58 4056038-10 1985 These findings suggest that high levels of non-transferrin-bound iron in plasma may be an important cause of hepatic iron loading in iron overload states. Iron 117-121 transferrin Rattus norvegicus 47-58 4056038-10 1985 These findings suggest that high levels of non-transferrin-bound iron in plasma may be an important cause of hepatic iron loading in iron overload states. Iron 117-121 transferrin Rattus norvegicus 47-58 4020242-2 1985 Radioactive iron uptake per 2 X 10(6) cells/24 hr was 3.8% for 59Fe-transferrin, 15.8% for 59Fe-ferric ammonium citrate (FeAC) at 20 micrograms Fe/ml in 20% serum, and 37.1% for 59FeAC at 20 micrograms Fe/ml in serum-free medium. Iron 65-67 transferrin Rattus norvegicus 68-79 3968194-6 1985 Only this internalized transferrin was capable of donating iron to the cells. Iron 59-63 transferrin Rattus norvegicus 23-34 2863261-9 1985 These results indicated that iron was removed from transferrin at an intracellular site in an acidic environment. Iron 29-33 transferrin Rattus norvegicus 51-62 2989832-0 1985 Transferrin receptors in rat brain: neuropeptide-like pattern and relationship to iron distribution. Iron 82-86 transferrin Rattus norvegicus 0-11 2989832-5 1985 Iron-rich brain areas generally receive neuronal projections from areas with abundant transferrin receptors, suggesting that iron may be transported neuronally. Iron 0-4 transferrin Rattus norvegicus 86-97 2989832-5 1985 Iron-rich brain areas generally receive neuronal projections from areas with abundant transferrin receptors, suggesting that iron may be transported neuronally. Iron 125-129 transferrin Rattus norvegicus 86-97 2993056-7 1985 Iron is accumulated via both receptor systems in the heterologous system, but only via the transferrin receptors in the homologous system. Iron 0-4 transferrin Rattus norvegicus 91-102 3966565-4 1985 These results suggest that at least part of iron uptake by hepatocytes is mediated by the reversible binding of transferrin in a manner comparable with erythroid cells and placenta. Iron 44-48 transferrin Rattus norvegicus 112-123 3971047-4 1985 The tumor promoters phorbol 12-myristate 13-acetate (PMA) and phorbol 12,13-dibutyrate (PDB) were shown to increase the rates of iron and transferrin uptake by reticulocytes and fetal liver erythroid cells by accelerating the rates of transferrin endocytosis and exocytosis. Iron 129-133 transferrin Rattus norvegicus 235-246 6487660-1 1984 The inhibitory effect of heme on iron uptake from transferrin by rat and rabbit reticulocytes and erythroid cells from the fetal rat liver was studied in vitro. Iron 33-37 transferrin Rattus norvegicus 50-61 4086199-3 1985 A separation of the albumin- and transferrin-proteins by ion-exchange chromatography using DEAE-cellulose showed the 239Np being entirely bound to the iron-carrier protein transferrin. Iron 151-155 transferrin Rattus norvegicus 33-44 4086199-3 1985 A separation of the albumin- and transferrin-proteins by ion-exchange chromatography using DEAE-cellulose showed the 239Np being entirely bound to the iron-carrier protein transferrin. Iron 151-155 transferrin Rattus norvegicus 172-183 4086199-5 1985 The binding capacity of transferrin for neptunium in vivo was found to decline when the iron level in blood serum was increased. Iron 88-92 transferrin Rattus norvegicus 24-35 6517927-0 1984 Iron uptake from transferrin by isolated hepatocytes: effect of ethanol. Iron 0-4 transferrin Rattus norvegicus 17-28 6517927-3 1984 These data are compatible with the hypothesis that iron uptake from transferrin by hepatocytes is mediated by a pH dependent transferrin receptor mechanism similar to that in reticulocytes. Iron 51-55 transferrin Rattus norvegicus 68-79 6517927-3 1984 These data are compatible with the hypothesis that iron uptake from transferrin by hepatocytes is mediated by a pH dependent transferrin receptor mechanism similar to that in reticulocytes. Iron 51-55 transferrin Rattus norvegicus 125-136 6095085-5 1984 It is possible that transferrin receptors are expressed on these cells to allow transport of transferrin (and thus iron) into brain tissues. Iron 115-119 transferrin Rattus norvegicus 20-31 6487660-2 1984 Addition of hemin was shown to cause a decrease in the rate of transferrin endocytosis, the degree of inhibition being proportional to the reduction in iron uptake. Iron 152-156 transferrin Rattus norvegicus 63-74 6487660-4 1984 It is concluded from these results that heme affects iron uptake by influencing the rate of transferrin endocytosis and recycling. Iron 53-57 transferrin Rattus norvegicus 92-103 6478224-6 1984 Muscles denervated for 7 days and injected daily with 1 of several doses of iron-conjugated rat transferrin exhibited a rate of atrophy equivalent to that in denervated muscles that either were not treated or were injected with saline. Iron 76-80 transferrin Rattus norvegicus 96-107 6592293-2 1984 The results indicate that: (a) the liver can take up Ga-67 and secrete it into the bile, even in the absence of transferrin; (b) transferrin inhibits hepatic uptake of Ga-67 and its biliary excretion; and (c) iron deficiency markedly enhances hepatic uptake of Ga-67. Iron 209-213 transferrin Rattus norvegicus 129-140 6088313-1 1984 Transferrin receptor in hepatocytes was studied by iron-saturated[125I]transferrin binding. Iron 51-55 transferrin Rattus norvegicus 0-11 6377946-6 1984 We suggest that the increased capacity of transferrin deficient in sialic acid to selectively deposit iron in the hepatocyte may be of significance for the development of the hepatic siderosis observed in alcoholism. Iron 102-106 transferrin Rattus norvegicus 42-53 6141733-3 1984 Total transferrin and iron uptake increased in a linear manner as the transferrin concentration was raised up to at least 130 microM. Iron 22-26 transferrin Rattus norvegicus 70-81 6141733-4 1984 This indicates that transferrin and iron are taken up primarily by nonspecific processes, possibly by endocytosis (absorptive or fluid) and by the action of iron chelators. Iron 157-161 transferrin Rattus norvegicus 20-31 6141733-5 1984 However, some evidence indicated the presence of receptors for diferric transferrin on hepatocytes: the molar ratio of iron to transferrin accumulation increased with incubation time, transferrin and iron uptake was proportional to the iron saturation of the transferrin, apotransferrin displaced bound apotransferrin but had no effect on the binding of diferric transferrin, and the molar ratio of iron to transferrin uptake decreased with increasing transferrin concentrations. Iron 119-123 transferrin Rattus norvegicus 72-83 6141733-5 1984 However, some evidence indicated the presence of receptors for diferric transferrin on hepatocytes: the molar ratio of iron to transferrin accumulation increased with incubation time, transferrin and iron uptake was proportional to the iron saturation of the transferrin, apotransferrin displaced bound apotransferrin but had no effect on the binding of diferric transferrin, and the molar ratio of iron to transferrin uptake decreased with increasing transferrin concentrations. Iron 200-204 transferrin Rattus norvegicus 72-83 6141733-5 1984 However, some evidence indicated the presence of receptors for diferric transferrin on hepatocytes: the molar ratio of iron to transferrin accumulation increased with incubation time, transferrin and iron uptake was proportional to the iron saturation of the transferrin, apotransferrin displaced bound apotransferrin but had no effect on the binding of diferric transferrin, and the molar ratio of iron to transferrin uptake decreased with increasing transferrin concentrations. Iron 200-204 transferrin Rattus norvegicus 72-83 6141733-5 1984 However, some evidence indicated the presence of receptors for diferric transferrin on hepatocytes: the molar ratio of iron to transferrin accumulation increased with incubation time, transferrin and iron uptake was proportional to the iron saturation of the transferrin, apotransferrin displaced bound apotransferrin but had no effect on the binding of diferric transferrin, and the molar ratio of iron to transferrin uptake decreased with increasing transferrin concentrations. Iron 200-204 transferrin Rattus norvegicus 72-83 6088313-1 1984 Transferrin receptor in hepatocytes was studied by iron-saturated[125I]transferrin binding. Iron 51-55 transferrin Rattus norvegicus 71-82 6088317-2 1984 Incubation of rat reticulocytes at 37 and 4 degrees C with differic preparations of four of these transferrin forms labeled with 59Fe and 125I show no differences in membrane binding of iron and transferrin and in iron uptake. Iron 186-190 transferrin Rattus norvegicus 98-109 6331503-1 1984 Rat liver mitochondria accumulate iron mobilized from transferrin by pyrophosphate. Iron 34-38 transferrin Rattus norvegicus 54-65 6547607-7 1984 These results are analyzed in the light of the evidence that transferrin is not only an iron-binding protein, but also a factor involved in cell proliferation and differentiation, and particularly in nerve control of muscle differentiation. Iron 88-92 transferrin Rattus norvegicus 61-72 6326850-0 1984 Uptake of iron from transferrin by isolated hepatocytes. Iron 10-14 transferrin Rattus norvegicus 20-31 6326850-1 1984 Isolated rat hepatocytes containing 0.56-1.79 micrograms iron/10(6) cells and with an intracellular ATP concentration of 3-4 mM, accumulate iron from transferrin linearly with time for at least 3 h. At 37 degrees C the rate of uptake amounts to 0.3-0.7 pmol/mg cell protein per min. Iron 57-61 transferrin Rattus norvegicus 150-161 6326850-1 1984 Isolated rat hepatocytes containing 0.56-1.79 micrograms iron/10(6) cells and with an intracellular ATP concentration of 3-4 mM, accumulate iron from transferrin linearly with time for at least 3 h. At 37 degrees C the rate of uptake amounts to 0.3-0.7 pmol/mg cell protein per min. Iron 140-144 transferrin Rattus norvegicus 150-161 6326850-7 1984 The results suggest that iron uptake from transferrin by hepatocytes in suspension involves reductive removal of iron. Iron 25-29 transferrin Rattus norvegicus 42-53 6326850-7 1984 The results suggest that iron uptake from transferrin by hepatocytes in suspension involves reductive removal of iron. Iron 113-117 transferrin Rattus norvegicus 42-53 6421305-6 1984 The iron-binding capacity of plasma, an activity ascribed to plasma transferrin, was reduced in selenium-deficient and increased in selenium-supplemented animals. Iron 4-8 transferrin Rattus norvegicus 68-79 6325265-2 1984 It seems that two mechanisms are involved: Iron is released from endocytosed transferrin by acid vesicles. Iron 43-47 transferrin Rattus norvegicus 77-88 6325265-3 1984 Iron is released from surface-receptor-bound transferrin at the plasma membrane, without internalization of the transferrin receptor complex. Iron 0-4 transferrin Rattus norvegicus 45-56 6675690-1 1983 Electron microscope autoradiography was used to quantitate the uptake of transferrin and transferrin-bound iron by rat erythroid cells at the various stages of development. Iron 107-111 transferrin Rattus norvegicus 89-100 6633931-0 1983 Trophic effect of iron-bound transferrin on acetylcholine receptors in rat skeletal muscle in vivo. Iron 18-22 transferrin Rattus norvegicus 29-40 6633931-1 1983 Trophic effect of iron-bound transferrin (FeTf) on the total content of acetylcholine receptors (AChRs) and the specific activity of AChRs in innervated and denervated skeletal muscle was investigated in vivo. Iron 18-22 transferrin Rattus norvegicus 29-40 6870878-0 1983 Transferrin recycling in reticulocytes: pH and iron are important determinants of ligand binding and processing. Iron 47-51 transferrin Rattus norvegicus 0-11 6853722-6 1983 Transferrin was found in similar amounts in all regions of the small intestine, was not affected by iron loading but doubled in response to iron deficiency. Iron 140-144 transferrin Rattus norvegicus 0-11 6824083-0 1983 Effect of iron stores on hepatic metabolism of transferrin-bound iron. Iron 10-14 transferrin Rattus norvegicus 47-58 6824083-0 1983 Effect of iron stores on hepatic metabolism of transferrin-bound iron. Iron 65-69 transferrin Rattus norvegicus 47-58 6131699-6 1983 Instead they show that the major effect of the bases is to inhibit iron release from transferrin molecules on or within the cells. Iron 67-71 transferrin Rattus norvegicus 85-96 6131699-9 1983 It is concluded that the bases tested in this work inhibit iron release from transferrin in intracellular vesicles by increasing their pH rather than by blocking transglutaminase and thereby restricting endocytosis. Iron 59-63 transferrin Rattus norvegicus 77-88 6821698-0 1983 The significance of transferrin for intestinal iron absorption. Iron 47-51 transferrin Rattus norvegicus 20-31 6821698-2 1983 Within the cell, iron is released and transferred to the blood stream, whereas iron-free transferrin returns to the brush border to be recycled. Iron 79-83 transferrin Rattus norvegicus 89-100 6821698-6 1983 In normal animals, 4 micrograms of the 50 micrograms of transferrin iron was absorbed over 1 hr. Iron 68-72 transferrin Rattus norvegicus 56-67 6821698-13 1983 These studies support the role of mucosal transferrin as a shuttle protein for iron absorption. Iron 79-83 transferrin Rattus norvegicus 42-53 6296164-1 1983 Iron-loaded transferrin has been shown to be necessary for the support of cell proliferation in culture. Iron 0-4 transferrin Rattus norvegicus 12-23 6675690-2 1983 The capacity of the cells to take up iron closely paralleled their ability to bind transferrin, suggesting that the level of transferrin receptors is the major factor which regulates the rate at which immature erythroid cells can accumulate iron. Iron 37-41 transferrin Rattus norvegicus 125-136 6675690-2 1983 The capacity of the cells to take up iron closely paralleled their ability to bind transferrin, suggesting that the level of transferrin receptors is the major factor which regulates the rate at which immature erythroid cells can accumulate iron. Iron 241-245 transferrin Rattus norvegicus 83-94 6675690-2 1983 The capacity of the cells to take up iron closely paralleled their ability to bind transferrin, suggesting that the level of transferrin receptors is the major factor which regulates the rate at which immature erythroid cells can accumulate iron. Iron 241-245 transferrin Rattus norvegicus 125-136 6675690-4 1983 During development, immature rat erythroid cells acquire about twice as much iron from transferrin as is present in the haemoglobin of mature erythrocytes. Iron 77-81 transferrin Rattus norvegicus 87-98 6679475-2 1983 Intracellular transferrin was able to donate iron to the small-molecular weight iron pool, and the latter was able to transfer, by a process not requiring energy or movement of serum transferrin, iron to ferritin. Iron 45-49 transferrin Rattus norvegicus 14-25 6094079-2 1983 Such iron transfer from serotransferrin (TF) to hepatocytes involves a TF receptor. Iron 5-9 transferrin Rattus norvegicus 24-39 6679475-2 1983 Intracellular transferrin was able to donate iron to the small-molecular weight iron pool, and the latter was able to transfer, by a process not requiring energy or movement of serum transferrin, iron to ferritin. Iron 80-84 transferrin Rattus norvegicus 14-25 6679475-2 1983 Intracellular transferrin was able to donate iron to the small-molecular weight iron pool, and the latter was able to transfer, by a process not requiring energy or movement of serum transferrin, iron to ferritin. Iron 80-84 transferrin Rattus norvegicus 14-25 6679475-5 1983 It is concluded that iron is taken up by the rat hepatocyte from serum transferrin by a process not requiring energy or movement of serum transferrin into the cell interior; and that intracellular transferrin is involved in acquiring iron from serum transferrin at the cell surface, with iron then being transferred to the small-molecular weight iron pool and hence to ferritin. Iron 21-25 transferrin Rattus norvegicus 71-82 7160481-3 1982 At 37 degrees C, iron uptake is much more important than transferrin uptake; it proceeds linearly over the time of incubation, is largely proportional to the extracellular transferrin concentration, and is compatible with uptake by fluid phase endocytosis. Iron 17-21 transferrin Rattus norvegicus 172-183 7160481-4 1982 The difference observed between iron and transferrin uptake implies the existence of a mechanism allowing the reutilization of transferrin after iron delivery. Iron 32-36 transferrin Rattus norvegicus 127-138 7160481-4 1982 The difference observed between iron and transferrin uptake implies the existence of a mechanism allowing the reutilization of transferrin after iron delivery. Iron 145-149 transferrin Rattus norvegicus 41-52 7160481-4 1982 The difference observed between iron and transferrin uptake implies the existence of a mechanism allowing the reutilization of transferrin after iron delivery. Iron 145-149 transferrin Rattus norvegicus 127-138 7126464-5 1982 Transferrin 59Fe was distinguished by a greater reflux to the erythron in iron deficient rats, and by excretion of a larger proportion of 59Fe chelated by DF in the urine. Iron 74-78 transferrin Rattus norvegicus 0-11 7175808-3 1982 These results suggest that the increase in iron transfer to the fetus occurs as a result of an increase in the number of transferrin receptors on the maternal surface of the placenta rather than being due to a change in the affinity or turnover rate of the existing receptors, although disproportionate change in the number of receptors and maternal placental surface area suggests that there may be a reduction of the density of transferrin receptors. Iron 43-47 transferrin Rattus norvegicus 121-132 7175808-3 1982 These results suggest that the increase in iron transfer to the fetus occurs as a result of an increase in the number of transferrin receptors on the maternal surface of the placenta rather than being due to a change in the affinity or turnover rate of the existing receptors, although disproportionate change in the number of receptors and maternal placental surface area suggests that there may be a reduction of the density of transferrin receptors. Iron 43-47 transferrin Rattus norvegicus 430-441 7175808-4 1982 The ratios of fetal and total (fetal plus placental) iron to transferrin showed that maturation of the mechanism of iron release from transferrin and the intra-placental iron transport system occurred during development. Iron 116-120 transferrin Rattus norvegicus 61-72 7175808-4 1982 The ratios of fetal and total (fetal plus placental) iron to transferrin showed that maturation of the mechanism of iron release from transferrin and the intra-placental iron transport system occurred during development. Iron 116-120 transferrin Rattus norvegicus 134-145 7175808-4 1982 The ratios of fetal and total (fetal plus placental) iron to transferrin showed that maturation of the mechanism of iron release from transferrin and the intra-placental iron transport system occurred during development. Iron 116-120 transferrin Rattus norvegicus 61-72 7175808-4 1982 The ratios of fetal and total (fetal plus placental) iron to transferrin showed that maturation of the mechanism of iron release from transferrin and the intra-placental iron transport system occurred during development. Iron 116-120 transferrin Rattus norvegicus 134-145 7138904-0 1982 Evidence for the functional equivalence of the iron-binding sites of rat transferrin. Iron 47-51 transferrin Rattus norvegicus 73-84 7138904-1 1982 The role of the two iron-binding sites of rat transferrin in the exchange of iron with cells has been assessed using urea polyacrylamide gel electrophoresis to separate and quantitate the four possible molecular species of transferrin generated during the incubation of 125I-labelled transferrin with rat reticulocytes and hepatocytes. Iron 20-24 transferrin Rattus norvegicus 46-57 7138904-1 1982 The role of the two iron-binding sites of rat transferrin in the exchange of iron with cells has been assessed using urea polyacrylamide gel electrophoresis to separate and quantitate the four possible molecular species of transferrin generated during the incubation of 125I-labelled transferrin with rat reticulocytes and hepatocytes. Iron 20-24 transferrin Rattus norvegicus 223-234 7138904-1 1982 The role of the two iron-binding sites of rat transferrin in the exchange of iron with cells has been assessed using urea polyacrylamide gel electrophoresis to separate and quantitate the four possible molecular species of transferrin generated during the incubation of 125I-labelled transferrin with rat reticulocytes and hepatocytes. Iron 20-24 transferrin Rattus norvegicus 223-234 7138904-1 1982 The role of the two iron-binding sites of rat transferrin in the exchange of iron with cells has been assessed using urea polyacrylamide gel electrophoresis to separate and quantitate the four possible molecular species of transferrin generated during the incubation of 125I-labelled transferrin with rat reticulocytes and hepatocytes. Iron 77-81 transferrin Rattus norvegicus 46-57 7138904-3 1982 After 2 h 44.8% of the iron had been removed by the cells, and of the iron-depleted transferrin 71.8% was apotransferrin, the remainder being monoferric transferrin, 16.1% with N-terminal iron and 12.1% with C-terminal iron. Iron 70-74 transferrin Rattus norvegicus 84-95 7138904-3 1982 After 2 h 44.8% of the iron had been removed by the cells, and of the iron-depleted transferrin 71.8% was apotransferrin, the remainder being monoferric transferrin, 16.1% with N-terminal iron and 12.1% with C-terminal iron. Iron 70-74 transferrin Rattus norvegicus 109-120 7138904-3 1982 After 2 h 44.8% of the iron had been removed by the cells, and of the iron-depleted transferrin 71.8% was apotransferrin, the remainder being monoferric transferrin, 16.1% with N-terminal iron and 12.1% with C-terminal iron. Iron 70-74 transferrin Rattus norvegicus 84-95 7138904-3 1982 After 2 h 44.8% of the iron had been removed by the cells, and of the iron-depleted transferrin 71.8% was apotransferrin, the remainder being monoferric transferrin, 16.1% with N-terminal iron and 12.1% with C-terminal iron. Iron 70-74 transferrin Rattus norvegicus 109-120 7138904-3 1982 After 2 h 44.8% of the iron had been removed by the cells, and of the iron-depleted transferrin 71.8% was apotransferrin, the remainder being monoferric transferrin, 16.1% with N-terminal iron and 12.1% with C-terminal iron. Iron 70-74 transferrin Rattus norvegicus 84-95 7138904-3 1982 After 2 h 44.8% of the iron had been removed by the cells, and of the iron-depleted transferrin 71.8% was apotransferrin, the remainder being monoferric transferrin, 16.1% with N-terminal iron and 12.1% with C-terminal iron. Iron 70-74 transferrin Rattus norvegicus 109-120 7138904-7 1982 Release of iron from hepatocytes to apotransferrin lead to the appearance of both monoferric species and then to increasing amounts of diferric transferrin. Iron 11-15 transferrin Rattus norvegicus 39-50 7138791-4 1982 Macrophages are also capable of binding about one-third as much iron-saturated transferrin as iron-free transferrin. Iron 64-68 transferrin Rattus norvegicus 79-90 7138791-4 1982 Macrophages are also capable of binding about one-third as much iron-saturated transferrin as iron-free transferrin. Iron 94-98 transferrin Rattus norvegicus 104-115 7059591-1 1982 The kinetics of the cellular uptake of iron-transferrin complex was studied in L1210 murine leukemia cells and rat reticulocytes using 125I-transferrin. Iron 39-43 transferrin Rattus norvegicus 140-151 6286381-3 1982 PAGE studies with a purified membrane complex B2, from which the functional role in transferrin binding and iron uptake has been shown previously, showed that the transferrin receptor is localized on a membrane protein with a mol. Iron 108-112 transferrin Rattus norvegicus 163-174 7055644-7 1982 Indeed, a higher plasma iron and transferrin saturation augmented the movement of iron into the plasma from iron-donating tissues. Iron 82-86 transferrin Rattus norvegicus 33-44 7055644-7 1982 Indeed, a higher plasma iron and transferrin saturation augmented the movement of iron into the plasma from iron-donating tissues. Iron 82-86 transferrin Rattus norvegicus 33-44 7055644-8 1982 It is proposed that the donation of iron by transferrin in some way immediately facilitates the procurement of more iron by transferrin. Iron 36-40 transferrin Rattus norvegicus 44-55 7055644-8 1982 It is proposed that the donation of iron by transferrin in some way immediately facilitates the procurement of more iron by transferrin. Iron 36-40 transferrin Rattus norvegicus 124-135 7055644-8 1982 It is proposed that the donation of iron by transferrin in some way immediately facilitates the procurement of more iron by transferrin. Iron 116-120 transferrin Rattus norvegicus 44-55 7055644-8 1982 It is proposed that the donation of iron by transferrin in some way immediately facilitates the procurement of more iron by transferrin. Iron 116-120 transferrin Rattus norvegicus 124-135 6268404-0 1981 Studies on the mechanism of pyrophosphate-mediated uptake of iron from transferrin by isolated rat-liver mitochondria. Iron 61-65 transferrin Rattus norvegicus 71-82 7296013-0 1981 Determination of transferrin-like immunoreactivity in the mucosal homogenate of the duodenum, jejunum, and ileum of normal and iron deficient rats. Iron 127-131 transferrin Rattus norvegicus 17-28 6947077-7 1981 Serum iron and iron binding in rats determined 20 hr after MTX therapy showed significantly higher levels of serum iron and lower levels of Ga-67 in blood, and the percent transferrin saturation was approximately 95%. Iron 15-19 transferrin Rattus norvegicus 172-183 6947077-7 1981 Serum iron and iron binding in rats determined 20 hr after MTX therapy showed significantly higher levels of serum iron and lower levels of Ga-67 in blood, and the percent transferrin saturation was approximately 95%. Iron 15-19 transferrin Rattus norvegicus 172-183 6268404-2 1981 Respiring rat liver mitochondria accumulate iron released from transferrin by pyrophosphate. Iron 44-48 transferrin Rattus norvegicus 63-74 6268404-3 1981 The amount of iron accumulated is 1--1.5 nmol mg protein-1 h-1, or approximately 60% of the amount of iron mobilized from transferrin. Iron 14-18 transferrin Rattus norvegicus 122-133 6268404-3 1981 The amount of iron accumulated is 1--1.5 nmol mg protein-1 h-1, or approximately 60% of the amount of iron mobilized from transferrin. Iron 102-106 transferrin Rattus norvegicus 122-133 6268404-13 1981 The results are compatible with a model in which ferric iron is mobilized from transferrin by pyrophosphate, ferric iron pyrophosphate is bound to the mitochondria, iron is reduced, dissociates from pyrophosphate and is taken up by the mitochondria. Iron 56-60 transferrin Rattus norvegicus 79-90 6271283-7 1981 It is clear that myocytes acquire iron from diferric (ovo)transferrin in a process that involves high-affinity, specific binding to membrane receptors. Iron 34-38 transferrin Rattus norvegicus 58-69 7448422-0 1981 The behavior of transferrin iron in the rat. Iron 28-32 transferrin Rattus norvegicus 16-27 6269977-1 1981 Isolated rat hepatocytes accumulate iron from iron-transferrin by a process which is dependent on the temperature and on the transferrin concentration, and which is diminished by treatment of the cells with a proteolytic enzyme. Iron 36-40 transferrin Rattus norvegicus 51-62 6269977-1 1981 Isolated rat hepatocytes accumulate iron from iron-transferrin by a process which is dependent on the temperature and on the transferrin concentration, and which is diminished by treatment of the cells with a proteolytic enzyme. Iron 36-40 transferrin Rattus norvegicus 125-136 6269977-1 1981 Isolated rat hepatocytes accumulate iron from iron-transferrin by a process which is dependent on the temperature and on the transferrin concentration, and which is diminished by treatment of the cells with a proteolytic enzyme. Iron 46-50 transferrin Rattus norvegicus 51-62 6269977-1 1981 Isolated rat hepatocytes accumulate iron from iron-transferrin by a process which is dependent on the temperature and on the transferrin concentration, and which is diminished by treatment of the cells with a proteolytic enzyme. Iron 46-50 transferrin Rattus norvegicus 125-136 6269977-2 1981 These observations are consistent with a mechanism for iron uptake into hepatocytes involving the binding of iron-transferrin to a specific cell-surface receptor. Iron 55-59 transferrin Rattus norvegicus 114-125 6269977-2 1981 These observations are consistent with a mechanism for iron uptake into hepatocytes involving the binding of iron-transferrin to a specific cell-surface receptor. Iron 109-113 transferrin Rattus norvegicus 114-125 6269977-3 1981 Apotransferrin is also able to bind to the hepatocyte but the apparent binding constant is about 35 times lower than that observed for the binding of iron-transferrin. Iron 150-154 transferrin Rattus norvegicus 3-14 6269977-4 1981 The binding of apotransferrin to the cells is completely abolished by a low concentration of iron-transferrin. Iron 93-97 transferrin Rattus norvegicus 18-29 6269977-5 1981 This suggests that the apotransferrin is binding weakly to the same receptor to which iron-transferrin binds and that there are not receptors on the surface of the hepatocyte specific for apotransferrin. Iron 86-90 transferrin Rattus norvegicus 26-37 7448423-4 1981 Only part of this effect in the rat was due to the different rates of clearance of mono-and differic transferrin, the latter having a higher iron delivery rate in vivo. Iron 141-145 transferrin Rattus norvegicus 101-112 7448422-3 1981 Complete and specific binding of 59FeSO4 by the iron binding sites of transferrin was demonstrated after in vitro or in vivo addition of ferrous ammonium sulfate in pH 2 saline up to the point of iron saturation. Iron 48-52 transferrin Rattus norvegicus 70-81 7448422-3 1981 Complete and specific binding of 59FeSO4 by the iron binding sites of transferrin was demonstrated after in vitro or in vivo addition of ferrous ammonium sulfate in pH 2 saline up to the point of iron saturation. Iron 196-200 transferrin Rattus norvegicus 70-81 7448422-4 1981 In vitro the radioriron transferrin complex in plasma was stable and its iron had a negligible exchange with other transferrin binding sites over several hours. Iron 19-23 transferrin Rattus norvegicus 24-35 7448422-4 1981 In vitro the radioriron transferrin complex in plasma was stable and its iron had a negligible exchange with other transferrin binding sites over several hours. Iron 19-23 transferrin Rattus norvegicus 115-126 7448422-6 1981 Iron distribution among body tissues was similar for mono- and diferric transferrin iron and was not affected by the site distribution of iron on the transferrin molecule. Iron 0-4 transferrin Rattus norvegicus 72-83 7448422-7 1981 The only important aspect of transferrin iron binding was the more rapid tissue uptake of iron in the diferric form was compared to monoferric transferrin. Iron 41-45 transferrin Rattus norvegicus 29-40 7448422-7 1981 The only important aspect of transferrin iron binding was the more rapid tissue uptake of iron in the diferric form was compared to monoferric transferrin. Iron 41-45 transferrin Rattus norvegicus 143-154 7448422-7 1981 The only important aspect of transferrin iron binding was the more rapid tissue uptake of iron in the diferric form was compared to monoferric transferrin. Iron 90-94 transferrin Rattus norvegicus 29-40 7448422-9 1981 In the iron loaded animal, monoferric transferrin injected into the plasma was rapidly loaded by iron from tissue and thereby converted to diferric transferrin. Iron 7-11 transferrin Rattus norvegicus 38-49 7448422-9 1981 In the iron loaded animal, monoferric transferrin injected into the plasma was rapidly loaded by iron from tissue and thereby converted to diferric transferrin. Iron 7-11 transferrin Rattus norvegicus 148-159 7448422-9 1981 In the iron loaded animal, monoferric transferrin injected into the plasma was rapidly loaded by iron from tissue and thereby converted to diferric transferrin. Iron 97-101 transferrin Rattus norvegicus 38-49 7448422-9 1981 In the iron loaded animal, monoferric transferrin injected into the plasma was rapidly loaded by iron from tissue and thereby converted to diferric transferrin. Iron 97-101 transferrin Rattus norvegicus 148-159 7448422-10 1981 Injection of diferric transferrin in the iron deficient animal was associated with a rapid disappearance from circulation of the original complex and a subsequent appearance of monoferric transferrin as a result of iron returning from tissues. Iron 41-45 transferrin Rattus norvegicus 22-33 7448422-10 1981 Injection of diferric transferrin in the iron deficient animal was associated with a rapid disappearance from circulation of the original complex and a subsequent appearance of monoferric transferrin as a result of iron returning from tissues. Iron 41-45 transferrin Rattus norvegicus 188-199 7448422-10 1981 Injection of diferric transferrin in the iron deficient animal was associated with a rapid disappearance from circulation of the original complex and a subsequent appearance of monoferric transferrin as a result of iron returning from tissues. Iron 215-219 transferrin Rattus norvegicus 22-33 7448422-10 1981 Injection of diferric transferrin in the iron deficient animal was associated with a rapid disappearance from circulation of the original complex and a subsequent appearance of monoferric transferrin as a result of iron returning from tissues. Iron 215-219 transferrin Rattus norvegicus 188-199 7437510-1 1980 Using highly sensitive 2-site immunoradiometric assays, we examined the relationship between iron absorption from closed intestinal loops and transferrin and ferritin concentrations in isolated duodenal mucosal cells. Iron 93-97 transferrin Rattus norvegicus 142-153 7459386-4 1980 Uptake of iron from diferic transferrin by hepatocytes is linear with time and is accelerated at increased diferric transferrin concentrations. Iron 10-14 transferrin Rattus norvegicus 28-39 7459386-4 1980 Uptake of iron from diferic transferrin by hepatocytes is linear with time and is accelerated at increased diferric transferrin concentrations. Iron 10-14 transferrin Rattus norvegicus 116-127 7437510-4 1980 The highest correlation with iron absorption was observed with the transferrin-ferritin ratio in isolated mucosal cells. Iron 29-33 transferrin Rattus norvegicus 67-78 7459386-5 1980 Apotransferrin is able to decrease net iron uptake by hepatocytes from diferric transferrin by a process not dependent on the apotransferrin concentrations used or on the rate at which the cells take up iron. Iron 39-43 transferrin Rattus norvegicus 3-14 7398651-0 1980 Uptake of iron from transferrin by isolated rat-liver mitochondria mediated by phosphate compounds. Iron 10-14 transferrin Rattus norvegicus 20-31 7459386-5 1980 Apotransferrin is able to decrease net iron uptake by hepatocytes from diferric transferrin by a process not dependent on the apotransferrin concentrations used or on the rate at which the cells take up iron. Iron 203-207 transferrin Rattus norvegicus 3-14 7459386-6 1980 Immunoprecipitation of the apotransferrin during these incubations indicate that iron is being released from the cells to apotransferrin at the same time as iron is being taken up from diferric transferrin. Iron 81-85 transferrin Rattus norvegicus 30-41 7459386-6 1980 Immunoprecipitation of the apotransferrin during these incubations indicate that iron is being released from the cells to apotransferrin at the same time as iron is being taken up from diferric transferrin. Iron 157-161 transferrin Rattus norvegicus 30-41 7437475-0 1980 Studies on the mechanism of transferrin iron uptake by rat reticulocytes. Iron 40-44 transferrin Rattus norvegicus 28-39 7437475-1 1980 Mechanism of transferrin iron uptake by rat reticulocytes was studied using 59Fe- and 125I-labelled rat transferrin. Iron 25-29 transferrin Rattus norvegicus 13-24 7437475-1 1980 Mechanism of transferrin iron uptake by rat reticulocytes was studied using 59Fe- and 125I-labelled rat transferrin. Iron 25-29 transferrin Rattus norvegicus 104-115 7412500-0 1980 Transferrin acquisition of catabolized erythrocyte iron in the rat. Iron 51-55 transferrin Rattus norvegicus 0-11 7426440-3 1980 The mean rate of efflux into a plasma pool containing normal iron and transferrin concentrations was 0.9% of the initial hepatic radioactive iron pool per hour. Iron 141-145 transferrin Rattus norvegicus 70-81 7426440-10 1980 However, increasing the iron concentration in the perfusate by the addition of iron-saturated transferrin without any reduction in the unsaturated iron binding capacity additionally increased iron release into plasma and EBM. Iron 24-28 transferrin Rattus norvegicus 94-105 7426440-10 1980 However, increasing the iron concentration in the perfusate by the addition of iron-saturated transferrin without any reduction in the unsaturated iron binding capacity additionally increased iron release into plasma and EBM. Iron 79-83 transferrin Rattus norvegicus 94-105 7426440-10 1980 However, increasing the iron concentration in the perfusate by the addition of iron-saturated transferrin without any reduction in the unsaturated iron binding capacity additionally increased iron release into plasma and EBM. Iron 79-83 transferrin Rattus norvegicus 94-105 7411140-4 1980 Biochem., 13-5-R122, Toronto, Canada) was extended to the vanadium in the biochemical mechanisms which involve the exchange of iron between transferrin and ferritin. Iron 127-131 transferrin Rattus norvegicus 140-151 6902969-0 1980 The role of plasma transferrin in iron absorption in the rat. Iron 34-38 transferrin Rattus norvegicus 19-30 6902969-4 1980 The rate of exchange were insufficient for transferrin to act as the carrier of iron at the rate at which it passes from intestinal cells to portal plasma after ingesting a dose of inorganic iron. Iron 80-84 transferrin Rattus norvegicus 43-54 6902969-5 1980 Some specific binding of transferrin and cellular uptake of iron by intestinal mucosa was observed after the intravenous injection of transferrin labelled with 59Fe and 125I. Iron 60-64 transferrin Rattus norvegicus 134-145 6902969-7 1980 The passage of plasma transferrin into the interstitial fluid of the intestinal mucosa and binding to mucosal cells probably functions primarily to supply iron to the cells and not to act as a carrier of iron from the cells. Iron 155-159 transferrin Rattus norvegicus 22-33 6902969-7 1980 The passage of plasma transferrin into the interstitial fluid of the intestinal mucosa and binding to mucosal cells probably functions primarily to supply iron to the cells and not to act as a carrier of iron from the cells. Iron 204-208 transferrin Rattus norvegicus 22-33 7398651-2 1980 Isolated rat-liver mitochondria accumulate iron from transferrin at neutral pH by a mechanism which is markedly stimulated by small-molecular-weight polyphosphate compounds. Iron 43-47 transferrin Rattus norvegicus 53-64 7398651-11 1980 The results suggest that iron is mobilized from transferrin by the polyphosphate compounds outside the mitochondria in a subsequent reaction. Iron 25-29 transferrin Rattus norvegicus 48-59 7357090-2 1980 When reticulocyte-rich red cells were incubated in vitro with doubly (59Fe, 125I) labeled transferrin, b/b cells demonstrated a significantly higher uptake of transferrin (164% of control at 60 min), and a significantly lower uptake of iron (21% of control at 60 min) than control cells. Iron 236-240 transferrin Rattus norvegicus 90-101 7357090-5 1980 These findings suggest a defect in the delivery of iron to the b/b reticulocyte, which is distal to the binding of transferrin to its cell surface receptor. Iron 51-55 transferrin Rattus norvegicus 115-126 7356025-0 1980 A physiological model for hepatic metabolism of transferrin-bound iron. Iron 66-70 transferrin Rattus norvegicus 48-59 719174-0 1978 Differences between the binding sites for iron binding and release in human and rat transferrin. Iron 42-46 transferrin Rattus norvegicus 84-95 429862-0 1979 Transferrin binding and iron transport in iron-deficient and iron-replete rat reticulocytes. Iron 42-46 transferrin Rattus norvegicus 0-11 429862-0 1979 Transferrin binding and iron transport in iron-deficient and iron-replete rat reticulocytes. Iron 42-46 transferrin Rattus norvegicus 0-11 496901-0 1979 The mechanism of hepatic iron uptake from native and denatured transferrin and its subcellular metabolism in the liver cell. Iron 25-29 transferrin Rattus norvegicus 63-74 496901-9 1979 The study suggests that hepatic iron uptake from native transferrin does not involve endocytosis. Iron 32-36 transferrin Rattus norvegicus 56-67 424657-8 1979 The distribution of copper in the supernatant was changed due to a simultaneous administration of iron; the amount of copper bound in the transferrin fraction decreased in favor of the metallothionein fraction and another copper binding fraction was eluted between the transferrin and the metallothionein fraction. Iron 98-102 transferrin Rattus norvegicus 138-149 424657-12 1979 The results suggest that the affinity of copper to two mucosal iron binding proteins, transferrin and metallothionein, is at least partly responsible for the inhibitory effect of copper on iron absorption in iron deficiency. Iron 63-67 transferrin Rattus norvegicus 86-97 424657-12 1979 The results suggest that the affinity of copper to two mucosal iron binding proteins, transferrin and metallothionein, is at least partly responsible for the inhibitory effect of copper on iron absorption in iron deficiency. Iron 189-193 transferrin Rattus norvegicus 86-97 429836-0 1979 In vivo evidence for the functional heterogeneity of transferrin-bound iron. Iron 71-75 transferrin Rattus norvegicus 53-64 684293-9 1978 In anemia due to protein deficiency the typical increase of 59Fe incorporation into the fraction of mucosal transferrin--usually occuring in iron deficiency--could not be observed. Iron 141-145 transferrin Rattus norvegicus 108-119 751406-0 1978 The iron binding and releasing functions of the transferrin with special reference to rat isotransferrins. Iron 4-8 transferrin Rattus norvegicus 48-59 711859-0 1978 Iron uptake from rat plasma transferrin by rat reticulocytes. Iron 0-4 transferrin Rattus norvegicus 28-39 711859-3 1978 Reticulocyte uptake of diferric transferrin resulted in the removal of both iron atoms from the transferrin molecule. Iron 76-80 transferrin Rattus norvegicus 32-43 711859-3 1978 Reticulocyte uptake of diferric transferrin resulted in the removal of both iron atoms from the transferrin molecule. Iron 76-80 transferrin Rattus norvegicus 96-107 711859-5 1978 It is concluded that the two species of transferrin and their individual sites function similarly in their release of iron to tissue receptors. Iron 118-122 transferrin Rattus norvegicus 40-51 30489-0 1978 The effect of acid pH and citrate on the release and exchange of iron on rat transferrin. Iron 65-69 transferrin Rattus norvegicus 77-88 30489-1 1978 The effect of acid pH and citrate on the exchange of iron between binding sites of rat transferrin has been studied. Iron 53-57 transferrin Rattus norvegicus 87-98 30489-2 1978 In the absence of citrate, diferric transferrin shows stepwise loss of iron atoms with the first atom of iron released at approximately pH 5.2. Iron 71-75 transferrin Rattus norvegicus 36-47 30489-4 1978 Iron dissociation from monoferric transferrin at acid pH, with or without citrate, is a random process. Iron 0-4 transferrin Rattus norvegicus 34-45 30489-5 1978 At pH 7.4, randomization of iron on transferrin takes from 3 to 6 h in the presence of millimolar concentrations of citrate. Iron 28-32 transferrin Rattus norvegicus 36-47 687622-0 1978 Binding sites of iron transferrin on rat reticulocytes. Iron 17-21 transferrin Rattus norvegicus 22-33 687622-3 1978 In the process of iron uptake by precursors of the erythrocytes probably more than one membrane component is involved; besides the specific transferrin receptor, another membrane component with a high iron activity after incubation with 59Fe can be isolated. Iron 18-22 transferrin Rattus norvegicus 140-151 687622-7 1978 Incubation of reticulocytes with Fab fragments of an antibody against the membrane receptor for transferrin causes a concentration-dependent decrease in transferrin binding and iron uptake. Iron 177-181 transferrin Rattus norvegicus 96-107 687622-11 1978 Intact immature red cells are necessary for specific binding of transferrin with the receptor followed by iron uptake. Iron 106-110 transferrin Rattus norvegicus 64-75 684293-11 1978 Moreover a decrease of iron absorption is observed, which is associated with a decreased 59Fe ratio of transferrin/ferritin-fraction. Iron 23-27 transferrin Rattus norvegicus 103-114 700103-0 1978 Differential effects of metal-binding agents on the uptake of iron from transferrin by isolated rat liver mitochondria. Iron 62-66 transferrin Rattus norvegicus 72-83 677335-0 1978 Effect of transferrin saturation on iron delivery in rats. Iron 36-40 transferrin Rattus norvegicus 10-21 698124-3 1978 Specific incorporation of iron into feritin from a perfusate of normal transferrin iron saturation was enhanced in nutritional iron deficiency as compared to controls after 5 h of perfusion but not after 1 h, suggesting that increased uptake of iron from the perfusate may play a role in stimulating hepatic ferritin synthesis and assembly. Iron 26-30 transferrin Rattus norvegicus 71-82 698124-3 1978 Specific incorporation of iron into feritin from a perfusate of normal transferrin iron saturation was enhanced in nutritional iron deficiency as compared to controls after 5 h of perfusion but not after 1 h, suggesting that increased uptake of iron from the perfusate may play a role in stimulating hepatic ferritin synthesis and assembly. Iron 83-87 transferrin Rattus norvegicus 71-82 698124-3 1978 Specific incorporation of iron into feritin from a perfusate of normal transferrin iron saturation was enhanced in nutritional iron deficiency as compared to controls after 5 h of perfusion but not after 1 h, suggesting that increased uptake of iron from the perfusate may play a role in stimulating hepatic ferritin synthesis and assembly. Iron 83-87 transferrin Rattus norvegicus 71-82 698124-5 1978 In control, nutritionally iron deficient and iron-refed rats there was a significant, direct correlation between the transferrin-iron saturation of the perfusate at physiological transferrin concentrations and total hepatic iron uptake after 5 h perfusion. Iron 26-30 transferrin Rattus norvegicus 117-128 698124-5 1978 In control, nutritionally iron deficient and iron-refed rats there was a significant, direct correlation between the transferrin-iron saturation of the perfusate at physiological transferrin concentrations and total hepatic iron uptake after 5 h perfusion. Iron 45-49 transferrin Rattus norvegicus 117-128 698124-5 1978 In control, nutritionally iron deficient and iron-refed rats there was a significant, direct correlation between the transferrin-iron saturation of the perfusate at physiological transferrin concentrations and total hepatic iron uptake after 5 h perfusion. Iron 45-49 transferrin Rattus norvegicus 179-190 698124-5 1978 In control, nutritionally iron deficient and iron-refed rats there was a significant, direct correlation between the transferrin-iron saturation of the perfusate at physiological transferrin concentrations and total hepatic iron uptake after 5 h perfusion. Iron 45-49 transferrin Rattus norvegicus 117-128 698124-5 1978 In control, nutritionally iron deficient and iron-refed rats there was a significant, direct correlation between the transferrin-iron saturation of the perfusate at physiological transferrin concentrations and total hepatic iron uptake after 5 h perfusion. Iron 45-49 transferrin Rattus norvegicus 179-190 698124-5 1978 In control, nutritionally iron deficient and iron-refed rats there was a significant, direct correlation between the transferrin-iron saturation of the perfusate at physiological transferrin concentrations and total hepatic iron uptake after 5 h perfusion. Iron 45-49 transferrin Rattus norvegicus 117-128 698124-5 1978 In control, nutritionally iron deficient and iron-refed rats there was a significant, direct correlation between the transferrin-iron saturation of the perfusate at physiological transferrin concentrations and total hepatic iron uptake after 5 h perfusion. Iron 45-49 transferrin Rattus norvegicus 179-190 698124-6 1978 A significant positive correlation was found between the hepatic total and ferritin iron uptake and the transferrin synthetic rate measured in the same liver. Iron 84-88 transferrin Rattus norvegicus 104-115 698124-7 1978 It is proposed that in the liver the negative feedback of iron supply on transferrin synthesis may be linked with a positive feedback on ferritin synthesis. Iron 58-62 transferrin Rattus norvegicus 73-84 698124-8 1978 The time-course of these reciprocal responses suggests a role for hepatic ferritin and/or a component of the non-haem, non-ferritin iron pool in the regulation of transferrin synthesis. Iron 132-136 transferrin Rattus norvegicus 163-174 677335-1 1978 Studies were carried out in rats to evaluate the release of iron from monoferric and diferric transferrin. Iron 60-64 transferrin Rattus norvegicus 94-105 677335-4 1978 In all three groups there was a greater in vivo uptake of iron from diferric transferrin by all tissues monitored. Iron 58-62 transferrin Rattus norvegicus 77-88 677335-5 1978 Though the amount varied in different animals, the ratio of uptake between diferric and monoferric transferrin iron varied between 1.56 and 2.10 in the erythron and between 2.38 and 2.65 in the liver. Iron 111-115 transferrin Rattus norvegicus 99-110 677335-6 1978 These studies indicate that changes in transferrin saturation, by changing the proportion of monoferric to diferric transferrin iron, changed the amount of iron released to tissues. Iron 128-132 transferrin Rattus norvegicus 39-50 677335-6 1978 These studies indicate that changes in transferrin saturation, by changing the proportion of monoferric to diferric transferrin iron, changed the amount of iron released to tissues. Iron 128-132 transferrin Rattus norvegicus 116-127 677335-6 1978 These studies indicate that changes in transferrin saturation, by changing the proportion of monoferric to diferric transferrin iron, changed the amount of iron released to tissues. Iron 156-160 transferrin Rattus norvegicus 39-50 677335-6 1978 These studies indicate that changes in transferrin saturation, by changing the proportion of monoferric to diferric transferrin iron, changed the amount of iron released to tissues. Iron 156-160 transferrin Rattus norvegicus 116-127 889709-0 1977 The role of iron in the regulation of hepatic transferrin synthesis. Iron 12-16 transferrin Rattus norvegicus 46-57 623907-4 1978 The second pathway, which was extracellular, could only be activated after saturation of the transferrin iron binding capacity, with the chelated iron excreted by the kidneys. Iron 105-109 transferrin Rattus norvegicus 93-104 623907-4 1978 The second pathway, which was extracellular, could only be activated after saturation of the transferrin iron binding capacity, with the chelated iron excreted by the kidneys. Iron 146-150 transferrin Rattus norvegicus 93-104 101008-0 1978 Functional heterogeneity of transferrin-bound iron: iron uptake by cell suspensions from bone marrow and liver and by cell cultures of fibroblasts and lymphoblasts. Iron 46-50 transferrin Rattus norvegicus 28-39 101008-0 1978 Functional heterogeneity of transferrin-bound iron: iron uptake by cell suspensions from bone marrow and liver and by cell cultures of fibroblasts and lymphoblasts. Iron 52-56 transferrin Rattus norvegicus 28-39 101008-1 1978 According to the hypothesis of Fletcher and Huehns, functional differences exist between both iron-binding sites of transferrin. Iron 94-98 transferrin Rattus norvegicus 116-127 101008-4 1978 Iron transferrin preincubated with rat bone marrow cells donates less iron to rat bone marrow cells, Chinese hamster fibroblasts, human fibroblasts and human lymphoblasts than freshly prepared iron transferrin equal in iron and transferrin concentraion. Iron 0-4 transferrin Rattus norvegicus 5-16 101008-4 1978 Iron transferrin preincubated with rat bone marrow cells donates less iron to rat bone marrow cells, Chinese hamster fibroblasts, human fibroblasts and human lymphoblasts than freshly prepared iron transferrin equal in iron and transferrin concentraion. Iron 70-74 transferrin Rattus norvegicus 5-16 101008-4 1978 Iron transferrin preincubated with rat bone marrow cells donates less iron to rat bone marrow cells, Chinese hamster fibroblasts, human fibroblasts and human lymphoblasts than freshly prepared iron transferrin equal in iron and transferrin concentraion. Iron 193-197 transferrin Rattus norvegicus 5-16 101008-4 1978 Iron transferrin preincubated with rat bone marrow cells donates less iron to rat bone marrow cells, Chinese hamster fibroblasts, human fibroblasts and human lymphoblasts than freshly prepared iron transferrin equal in iron and transferrin concentraion. Iron 193-197 transferrin Rattus norvegicus 5-16 101008-5 1978 Rat liver parenchymal cells, however, take up more iron from preincubated than from freshly prepared iron transferrin. Iron 51-55 transferrin Rattus norvegicus 106-117 101008-5 1978 Rat liver parenchymal cells, however, take up more iron from preincubated than from freshly prepared iron transferrin. Iron 101-105 transferrin Rattus norvegicus 106-117 660666-8 1978 Transferrin, the accessory factor in the SF condition, supplies iron for cells. Iron 64-68 transferrin Rattus norvegicus 0-11 210366-1 1978 The concentration of iron (III)-transferrin (IT) in whole blood and serum, along with another high-spin (five unpaired electrons) iron complex (probably IT) accumulated by tumor tissue, was investigated by electron paramagnetic resonance (EPR) spectroscopy during the development of Murphy-Sturm rat lymphosarcoma. Iron 21-25 transferrin Rattus norvegicus 32-43 889709-1 1977 The role of iron supply in the regulation of hepatic transferrin synthesis by the isolated perfused rat liver was studied using nutritional iron deficiency as the experimental model. Iron 12-16 transferrin Rattus norvegicus 53-64 889709-3 1977 Refeeding with iron, sufficient to restore plasma iron and hepatic ferritin iron but before correction of anaemia, promoted a reduction towards normal in the transferrin synthetic rate. Iron 15-19 transferrin Rattus norvegicus 158-169 889709-6 1977 The concentration of liver iron stores appears to be a major regulatory factor in the control of hepatic transferrin synthesis. Iron 27-31 transferrin Rattus norvegicus 105-116 830782-3 1977 In addition to the previously demonstrated selective tissue uptake of iron from the two binding sites of transferrin, the Fletcher-Huehns hypothesis predicts that iron absorbed by the intestine is delivered selectively to the erythroblast-oriented iron-binding site of transferrin in portal plasma. Iron 163-167 transferrin Rattus norvegicus 269-280 861377-0 1977 Role of transferrin in determining internal iron distribution. Iron 44-48 transferrin Rattus norvegicus 8-19 861377-1 1977 The behavior in vivo of transferrin in loading and unloading iron from its two sites was examined in rats. Iron 61-65 transferrin Rattus norvegicus 24-35 861377-4 1977 In 15 groups of animals in which 3 different iron salts were employed to load transferrin with iron, the mean isotope ratio in the erythron was 1.03 (+/-0.06 SD) and the mean liver ratio was 0.75 (+/-0.21 SD). Iron 45-49 transferrin Rattus norvegicus 78-89 861377-4 1977 In 15 groups of animals in which 3 different iron salts were employed to load transferrin with iron, the mean isotope ratio in the erythron was 1.03 (+/-0.06 SD) and the mean liver ratio was 0.75 (+/-0.21 SD). Iron 95-99 transferrin Rattus norvegicus 78-89 861377-7 1977 It is concluded that iron atoms from the two sites of transferrin have similar tissue distributions in vivo in the experimental situations examined. Iron 21-25 transferrin Rattus norvegicus 54-65 830225-0 1977 Effect of iron saturation of transferrin on hepatic iron uptake: an in vitro study. Iron 10-14 transferrin Rattus norvegicus 29-40 830225-0 1977 Effect of iron saturation of transferrin on hepatic iron uptake: an in vitro study. Iron 52-56 transferrin Rattus norvegicus 29-40 830225-1 1977 Studies were performed to delineate the effect of percentage of saturation of transferrin and total iron concentration on the rate of uptake of iron by the perfused rat liver. Iron 144-148 transferrin Rattus norvegicus 78-89 830225-4 1977 However, raising the concentration of iron in the perfusate while maintaining a constant saturation of transferrin did increase the uptake of iron by the liver. Iron 142-146 transferrin Rattus norvegicus 103-114 830225-5 1977 At similar concentrations of iron and transferrin saturation, iron-deficient livers took up greater amounts of iron than did normal livers. Iron 62-66 transferrin Rattus norvegicus 38-49 830225-5 1977 At similar concentrations of iron and transferrin saturation, iron-deficient livers took up greater amounts of iron than did normal livers. Iron 62-66 transferrin Rattus norvegicus 38-49 830225-6 1977 In our experiments, the hepatic uptake of transferrin-bound iron is determined by (1) the concentration of iron in perfusate and (2) the status of iron stores in the liver being perfused. Iron 60-64 transferrin Rattus norvegicus 42-53 830225-6 1977 In our experiments, the hepatic uptake of transferrin-bound iron is determined by (1) the concentration of iron in perfusate and (2) the status of iron stores in the liver being perfused. Iron 107-111 transferrin Rattus norvegicus 42-53 830225-6 1977 In our experiments, the hepatic uptake of transferrin-bound iron is determined by (1) the concentration of iron in perfusate and (2) the status of iron stores in the liver being perfused. Iron 107-111 transferrin Rattus norvegicus 42-53 830782-0 1977 In vivo evidence for the functional heterogeneity of transferrin-bound iron. Iron 71-75 transferrin Rattus norvegicus 53-64 830782-2 1977 Selective uptake by erythroid precursors of radioiron from portal vein plasma transferrin during intestinal iron absorption. Iron 49-53 transferrin Rattus norvegicus 78-89 830782-3 1977 In addition to the previously demonstrated selective tissue uptake of iron from the two binding sites of transferrin, the Fletcher-Huehns hypothesis predicts that iron absorbed by the intestine is delivered selectively to the erythroblast-oriented iron-binding site of transferrin in portal plasma. Iron 70-74 transferrin Rattus norvegicus 105-116 830782-3 1977 In addition to the previously demonstrated selective tissue uptake of iron from the two binding sites of transferrin, the Fletcher-Huehns hypothesis predicts that iron absorbed by the intestine is delivered selectively to the erythroblast-oriented iron-binding site of transferrin in portal plasma. Iron 163-167 transferrin Rattus norvegicus 269-280 830782-8 1977 These results support the concept of selective release of iron to erythroblast-oriented binding sites of portal plasma transferrin by intestinal cells during absorption. Iron 58-62 transferrin Rattus norvegicus 119-130 830782-9 1977 Combined with previously demonstrated selective tissue uptake of iron from transferrin, these experiments offer strong support for the active role of transferrin in the internal iron exchange of the rat. Iron 65-69 transferrin Rattus norvegicus 150-161 830782-9 1977 Combined with previously demonstrated selective tissue uptake of iron from transferrin, these experiments offer strong support for the active role of transferrin in the internal iron exchange of the rat. Iron 178-182 transferrin Rattus norvegicus 150-161 1009023-1 1976 Iron exchange in the pregnant rat was quantitated by repeated determinations of plasma iron turnover (PIT), transferrin iron distribution and measurements of storage iron and food iron utilization employing selective radio-iron probes. Iron 0-4 transferrin Rattus norvegicus 108-119 12556-1 1976 Isolated rat liver mitochondria accumulate iron from the suspending medium when [59Fe]transferrin is used as a model compound. Iron 43-47 transferrin Rattus norvegicus 86-97 12556-8 1976 The results indicate that the energy-dependent accumulation of [59Fe]transferrin represents a process by which mitochondria accumulate iron from transferrin. Iron 135-139 transferrin Rattus norvegicus 69-80 12556-8 1976 The results indicate that the energy-dependent accumulation of [59Fe]transferrin represents a process by which mitochondria accumulate iron from transferrin. Iron 135-139 transferrin Rattus norvegicus 145-156 1125327-5 1975 A proportion of the 59-Fe incorporated into the stroma and low molecular weight iron fractions during a 1 h incubation with 59-Fe-labelled transferrin was mobilised into ferritin and haemoglobin during a subsequent 4-h "cold-chase". Iron 80-84 transferrin Rattus norvegicus 139-150 1244908-4 1976 Time course and temperature dependence studies suggest the endocytosis of transferrin may be an important mechanism in delivery of iron to the developing red cell. Iron 131-135 transferrin Rattus norvegicus 74-85 1176811-0 1975 In vivo evidence for the functional heterogeneity of transferrin-bound iron. Iron 71-75 transferrin Rattus norvegicus 53-64 1176811-2 1975 Studies of transferrin at high and low iron saturation. Iron 39-43 transferrin Rattus norvegicus 11-22 1176811-3 1975 The functional heterogeneity of the transferrin iron pool of rats was studied by means of selective radioiron labeling of transferrin at high and low iron saturations. Iron 48-52 transferrin Rattus norvegicus 36-47 1176811-3 1975 The functional heterogeneity of the transferrin iron pool of rats was studied by means of selective radioiron labeling of transferrin at high and low iron saturations. Iron 105-109 transferrin Rattus norvegicus 122-133 1176811-4 1975 A sample of iron-poor plasma transferrin brought to 90 per cent iron saturation by the addition of 59Fe-nitrilotriacetate was mixed with a similarly labeled plasma sample of 55Fe-transferrin at 10 per cent iron saturation. Iron 12-16 transferrin Rattus norvegicus 29-40 954750-2 1976 From determination of their molecular weights, their electrophoretic and iron-binding properties it was established that one was a mucosal ferritin and the other a mucosal transferrin. Iron 73-77 transferrin Rattus norvegicus 172-183 954750-8 1976 Differences were also found in vitro in the iron-binding of mucosal transferrin as compared with plasma transferrin. Iron 44-48 transferrin Rattus norvegicus 68-79 962925-0 1976 Effect of hemin and isonicotinic acid hydrazide on the uptake of iron from transferrin by isolated rat liver mitochondria. Iron 65-69 transferrin Rattus norvegicus 75-86 1236505-0 1975 Uptake of transferrin-bound iron by rat cells in tissue culture. Iron 28-32 transferrin Rattus norvegicus 10-21 1176811-4 1975 A sample of iron-poor plasma transferrin brought to 90 per cent iron saturation by the addition of 59Fe-nitrilotriacetate was mixed with a similarly labeled plasma sample of 55Fe-transferrin at 10 per cent iron saturation. Iron 64-68 transferrin Rattus norvegicus 29-40 1176811-4 1975 A sample of iron-poor plasma transferrin brought to 90 per cent iron saturation by the addition of 59Fe-nitrilotriacetate was mixed with a similarly labeled plasma sample of 55Fe-transferrin at 10 per cent iron saturation. Iron 64-68 transferrin Rattus norvegicus 29-40 1176811-8 1975 These studies add further support for the Fletcher-Huehns hypothesis of the functional heterogeneity of the transferrin iron pool in the rat. Iron 120-124 transferrin Rattus norvegicus 108-119 4250625-0 1970 [Total serum transferrin and iron binding capacity in rats after iron overloads]. Iron 65-69 transferrin Rattus norvegicus 13-24 1123558-0 1975 In vivo evidence for the functional heterogeneity of transferrin-bound iron. Iron 71-75 transferrin Rattus norvegicus 53-64 1123558-3 1975 Functional heterogeneity of iron atoms bound to transferrin as postulated by Fletcher and Huehns was demonstrated by in vivo studies in rats. Iron 28-32 transferrin Rattus norvegicus 48-59 1123558-4 1975 Serum transferrin was selectively double-labeled by adding 59Fe to 90 per cent saturation of iron binding capacity, incubation with rat reticulocytes to reduce the saturation to 50 per cent or less, and then adding back 55Fe. Iron 93-97 transferrin Rattus norvegicus 6-17 1123558-8 1975 These studies confirm the hypothesis of Fletcher and Huehns that the iron atoms of transferrin are functionally different and support the concept that transferrin plays a selective role in the distribution of iron to tissues in the rat. Iron 69-73 transferrin Rattus norvegicus 83-94 1123558-8 1975 These studies confirm the hypothesis of Fletcher and Huehns that the iron atoms of transferrin are functionally different and support the concept that transferrin plays a selective role in the distribution of iron to tissues in the rat. Iron 209-213 transferrin Rattus norvegicus 151-162 1123559-0 1975 In vivo evidence for the functional heterogeneity of transferrin-bound iron. Iron 71-75 transferrin Rattus norvegicus 53-64 1123559-3 1975 Iron atoms from the two iron-binding sites of transferrin in the maternal plasma were selectively transferred to fetal tissues across the placenta of the pregnant rat. Iron 0-4 transferrin Rattus norvegicus 46-57 1123559-3 1975 Iron atoms from the two iron-binding sites of transferrin in the maternal plasma were selectively transferred to fetal tissues across the placenta of the pregnant rat. Iron 24-28 transferrin Rattus norvegicus 46-57 1123559-9 1975 These studies confirm the concept of functional heterogeneity of iron atoms bound to transferrin and indicate that the placenta of rats between the eleventh and twentieth day of pregnancy selectively removes erythroblast-oriented iron from transferrin and diverts it to fetal tissues. Iron 230-234 transferrin Rattus norvegicus 240-251 808936-2 1975 First, an 80% 59Fe-saturated transferrin solution was exposed to reticulocytes to reduce its iron content. Iron 93-97 transferrin Rattus norvegicus 29-40 4471358-0 1974 Interaction of transferrin with iron-binding sites on rat intestinal epithelial cell plasma membranes. Iron 32-36 transferrin Rattus norvegicus 15-26 4983829-0 1969 [Activity of ceruloplasmin, carbonic anhydrase and saturation of transferrin with iron in blood serum of rats developing experimental sarcoma M-1 against a background of E-avitaminosis]. Iron 82-86 transferrin Rattus norvegicus 65-76 5811077-1 1969 In vitro uptake of transferrin-bound iron by rat and rabbit cells. Iron 37-41 transferrin Rattus norvegicus 19-30 33446747-7 2021 After iron supplementation, serum iron, transferrin saturation and serum ferritin levels were increased compared with the IDA group. Iron 6-10 transferrin Rattus norvegicus 40-51 14236554-0 1964 IRON EXCHANGE BETWEEN TRANSFERRIN AND THE PLACENTA IN THE RAT. Iron 0-4 transferrin Rattus norvegicus 22-33 14024217-0 1963 [The role of transferrin in the intestinal absorption of Fe-59 of rats. Iron 57-59 transferrin Rattus norvegicus 13-24 34003408-6 2021 Iron speciation revealed a significant increase in serum transferrin-bound iron and reduced ferritin-bound Fe levels. Iron 0-4 transferrin Rattus norvegicus 57-68 34003408-6 2021 Iron speciation revealed a significant increase in serum transferrin-bound iron and reduced ferritin-bound Fe levels. Iron 75-79 transferrin Rattus norvegicus 57-68 30910397-9 2019 Iron-overload caused a graded increase (p < 0.05) in serum iron, ferritin, transferrin, creatinine, urea, IL-6, TNF-alpha, TAC, MDA and NO levels as well as a reduction in albumin levels, renal SOD and GSH in groups 2 (iron 15 mg/kg) and 3 (iron 30 mg/kg) respectively compared to control. Iron 0-4 transferrin Rattus norvegicus 78-89 32882879-8 2020 The neuroprotective benefits of TF non-viral gene delivery in retinal degenerative disease models further validates iron overload as a therapeutic target and supports the continued development of pEY611 for treatment of RP and dry AMD. Iron 116-120 transferrin Rattus norvegicus 32-34 31339120-8 2019 In addition, compared with FeSO4, APFP-Fe promoted significant weight gain and effectively improved haemoglobin, serum iron and transferrin levels, and recovery of the capacity of iron binding with transferrin, especially at the medium and high doses. Iron 180-184 transferrin Rattus norvegicus 198-209 32124228-8 2020 Iron overload groups increased serum levels of iron, transferrin saturation, and iron deposition in the liver, gastrocnemius muscle, and aorta, and the catalase was overexpressed in the aorta probably as a compensatory mechanism to the increased oxidative stress. Iron 0-4 transferrin Rattus norvegicus 53-64 32882879-2 2020 Transferrin (TF), an endogenous iron chelator, was proposed as a therapeutic candidate. Iron 32-36 transferrin Rattus norvegicus 0-11 31894046-7 2019 It can be concluded that Galacto Oligosaccharides helped enhance the absorption of iron in anemic rats, reflected by increase in serum iron and serum ferritin levels and decrease in serum transferrin and total iron binding capacity. Iron 83-87 transferrin Rattus norvegicus 188-199 29439469-1 2018 A rapid, sensitive and specific ultrafiltration inductively-coupled plasma mass spectrometry (UF-ICP-MSICP-MS) method was developed and validated for the quantification of non-transferrin bound iron (NTBI), transferrin bound iron (TBI), drug bound iron (DI) and total iron (TI) in the same rat serum sample after intravenous (IV) administration of iron gluconate nanoparticles in sucrose solution (Ferrlecit ). Iron 194-198 transferrin Rattus norvegicus 176-187 30833328-0 2019 Proximal tubule transferrin uptake is modulated by cellular iron and mediated by apical membrane megalin-cubilin complex and transferrin receptor 1. Iron 60-64 transferrin Rattus norvegicus 16-27 30279145-0 2018 Detection and quantitation of iron in ferritin, transferrin and labile iron pool (LIP) in cardiomyocytes using 55Fe and storage phosphorimaging. Iron 30-34 transferrin Rattus norvegicus 48-59 30584425-4 2018 Results: Iron overloaded group showed significant increase in serum iron, total iron binding capacity (TIBC), transferrin saturation percentage (TS %) hepcidin (HEPC), serum ferritin, nontransferrin bound iron (NTBI), and small intestinal tissues iron levels. Iron 9-13 transferrin Rattus norvegicus 110-121 30361476-6 2018 Iron therapy increased serum Fe, ferritin and transferrin saturation as well as cardiac and hepatic iron content in HF rats, but did not increase myocardial ferritin. Iron 0-4 transferrin Rattus norvegicus 46-57 29248829-0 2018 Iron-loaded transferrin (Tf) is detrimental whereas iron-free Tf confers protection against brain ischemia by modifying blood Tf saturation and subsequent neuronal damage. Iron 52-56 transferrin Rattus norvegicus 62-64 29248829-0 2018 Iron-loaded transferrin (Tf) is detrimental whereas iron-free Tf confers protection against brain ischemia by modifying blood Tf saturation and subsequent neuronal damage. Iron 52-56 transferrin Rattus norvegicus 62-64 29248829-2 2018 The objective of this study was to obtain evidence on whether TSAT determines the impact of experimental ischemic stroke on brain damage and whether iron-free transferrin (apotransferrin, ATf)-induced reduction of TSAT is neuroprotective. Iron 149-153 transferrin Rattus norvegicus 159-170 29248829-3 2018 We found that experimental ischemic stroke promoted an early extravasation of circulating iron-loaded transferrin (holotransferrin, HTf) to the ischemic brain parenchyma. Iron 90-94 transferrin Rattus norvegicus 102-113 29341909-1 2018 Deferoxamine (DFO) to treat iron overload (IO) has been limited by toxicity issues and short circulation times and it would be desirable to prolong circulation to improve non-transferrin bound iron (NTBI) chelation. Iron 193-197 transferrin Rattus norvegicus 175-186 29248829-0 2018 Iron-loaded transferrin (Tf) is detrimental whereas iron-free Tf confers protection against brain ischemia by modifying blood Tf saturation and subsequent neuronal damage. Iron 0-4 transferrin Rattus norvegicus 12-23 29248829-0 2018 Iron-loaded transferrin (Tf) is detrimental whereas iron-free Tf confers protection against brain ischemia by modifying blood Tf saturation and subsequent neuronal damage. Iron 0-4 transferrin Rattus norvegicus 25-27 29173471-12 2018 Fe deficiency increased TIBC and transferrin levels but reduced ferritin and most haematological parameters. Iron 0-2 transferrin Rattus norvegicus 33-44 28053961-8 2016 However, both alcohol and iron significantly increased hepatic ferritin levels and decreased hepatic transferrin receptor levels (P < 0.05). Iron 26-30 transferrin Rattus norvegicus 101-112 27592288-4 2016 When blood concentrations of glucose are high (as in a diabetic subject), transferrin can be glycated, modifying its ability to bind and transport iron. Iron 147-151 transferrin Rattus norvegicus 74-85 26099311-10 2016 ICH initiated endogenous iron chelators and transporters, both exogenous iron chelators enhanced expression of transferrin and transferrin receptor. Iron 25-29 transferrin Rattus norvegicus 127-138 26099311-10 2016 ICH initiated endogenous iron chelators and transporters, both exogenous iron chelators enhanced expression of transferrin and transferrin receptor. Iron 73-77 transferrin Rattus norvegicus 111-122 26099311-10 2016 ICH initiated endogenous iron chelators and transporters, both exogenous iron chelators enhanced expression of transferrin and transferrin receptor. Iron 73-77 transferrin Rattus norvegicus 127-138 26616369-4 2015 Iron status was displayed by an increase in transferrin saturation (up to 332%) and serum and liver iron burden (up to 19.3 mumol L-1 and 13.2 mumol g-1 wet tissue, respectively) together with a drop in total and unsaturated iron binding capacities "TIBC, UIBC" as surrogate markers of transferrin activity. Iron 0-4 transferrin Rattus norvegicus 44-55 27095095-7 2016 Since oxidative stress is also a general cause of mitochondrial impairment, cells were exposed to test compounds in the presence of transferrin to increase the generation of reactive oxygen species via increased uptake of iron. Iron 222-226 transferrin Rattus norvegicus 132-143 26463963-3 2016 Lipocalin 2 (LCN-2) is a siderophore-binding protein that mediates transferrin-independent iron transport. Iron 91-95 transferrin Rattus norvegicus 67-78 26463975-12 2016 Iron-handling protein levels in the brain, including ceruloplasmin and transferrin, were reduced in the minocycline co-injected animals. Iron 0-4 transferrin Rattus norvegicus 71-82 26523985-5 2015 KEY FINDINGS: Chronic iron administration increased serum iron and transferrin saturation with significant deposition in the liver. Iron 22-26 transferrin Rattus norvegicus 67-78 26978329-6 2016 Interestingly, we found that phosphorylation of Akt by SC79 reduced cell surface transferrin receptor-mediated iron uptake and promoted ferroportin-mediated iron transport after SAH. Iron 111-115 transferrin Rattus norvegicus 81-92 26616369-4 2015 Iron status was displayed by an increase in transferrin saturation (up to 332%) and serum and liver iron burden (up to 19.3 mumol L-1 and 13.2 mumol g-1 wet tissue, respectively) together with a drop in total and unsaturated iron binding capacities "TIBC, UIBC" as surrogate markers of transferrin activity. Iron 0-4 transferrin Rattus norvegicus 286-297 26454080-0 2015 Targeting iron-mediated retinal degeneration by local delivery of transferrin. Iron 10-14 transferrin Rattus norvegicus 66-77 26454080-2 2015 Iron retinal homeostasis is highly regulated and transferrin (Tf), a potent iron chelator, is endogenously secreted by retinal cells. Iron 76-80 transferrin Rattus norvegicus 49-60 26454080-2 2015 Iron retinal homeostasis is highly regulated and transferrin (Tf), a potent iron chelator, is endogenously secreted by retinal cells. Iron 76-80 transferrin Rattus norvegicus 62-64 26454080-6 2015 We found an association between Tf treatment and the modulation of iron homeostasis resulting in a decrease of iron content and oxidative stress marker. Iron 67-71 transferrin Rattus norvegicus 32-34 26454080-6 2015 We found an association between Tf treatment and the modulation of iron homeostasis resulting in a decrease of iron content and oxidative stress marker. Iron 111-115 transferrin Rattus norvegicus 32-34 25649872-4 2015 Zip8, DMT1, and Steap2 co-localize with the transferrin receptor/transferrin complex, suggesting they may be involved in transferrin receptor/transferrin-mediated iron assimilation. Iron 163-167 transferrin Rattus norvegicus 65-76 25115800-4 2015 We demonstrated that hepcidin significantly reduced brain iron in iron-overloaded rats and suppressed transport of transferrin-bound iron (Tf-Fe) from the periphery into the brain. Iron 142-144 transferrin Rattus norvegicus 115-126 25115800-5 2015 Also, the peptide significantly inhibited expression of TfR1, DMT1, and Fpn1 as well as reduced Tf-Fe and non-transferrin-bound iron uptake and iron release in cultured microvascular endothelial cells and neurons, while downregulation of hepcidin with hepcidin siRNA retrovirus generated opposite results. Iron 128-132 transferrin Rattus norvegicus 110-121 26276291-8 2015 CONCLUSIONS: Tf and TfR were important transporters in brain tissue excessive load iron transport after ICH, and detecting the expression levels of the two indicators can provide a reference for prognosis treatment in ICH. Iron 83-87 transferrin Rattus norvegicus 13-15 25649872-4 2015 Zip8, DMT1, and Steap2 co-localize with the transferrin receptor/transferrin complex, suggesting they may be involved in transferrin receptor/transferrin-mediated iron assimilation. Iron 163-167 transferrin Rattus norvegicus 44-55 26209813-6 2015 Further analysis demonstrated that the NO-dependent increase in iron deposition was mediated through increased transferrin receptor expression and a decrease in ferritin expression. Iron 64-68 transferrin Rattus norvegicus 111-122 25649872-5 2015 In brain interstitial fluid, transferring-bound iron (TBI) and non-transferrin-bound iron (NTBI) exist as potential iron sources. Iron 48-52 transferrin Rattus norvegicus 29-40 25649872-6 2015 Primary hippocampal neurons exhibit significant iron uptake from TBI (Transferrin-(59) Fe(3+)) and NTBI, whether presented as (59) Fe(2+) -citrate or (59) Fe(3+) -citrate; reductase-independent (59) Fe(2+) uptake was the most efficient uptake pathway of the three. Iron 48-52 transferrin Rattus norvegicus 70-81 25649872-13 2015 Zip8 and Steap2 are strongly expressed in the plasma membrane of both soma and processes, implying a crucial role in iron accumulation from NTBI and transferrin-bound iron (TBI) by hippocampal neurons. Iron 167-171 transferrin Rattus norvegicus 149-160 25380676-10 2014 Moreover, iron supplementation at high altitudes affected HIF-1alpha-mediated regulating expression of targeting genes such as EPO and transferrin. Iron 10-14 transferrin Rattus norvegicus 135-146 23361852-0 2013 DMT1 as a candidate for non-transferrin-bound iron uptake in the peripheral nervous system. Iron 46-50 transferrin Rattus norvegicus 28-39 26031015-12 2014 The obtained results revealed that, iron overload (IOL) resulted in significant increase in serum iron, TIBC, Tf, TS% and ferritin levels and AST and ALT activities and also increased liver iron, L-MDA and NO levels. Iron 36-40 transferrin Rattus norvegicus 110-112 26031015-14 2014 Rutin administration to iron-overloaded rats resulted in significant decrease in serum total iron, TIBC, Tf, TS%, ferritin levels and AST and ALT activities and liver total iron, L-MDA and NO levels with significant increases in serum UIBC, albumin, total protein and total cholesterol levels and in liver GSH, CAT and SOD activities compared with the IOL group. Iron 24-28 transferrin Rattus norvegicus 105-107 25206866-0 2014 Baicalin suppresses iron accumulation after substantia nigra injury: relationship between iron concentration and transferrin expression. Iron 90-94 transferrin Rattus norvegicus 113-124 23883622-1 2013 Transferrin (Tf), an iron-transporting serum glycoprotein that binds to receptors overexpressed at the surface of glioma cells, was chosen as the ligand to develop Tf-conjugated PEGylated nanoscaled graphene oxide (GO) for loading and glioma targeting delivery of anticancer drug doxorubicin (Dox) (Tf-PEG-GO-Dox). Iron 21-25 transferrin Rattus norvegicus 0-11 23883622-1 2013 Transferrin (Tf), an iron-transporting serum glycoprotein that binds to receptors overexpressed at the surface of glioma cells, was chosen as the ligand to develop Tf-conjugated PEGylated nanoscaled graphene oxide (GO) for loading and glioma targeting delivery of anticancer drug doxorubicin (Dox) (Tf-PEG-GO-Dox). Iron 21-25 transferrin Rattus norvegicus 13-15 23883622-1 2013 Transferrin (Tf), an iron-transporting serum glycoprotein that binds to receptors overexpressed at the surface of glioma cells, was chosen as the ligand to develop Tf-conjugated PEGylated nanoscaled graphene oxide (GO) for loading and glioma targeting delivery of anticancer drug doxorubicin (Dox) (Tf-PEG-GO-Dox). Iron 21-25 transferrin Rattus norvegicus 164-166 23361852-3 2013 Since iron elicits its effect in a transferrin (Tf)-free environment, in this work we postulate that non-transferrin-bound iron (NTBI) uptake must be involved. Iron 6-10 transferrin Rattus norvegicus 35-46 23361852-3 2013 Since iron elicits its effect in a transferrin (Tf)-free environment, in this work we postulate that non-transferrin-bound iron (NTBI) uptake must be involved. Iron 6-10 transferrin Rattus norvegicus 48-50 23361852-3 2013 Since iron elicits its effect in a transferrin (Tf)-free environment, in this work we postulate that non-transferrin-bound iron (NTBI) uptake must be involved. Iron 6-10 transferrin Rattus norvegicus 105-116 23361852-3 2013 Since iron elicits its effect in a transferrin (Tf)-free environment, in this work we postulate that non-transferrin-bound iron (NTBI) uptake must be involved. Iron 60-64 transferrin Rattus norvegicus 48-50 23349308-2 2013 These tissues take up plasma iron from transferrin or non-transferrin-bound iron, which appears during iron overload. Iron 29-33 transferrin Rattus norvegicus 39-50 23349308-2 2013 These tissues take up plasma iron from transferrin or non-transferrin-bound iron, which appears during iron overload. Iron 76-80 transferrin Rattus norvegicus 58-69 23349308-2 2013 These tissues take up plasma iron from transferrin or non-transferrin-bound iron, which appears during iron overload. Iron 76-80 transferrin Rattus norvegicus 58-69 23387277-7 2012 This iron pool content in the interval from the 1st to the 6st day was more than 2 mg/l and significantly higher than the transferrin iron level. Iron 134-138 transferrin Rattus norvegicus 122-133 23349308-3 2013 Here, we assessed the effect of iron status on the levels of the transmembrane transporters, ZRT/IRT-like protein 14 and divalent metal-ion transporter-1, which have both been implicated in transferrin- and non-transferrin-bound iron uptake. Iron 32-36 transferrin Rattus norvegicus 190-201 23349308-3 2013 Here, we assessed the effect of iron status on the levels of the transmembrane transporters, ZRT/IRT-like protein 14 and divalent metal-ion transporter-1, which have both been implicated in transferrin- and non-transferrin-bound iron uptake. Iron 32-36 transferrin Rattus norvegicus 211-222 23349308-3 2013 Here, we assessed the effect of iron status on the levels of the transmembrane transporters, ZRT/IRT-like protein 14 and divalent metal-ion transporter-1, which have both been implicated in transferrin- and non-transferrin-bound iron uptake. Iron 229-233 transferrin Rattus norvegicus 211-222 23399663-5 2013 Plasma iron and transferrin saturation were affected by an interaction between dietary fat and iron. Iron 95-99 transferrin Rattus norvegicus 16-27 24024382-7 2013 CONCLUSION: The nutritional status of the iron may be affected by copper deficiency through influencing the absorption, the results indicate that copper deficiency influences iron homeostasis in cells through affecting the expression of IRP2 and the activity of IRP-RNA combination which change the expressions of ferritin and transferrin mRNA. Iron 42-46 transferrin Rattus norvegicus 327-338 23635304-7 2013 RESULTS: A reduction in maternal liver iron content in response to the low iron diet was associated with upregulation of transferrin receptor expression and a reduction in hepcidin expression in the liver of both strains, which would be expected to promote increased iron absorption across the gut and increased turnover of iron in the liver. Iron 39-43 transferrin Rattus norvegicus 121-132 23635304-7 2013 RESULTS: A reduction in maternal liver iron content in response to the low iron diet was associated with upregulation of transferrin receptor expression and a reduction in hepcidin expression in the liver of both strains, which would be expected to promote increased iron absorption across the gut and increased turnover of iron in the liver. Iron 75-79 transferrin Rattus norvegicus 121-132 23635304-7 2013 RESULTS: A reduction in maternal liver iron content in response to the low iron diet was associated with upregulation of transferrin receptor expression and a reduction in hepcidin expression in the liver of both strains, which would be expected to promote increased iron absorption across the gut and increased turnover of iron in the liver. Iron 75-79 transferrin Rattus norvegicus 121-132 23635304-7 2013 RESULTS: A reduction in maternal liver iron content in response to the low iron diet was associated with upregulation of transferrin receptor expression and a reduction in hepcidin expression in the liver of both strains, which would be expected to promote increased iron absorption across the gut and increased turnover of iron in the liver. Iron 75-79 transferrin Rattus norvegicus 121-132 23635304-8 2013 Placental expression of transferrin and DMT1+IRE were also upregulated, indicating adaptive responses to ensure availability of iron to the fetus. Iron 128-132 transferrin Rattus norvegicus 24-35 24592737-7 2013 Thus, the level of transferrin (Tf, which is responsible for the transport of iron ions, is reduced in 2.5 to 3 times (from 5.0 to 1.6 mg/ml) in the blood plasma, whereas the Tf level in the ascitic fluid increased from 1.5 to 2.7 mg/ml. Iron 78-82 transferrin Rattus norvegicus 19-30 22309085-5 2012 Significantly elevated serum iron and transferrin saturation levels were observed in the ISS groups suggesting a higher release of iron resulting in higher amounts of non-transferrin bound (free) iron compared to IS(ORIG). Iron 131-135 transferrin Rattus norvegicus 38-49 22089858-2 2012 Considerably less is known about the effect of increased plasma levels of redox-reactive non-transferrin bound iron (NTBI) and its impact on pulmonary endothelium. Iron 111-115 transferrin Rattus norvegicus 93-104 22309085-5 2012 Significantly elevated serum iron and transferrin saturation levels were observed in the ISS groups suggesting a higher release of iron resulting in higher amounts of non-transferrin bound (free) iron compared to IS(ORIG). Iron 131-135 transferrin Rattus norvegicus 171-182 22309085-5 2012 Significantly elevated serum iron and transferrin saturation levels were observed in the ISS groups suggesting a higher release of iron resulting in higher amounts of non-transferrin bound (free) iron compared to IS(ORIG). Iron 131-135 transferrin Rattus norvegicus 38-49 22309085-5 2012 Significantly elevated serum iron and transferrin saturation levels were observed in the ISS groups suggesting a higher release of iron resulting in higher amounts of non-transferrin bound (free) iron compared to IS(ORIG). Iron 131-135 transferrin Rattus norvegicus 171-182 21841538-3 2011 We aimed to characterize HO-1-mediated effects on Fe2+ levels in liver and transferrin-bound iron (TFBI) in plasma following HTS, including laparotomy, bleeding, and inadequate and adequate reperfusion. Iron 93-97 transferrin Rattus norvegicus 75-86 22212390-5 2012 IV iron preparations raise plasma non-transferrin-bound iron which can promote oxidative stress, endothelial damage and dysfunction. Iron 3-7 transferrin Rattus norvegicus 38-49 22212390-5 2012 IV iron preparations raise plasma non-transferrin-bound iron which can promote oxidative stress, endothelial damage and dysfunction. Iron 56-60 transferrin Rattus norvegicus 38-49 21841538-10 2011 Transferrin-bound iron levels were affected by pharmacological modulation before shock. Iron 18-22 transferrin Rattus norvegicus 0-11 21770702-4 2011 RESULTS: Molecular plutonium complexes introduced to cell growth media in the form of nitrilotriacetic acid (NTA), citrate, or transferrin complexes were taken up by PC12 cells, and mostly colocalized with iron within the cells. Iron 206-210 transferrin Rattus norvegicus 127-138 21120509-6 2011 Iron accumulation was attributable to prolonged upregulation of the transferrin receptor and to increased uptake of peripheral iron through a leaky blood-brain barrier. Iron 0-4 transferrin Rattus norvegicus 68-79 21851051-7 2011 The obtained data shows that under NO hyperproduction certain changes in iron metabolism take place, such as: the decrease of transferrin iron and the accumulation of ferric iron not bound with transferrin. Iron 73-77 transferrin Rattus norvegicus 126-137 21211566-12 2011 Immunoprecipitates of homogenates of the optic nerve revealed that (59)Fe was precipitable with an antibody raised against ferritin, indicative of detachment of iron from transferrin within the axons of the retinal ganglion cells. Iron 71-73 transferrin Rattus norvegicus 171-182 21851051-7 2011 The obtained data shows that under NO hyperproduction certain changes in iron metabolism take place, such as: the decrease of transferrin iron and the accumulation of ferric iron not bound with transferrin. Iron 73-77 transferrin Rattus norvegicus 194-205 21851051-7 2011 The obtained data shows that under NO hyperproduction certain changes in iron metabolism take place, such as: the decrease of transferrin iron and the accumulation of ferric iron not bound with transferrin. Iron 138-142 transferrin Rattus norvegicus 126-137 20938344-11 2011 Decreased plasma transferrin-bound iron levels were measured in the nonformulated gadodiamide group. Iron 35-39 transferrin Rattus norvegicus 17-28 20015204-3 2011 We suggested that following receptor mediated endocytosis of transferrin filtered by the glomerulus, DMT1 exports iron liberated from transferrin into the cytosol. Iron 114-118 transferrin Rattus norvegicus 61-72 20015204-3 2011 We suggested that following receptor mediated endocytosis of transferrin filtered by the glomerulus, DMT1 exports iron liberated from transferrin into the cytosol. Iron 114-118 transferrin Rattus norvegicus 134-145 20549524-1 2010 Iron and zinc are essential for normal brain function, yet the mechanisms used by astrocytes to scavenge non-transferrin-bound iron (NTBI) and zinc are not well understood. Iron 127-131 transferrin Rattus norvegicus 109-120 20726229-10 2010 Under the condition of copper deficiency, the expression of hepcidin mRNA in liver was lowered and the expression of transferrin receptor mRNA was enhanced through the way of iron response element-iron regulatory protein (IRE-IRP) to regulate iron metabolism. Iron 175-179 transferrin Rattus norvegicus 117-128 20726229-10 2010 Under the condition of copper deficiency, the expression of hepcidin mRNA in liver was lowered and the expression of transferrin receptor mRNA was enhanced through the way of iron response element-iron regulatory protein (IRE-IRP) to regulate iron metabolism. Iron 197-201 transferrin Rattus norvegicus 117-128 19117049-2 2009 Slow and prolonged transdermal delivery of iron would also avoid potential oversaturation of transferrin and overcome accumulation of free iron in the systemic circulation. Iron 43-47 transferrin Rattus norvegicus 93-104 20102755-4 2010 Changes in intracellular iron status were determined by measuring alterations in gene and protein expression of transferrin receptor and ferritin light chain and heavy chain. Iron 25-29 transferrin Rattus norvegicus 112-123 20391109-10 2010 BALF Fe-binding capacity was decreased in SHHF relative to WKY rats and was associated with increased transferrin (Trf) and ferritin. Iron 5-7 transferrin Rattus norvegicus 102-113 20391109-10 2010 BALF Fe-binding capacity was decreased in SHHF relative to WKY rats and was associated with increased transferrin (Trf) and ferritin. Iron 5-7 transferrin Rattus norvegicus 115-118 20338211-0 2010 Effects of carboxylic acids on the uptake of non-transferrin-bound iron by astrocytes. Iron 67-71 transferrin Rattus norvegicus 49-60 20338211-1 2010 The concentrations of non-transferrin-bound iron are elevated in the brain during pathological conditions such as stroke and Alzheimer"s disease. Iron 44-48 transferrin Rattus norvegicus 26-37 19655216-2 2010 Neurons acquire iron through transferrin receptor-mediated endocytosis and via the divalent metal transporter 1 (DMT1). Iron 16-20 transferrin Rattus norvegicus 29-40 18806096-8 2008 Brain Fe deficit and brain transferrin receptor enhancement were eliminated in the Cu- group injected with Fe compared with Cu-S pups, supporting an association between low plasma Fe and low brain Fe. Iron 107-109 transferrin Rattus norvegicus 27-38 19014383-2 2008 For most cell types transferrin is the major iron delivery protein, yet neither transferrin receptor protein nor mRNA are detectable in mature oligodendrocytes. Iron 45-49 transferrin Rattus norvegicus 20-31 19166243-1 2009 Transferrin (Tf), an iron-transporting serum glycoprotein, which binds to receptors expressed at the surface of most proliferating cells with particularly high expression on erythroblasts and cancer cells, was chosen as the ligand to develop BCNU-loaded biodegradable poly(D,L-lactic acid) nanoparticles (NPs) containing a ligand, which specifically binds to glioma cells, and their anti-tumor ability was evaluated using a C6 glioma model. Iron 21-25 transferrin Rattus norvegicus 0-11 18806096-8 2008 Brain Fe deficit and brain transferrin receptor enhancement were eliminated in the Cu- group injected with Fe compared with Cu-S pups, supporting an association between low plasma Fe and low brain Fe. Iron 107-109 transferrin Rattus norvegicus 27-38 18806096-8 2008 Brain Fe deficit and brain transferrin receptor enhancement were eliminated in the Cu- group injected with Fe compared with Cu-S pups, supporting an association between low plasma Fe and low brain Fe. Iron 107-109 transferrin Rattus norvegicus 27-38 18673149-1 2008 Plasma non-transferrin bound iron (NTBI) is potentially toxic and contributes to the generation of reactive oxygen species (ROS), consequently leading to tissue damage and organ dysfunction. Iron 29-33 transferrin Rattus norvegicus 11-22 18549825-2 2008 We previously found that lack of aldose reductase (AR), the first enzyme of the polyol pathway, attenuated the increase in transferrin (Tf) level in I/R brain, suggesting that AR contributes to iron-catalyzed free radical-induced damage. Iron 194-198 transferrin Rattus norvegicus 123-134 18549825-2 2008 We previously found that lack of aldose reductase (AR), the first enzyme of the polyol pathway, attenuated the increase in transferrin (Tf) level in I/R brain, suggesting that AR contributes to iron-catalyzed free radical-induced damage. Iron 194-198 transferrin Rattus norvegicus 136-138 18549825-7 2008 This activates HIF-1alpha that induces the expression of TfR, which in turn increases Tf uptake and iron accumulation and exacerbates oxidative damage that increases the lipid peroxidation. Iron 100-104 transferrin Rattus norvegicus 57-59 18254965-0 2008 Neoplastic transformation of rat liver epithelial cells is enhanced by non-transferrin-bound iron. Iron 93-97 transferrin Rattus norvegicus 75-86 18839536-8 2008 With the increases of iron levels in diet, the levels of serum iron, serum ferretin, and transferrin saturation were gradually increased, and the hepcidin mRNA expression level in liver significantly increased, and the expression of ferroprotin mRNA expression level in duodenum was decreased. Iron 22-26 transferrin Rattus norvegicus 89-100 18515233-4 2008 Besides transferrin iron release, mobilization of ferritin iron is also possible. Iron 20-24 transferrin Rattus norvegicus 8-19 18254965-2 2008 While most iron circulates in blood as transferrin-bound iron, non-transferrin-bound iron (NTBI) also becomes elevated and contributes to toxicity in the setting of iron overload. Iron 11-15 transferrin Rattus norvegicus 39-50 18254965-2 2008 While most iron circulates in blood as transferrin-bound iron, non-transferrin-bound iron (NTBI) also becomes elevated and contributes to toxicity in the setting of iron overload. Iron 57-61 transferrin Rattus norvegicus 39-50 18254965-2 2008 While most iron circulates in blood as transferrin-bound iron, non-transferrin-bound iron (NTBI) also becomes elevated and contributes to toxicity in the setting of iron overload. Iron 57-61 transferrin Rattus norvegicus 39-50 18254965-2 2008 While most iron circulates in blood as transferrin-bound iron, non-transferrin-bound iron (NTBI) also becomes elevated and contributes to toxicity in the setting of iron overload. Iron 57-61 transferrin Rattus norvegicus 39-50 27263618-3 2007 SMF exposure increased the plasma transferrin concentration (+25%, p<0.05) and the capacity of iron saturation in transferrin (+24%, p<0.05). Iron 98-102 transferrin Rattus norvegicus 117-128 17459943-1 2007 Traditionally, transferrin has been considered the primary mechanism for cellular iron delivery, despite suggestive evidence for additional iron delivery mechanisms. Iron 82-86 transferrin Rattus norvegicus 15-26 17503500-5 2007 Tissue iron levels were elevated in senescence, paralleling an increase in transferrin. Iron 7-11 transferrin Rattus norvegicus 75-86 18710026-2 2008 It was established by EPR spectroscopy method that STZ administration reduced transferrin levels in the blood as well as pools of iron associated with blood transferrin and with ferritin in the heart and aorta of rats with hyperglycaemia. Iron 130-134 transferrin Rattus norvegicus 157-168 17628542-1 2007 Transferrin, the iron carrier protein, has been shown to be involved in oligodendroglial cell differentiation in the central nervous system but little is known about its role in the peripheral nervous system. Iron 17-21 transferrin Rattus norvegicus 0-11 16781861-15 2006 Serum total iron binding capacity [transferrin (Tf)] was not changed by Cu deficiency or by Fe supplementation; however, percent Tf saturation was reduced in CuD rats but was not enhanced by Fe supplementation. Iron 12-16 transferrin Rattus norvegicus 35-46 17383861-3 2007 Heart cells have the ability to accumulate transferrin-bound-iron via the transferrin receptor and non-transferrin-bound-iron probably via the L-type Ca2+ channel and the divalent metal transporter1. Iron 61-65 transferrin Rattus norvegicus 43-54 17383861-3 2007 Heart cells have the ability to accumulate transferrin-bound-iron via the transferrin receptor and non-transferrin-bound-iron probably via the L-type Ca2+ channel and the divalent metal transporter1. Iron 61-65 transferrin Rattus norvegicus 74-85 17383861-3 2007 Heart cells have the ability to accumulate transferrin-bound-iron via the transferrin receptor and non-transferrin-bound-iron probably via the L-type Ca2+ channel and the divalent metal transporter1. Iron 61-65 transferrin Rattus norvegicus 74-85 17091493-1 2007 Transferrin receptors (Tfrc) are membrane bound glycoproteins which function to mediate cellular uptake of iron from transferrin. Iron 107-111 transferrin Rattus norvegicus 117-128 17497533-5 2007 We conclude that the reductions in Fe status detected here via the IRP assay arose, in part, from effects on transferrin-mediated Fe3+ delivery to the AM. Iron 35-37 transferrin Rattus norvegicus 109-120 17331953-7 2007 In agreement with the observations in iron-deficient rats, HJV shedding in these cell lines was down-regulated by holo-transferrin in a concentration-dependent manner. Iron 38-42 transferrin Rattus norvegicus 119-130 17373738-0 2007 Evidence for a sequential transfer of iron amongst ferritin, transferrin and transferrin receptor during duodenal absorption of iron in rat and human. Iron 38-42 transferrin Rattus norvegicus 61-72 17373738-0 2007 Evidence for a sequential transfer of iron amongst ferritin, transferrin and transferrin receptor during duodenal absorption of iron in rat and human. Iron 38-42 transferrin Rattus norvegicus 77-88 17373738-0 2007 Evidence for a sequential transfer of iron amongst ferritin, transferrin and transferrin receptor during duodenal absorption of iron in rat and human. Iron 128-132 transferrin Rattus norvegicus 61-72 17373738-0 2007 Evidence for a sequential transfer of iron amongst ferritin, transferrin and transferrin receptor during duodenal absorption of iron in rat and human. Iron 128-132 transferrin Rattus norvegicus 77-88 16879716-0 2006 Brain capillary endothelial cells mediate iron transport into the brain by segregating iron from transferrin without the involvement of divalent metal transporter 1. Iron 42-46 transferrin Rattus norvegicus 97-108 16879716-6 2006 Immunoprecipitation with transferrin antibodies on brains from Belgrade rats revealed lower uptake of transferrin-bound (59)Fe. Iron 124-126 transferrin Rattus norvegicus 25-36 16879716-6 2006 Immunoprecipitation with transferrin antibodies on brains from Belgrade rats revealed lower uptake of transferrin-bound (59)Fe. Iron 124-126 transferrin Rattus norvegicus 102-113 16879716-10 2006 In conclusion, BCECs probably mediate iron transport into the brain by segregating iron from transferrin without involvement of DMT1. Iron 38-42 transferrin Rattus norvegicus 93-104 16819174-0 2006 The involvement of transferrin in the uptake of iron-59 by hepatocytes of carbon tetrachloride-damaged rats. Iron 48-52 transferrin Rattus norvegicus 19-30 16819174-2 2006 It had been reported that the binding affinity of Iron-59 ((59)Fe) to Tf was greater than that of (67)Ga. Iron 50-54 transferrin Rattus norvegicus 70-72 16460863-0 2006 The influence of gallium and other metal ions on the uptake of non-transferrin-bound iron by rat hepatocytes. Iron 85-89 transferrin Rattus norvegicus 67-78 16460863-1 2006 BACKGROUND: Under conditions of iron overload non-transferrin-bound iron (NTBI) occurs in the circulation and is mainly cleared by the liver. Iron 68-72 transferrin Rattus norvegicus 50-61 16460863-9 2006 In iron-loaded cells, inhibition of NTBI uptake by diferric transferrin completely disappeared within 2 hours. Iron 3-7 transferrin Rattus norvegicus 60-71 16728372-1 2006 It was hypothesized that relative mass relationships among select constituent metals and iron (Fe3+) govern the pulmonary immunotoxic potential of any PM(2.5) sample, as these determine the extent to which Fe3+ binding by transferrin is affected (resulting in altered alveolar macrophage [AM] Fe status and subsequent antibacterial function). Iron 95-97 transferrin Rattus norvegicus 222-233 16467964-2 2006 The cleavage results in the release of iron, a regulator of transferrin, ferritin, and nitric oxide (NO) synthase gene expression. Iron 39-43 transferrin Rattus norvegicus 60-71 16137791-1 2005 Divalent metal transporter 1 (DMT1) and transferrin receptor (TfR) might play a key role in non-transferrin-bound iron (NTBI) and transferrin-bound iron (Tf-Fe) uptake by neuronal cells. Iron 148-152 transferrin Rattus norvegicus 40-51 16286684-9 2005 Transferrin saturation in the -Fe and -Zn-Fe groups was significantly lower than the Cont group (p < 0.01), and that of the -Zn group was highest among all groups. Iron 31-33 transferrin Rattus norvegicus 0-11 16137791-1 2005 Divalent metal transporter 1 (DMT1) and transferrin receptor (TfR) might play a key role in non-transferrin-bound iron (NTBI) and transferrin-bound iron (Tf-Fe) uptake by neuronal cells. Iron 157-159 transferrin Rattus norvegicus 40-51 16137791-1 2005 Divalent metal transporter 1 (DMT1) and transferrin receptor (TfR) might play a key role in non-transferrin-bound iron (NTBI) and transferrin-bound iron (Tf-Fe) uptake by neuronal cells. Iron 114-118 transferrin Rattus norvegicus 40-51 16137791-1 2005 Divalent metal transporter 1 (DMT1) and transferrin receptor (TfR) might play a key role in non-transferrin-bound iron (NTBI) and transferrin-bound iron (Tf-Fe) uptake by neuronal cells. Iron 114-118 transferrin Rattus norvegicus 96-107 15699234-11 2005 On day 20, transferrin receptor increased in the low-iron rats, whereas mammary gland iron, ferritin, DMT1, and FPN1 were unchanged. Iron 53-57 transferrin Rattus norvegicus 11-22 15880490-7 2005 However, rat pups with decreased iron and CO exposure (ARIDCO) exhibited in their cochlea an up-regulation of transferrin, whereas their expression of neurofilament proteins and SOD1 were similar to control. Iron 33-37 transferrin Rattus norvegicus 110-121 16164836-4 2005 Blood plasma transferrin is a major carrier of blood iron essential for proliferative "emergency" response of hematopoietic and immune systems as well as injured tissue in major trauma. Iron 53-57 transferrin Rattus norvegicus 13-24 15550752-11 2004 Fe administration raised Hb, serum Fe and transferrin saturation in both CRF and CTL groups. Iron 0-2 transferrin Rattus norvegicus 42-53 15637325-3 2005 This study, therefore, examined whether another iron-containing component of blood, holo-transferrin (holo-Tf), might also induce brain injury either alone or in combination with thrombin, another factor involved in early ICH-induced brain injury. Iron 48-52 transferrin Rattus norvegicus 89-100 15469901-1 2004 Melanotransferrin (MTf) or melanoma tumor antigen p97 is a membrane-bound transferrin (Tf) homologue that binds iron (Fe). Iron 112-116 transferrin Rattus norvegicus 6-17 15469901-1 2004 Melanotransferrin (MTf) or melanoma tumor antigen p97 is a membrane-bound transferrin (Tf) homologue that binds iron (Fe). Iron 118-120 transferrin Rattus norvegicus 6-17 15318094-5 2004 RESULTS: Ethanol exposure to the hepatocytes demonstrated an ~2-fold increase in transferrin receptor expression for 24 hr, shown by Western blot analysis and S-methionine metabolic labeling, 19% increase in Fe-transferrin uptake by hepatocytes, and 20% increase in activity of iron regulatory protein examined by band shift assay. Iron 208-210 transferrin Rattus norvegicus 81-92 15318094-5 2004 RESULTS: Ethanol exposure to the hepatocytes demonstrated an ~2-fold increase in transferrin receptor expression for 24 hr, shown by Western blot analysis and S-methionine metabolic labeling, 19% increase in Fe-transferrin uptake by hepatocytes, and 20% increase in activity of iron regulatory protein examined by band shift assay. Iron 278-282 transferrin Rattus norvegicus 81-92 15318094-7 2004 The induction of transferrin receptor by ethanol might be one of the mechanisms of iron accumulation in the hepatocytes in alcoholic liver disease. Iron 83-87 transferrin Rattus norvegicus 17-28 14598909-6 2003 The Fe-deficient diet also induced an immediate fall in plasma Fe concentration, transferrin saturation, and apparent Fe absorption, while the concentrations of liver cytochrome c increased as Fe deficiency developed. Iron 4-6 transferrin Rattus norvegicus 81-92 15305020-2 2004 In the present study, we investigated whether the entering of indium-111 (111In) and iron-59 (59Fe) with high affinity to transferrin differed from the entering of 67Ga by the hepatocytes after partial hepatectomy. Iron 85-89 transferrin Rattus norvegicus 122-133 15086920-6 2004 Iron administration significantly raised the blood hemoglobin, serum iron concentration, and transferrin saturation in both CRF and control groups. Iron 0-4 transferrin Rattus norvegicus 93-104 15071397-14 2004 These effects were accompanied by a pronounced expression of CD11b in polymorphonuclear leukocytes and tissue sequestration of blood iron-transferrin complexes during the entire 24-hr period of observations. Iron 133-137 transferrin Rattus norvegicus 138-149 15071397-15 2004 The increase in circulatory polymorphonuclear leukocytes was accompanied by a decrease in iron-transferrin complex concentrations that apparently reflected implication of blood plasma iron in the inflammatory cell response to OPW-induced injury. Iron 90-94 transferrin Rattus norvegicus 95-106 15071397-18 2004 The data further suggest that the expression of polymorphonuclear leukocyte CD11b and the response of iron-transferrin complex can be considered as potential surrogate markers in blood for systemic alterations following OPW-induced injury and, therefore, warrant further investigation in a human pilot study. Iron 102-106 transferrin Rattus norvegicus 107-118 15056890-0 2004 Effect of transferrin on enhancing bioavailability of iron. Iron 54-58 transferrin Rattus norvegicus 10-21 15056890-3 2004 With addition of 10 and 20 mg of purified transferrin/ml, however, ratios of absorbed iron through duodenum segments were significantly increased to 52.7 and 57.9%, respectively. Iron 86-90 transferrin Rattus norvegicus 42-53 15056890-5 2004 Results of the animal experiment for comparing bioavailabilities of different irons showed that irons in Fe-transferrin extract was most efficiently absorbed and incorporated into hemoglobin generation in anemic rats. Iron 78-83 transferrin Rattus norvegicus 108-119 15056890-5 2004 Results of the animal experiment for comparing bioavailabilities of different irons showed that irons in Fe-transferrin extract was most efficiently absorbed and incorporated into hemoglobin generation in anemic rats. Iron 96-101 transferrin Rattus norvegicus 108-119 15056890-5 2004 Results of the animal experiment for comparing bioavailabilities of different irons showed that irons in Fe-transferrin extract was most efficiently absorbed and incorporated into hemoglobin generation in anemic rats. Iron 105-107 transferrin Rattus norvegicus 108-119 15056891-5 2004 We observed that the hematocrit (Ht), serum Fe concentration and transferrin saturation (%) were each reduced in those rats fed less than 20 mg/kg Fe in a dose-dependent manner. Iron 147-149 transferrin Rattus norvegicus 65-76 15009675-6 2004 Application of FAC to astrocyte cultures caused a strong increase in the cellular content of the iron storage protein ferritin and a decrease in the amount of transferrin receptor (TfR), which is involved in the transferrin-mediated uptake of iron into cells. Iron 243-247 transferrin Rattus norvegicus 159-170 15013638-1 2004 Transferrin (TF), a 76-80 kDa glycoprotein, is responsible for the transport of iron to cells within both the fetal and maternal systems, but it does not cross the multiple cell layer barrier of the placenta. Iron 80-84 transferrin Rattus norvegicus 0-11 15013638-1 2004 Transferrin (TF), a 76-80 kDa glycoprotein, is responsible for the transport of iron to cells within both the fetal and maternal systems, but it does not cross the multiple cell layer barrier of the placenta. Iron 80-84 transferrin Rattus norvegicus 13-15 15013638-7 2004 When taken together, these results demonstrate clearly that TF is expressed by both differentiated and non-differentiated placental cells, and when viewed in light of previous findings, strengthen the possibility that placental TF may be central to the passage of iron from the mother to the fetus during development. Iron 264-268 transferrin Rattus norvegicus 60-62 15013638-7 2004 When taken together, these results demonstrate clearly that TF is expressed by both differentiated and non-differentiated placental cells, and when viewed in light of previous findings, strengthen the possibility that placental TF may be central to the passage of iron from the mother to the fetus during development. Iron 264-268 transferrin Rattus norvegicus 228-230 14615611-11 2003 CONCLUSIONS: The iron overload and upregulation of iron-handling proteins, including transferrin, transferrin receptor, and ferritin, in the brain after ICH suggest that iron could be a target for ICH therapy. Iron 51-55 transferrin Rattus norvegicus 85-96 14615611-11 2003 CONCLUSIONS: The iron overload and upregulation of iron-handling proteins, including transferrin, transferrin receptor, and ferritin, in the brain after ICH suggest that iron could be a target for ICH therapy. Iron 51-55 transferrin Rattus norvegicus 98-109 14615611-11 2003 CONCLUSIONS: The iron overload and upregulation of iron-handling proteins, including transferrin, transferrin receptor, and ferritin, in the brain after ICH suggest that iron could be a target for ICH therapy. Iron 51-55 transferrin Rattus norvegicus 85-96 14615611-11 2003 CONCLUSIONS: The iron overload and upregulation of iron-handling proteins, including transferrin, transferrin receptor, and ferritin, in the brain after ICH suggest that iron could be a target for ICH therapy. Iron 51-55 transferrin Rattus norvegicus 98-109 15082582-4 2004 RESULTS: Decreased hepatic non-haem iron and transferrin saturation and increased expression of transferrin receptor 1 in the liver indicated a progressive reduction in maternal body iron stores during pregnancy. Iron 183-187 transferrin Rattus norvegicus 96-107 14640978-1 2004 Cells take up transferrin-bound iron or NTBI (non-transferrin-bound iron). Iron 32-36 transferrin Rattus norvegicus 14-25 14640978-1 2004 Cells take up transferrin-bound iron or NTBI (non-transferrin-bound iron). Iron 68-72 transferrin Rattus norvegicus 14-25 14640978-1 2004 Cells take up transferrin-bound iron or NTBI (non-transferrin-bound iron). Iron 68-72 transferrin Rattus norvegicus 50-61 14688618-10 2004 In contrast, in Belgrade rats, whose brain is iron deficient, the expression of both divalent metal transporter 1 and transferrin receptor was increased compared with control in almost all brain regions examined, but not transferrin or ferritin. Iron 46-50 transferrin Rattus norvegicus 118-129 14675167-2 2004 In adult rats, brain uptake of transferrin-bound iron injected intravenously (i.v.) Iron 49-53 transferrin Rattus norvegicus 31-42 14675167-9 2004 Neuronal expression of transferrin receptors and DMT1 in adult rats implies that neurones at this age acquire iron by receptor-mediated endocytosis of transferrin followed by iron transport out of endosomes mediated by DMT1. Iron 110-114 transferrin Rattus norvegicus 23-34 14675167-9 2004 Neuronal expression of transferrin receptors and DMT1 in adult rats implies that neurones at this age acquire iron by receptor-mediated endocytosis of transferrin followed by iron transport out of endosomes mediated by DMT1. Iron 110-114 transferrin Rattus norvegicus 151-162 14675167-9 2004 Neuronal expression of transferrin receptors and DMT1 in adult rats implies that neurones at this age acquire iron by receptor-mediated endocytosis of transferrin followed by iron transport out of endosomes mediated by DMT1. Iron 175-179 transferrin Rattus norvegicus 23-34 21166232-4 2003 RESULTS: As compared with the corresponding sedentary groups, plasma iron and transferrin-iron saturation of three exercise groups were decreased without significant changes of blood hemoglobin and hematocrit. Iron 90-94 transferrin Rattus norvegicus 78-89 12608731-0 2003 Gene expression of transferrin and transferrin receptor in brains of control vs. iron-deficient rats. Iron 81-85 transferrin Rattus norvegicus 19-30 12738232-0 2003 Differential accumulation of non-transferrin-bound iron by cardiac myocytes and fibroblasts. Iron 51-55 transferrin Rattus norvegicus 33-44 12634541-0 2003 Electron paramagnetic resonance analysis of transferrin-bound iron in animal models of blunt trauma. Iron 62-66 transferrin Rattus norvegicus 44-55 12634541-2 2003 The objective of the present research was to assess the effect of iron sequestration in animal models of blunt trauma by means of electron paramagnetic resonance spectroscopy of iron in complex with transferrin, a main iron-transporting protein in blood, and to correlate this effect with the extent of induced injury. Iron 66-70 transferrin Rattus norvegicus 199-210 12707050-10 2003 This suggests that transferrin may be an important factor in the activation of hepatic stellate cells in conditions of iron overload. Iron 119-123 transferrin Rattus norvegicus 19-30 12634541-8 2003 Amounts of transferrin-bound iron (TRF-[Fe3+]) in whole blood and blood plasma samples were measured using quantitative electron paramagnetic resonance spectroscopy. Iron 29-33 transferrin Rattus norvegicus 11-22 12608731-1 2003 The mechanism of the regulation of transferrin (Tf) and transferrin receptor (TfR) levels in rat brain by dietary iron status is not fully elucidated. Iron 114-118 transferrin Rattus norvegicus 35-46 12608731-1 2003 The mechanism of the regulation of transferrin (Tf) and transferrin receptor (TfR) levels in rat brain by dietary iron status is not fully elucidated. Iron 114-118 transferrin Rattus norvegicus 48-50 12608731-3 2003 In a region-specific fashion, iron-deficient diet decreased significantly brain iron concentration by 22-63%, and increased Tf level by 22-130% and TfR level by 74% in thalamus and 40% in cortex. Iron 30-34 transferrin Rattus norvegicus 124-126 12608731-8 2003 This capacity may be associated with increased iron-Tf uptake from plasma, stabilization of TfR mRNA, or increased Tf mRNA translation efficiency in specific cell types within the brain. Iron 47-51 transferrin Rattus norvegicus 52-54 12468600-10 2002 In conclusion, our data suggest that DADS could modify iron homeostasis through the modulation of ferritin and transferrin receptor gene expression. Iron 55-59 transferrin Rattus norvegicus 111-122 12547229-9 2002 The uptake of transferrin-bound iron and expression of functional TfR1 was shown to occur mainly in crypt cells and to be proportional to the plasma concentration of iron. Iron 32-36 transferrin Rattus norvegicus 14-25 12547229-3 2002 In the crypts the cells take up iron from plasma transferrin by receptor-mediated endocytosis, a process that is influenced by the hemochromatosis protein, HFE. Iron 32-36 transferrin Rattus norvegicus 49-60 12547229-4 2002 Hence, the availability of plasma transferrin-bound iron and the expression and function of transferrin receptors (TfR1), HFE and DMT1 should all contribute to the absorptive capacity of villus enterocytes. Iron 52-56 transferrin Rattus norvegicus 34-45 12429868-1 2002 The membrane transferrin receptor-mediated endocytosis or internalization of the complex of transferrin bound iron and the transferrin receptor is the major route of cellular iron uptake. Iron 110-114 transferrin Rattus norvegicus 13-24 12429868-1 2002 The membrane transferrin receptor-mediated endocytosis or internalization of the complex of transferrin bound iron and the transferrin receptor is the major route of cellular iron uptake. Iron 110-114 transferrin Rattus norvegicus 92-103 12429868-1 2002 The membrane transferrin receptor-mediated endocytosis or internalization of the complex of transferrin bound iron and the transferrin receptor is the major route of cellular iron uptake. Iron 175-179 transferrin Rattus norvegicus 13-24 12429868-1 2002 The membrane transferrin receptor-mediated endocytosis or internalization of the complex of transferrin bound iron and the transferrin receptor is the major route of cellular iron uptake. Iron 175-179 transferrin Rattus norvegicus 92-103 12547229-6 2002 In most experiments the function of the TfR1 was assessed by the uptake of radiolabeled transferrin-bound iron given intravenously. Iron 106-110 transferrin Rattus norvegicus 88-99 12547229-9 2002 The uptake of transferrin-bound iron and expression of functional TfR1 was shown to occur mainly in crypt cells and to be proportional to the plasma concentration of iron. Iron 166-170 transferrin Rattus norvegicus 14-25 12553165-2 2002 The significance of the iron for brain function is reflected by the presence of receptors for transferrin on brain capillary endothelial cells. Iron 24-28 transferrin Rattus norvegicus 94-105 12553165-13 2002 Accordingly, it was concluded that the paramount iron transport across the BBB is the result of receptor-mediated endocytosis of iron-containing transferrin by capillary endothelial cells, followed by recycling of transferrin to the blood and transport of non-transferrin-bound iron into the brain. Iron 129-133 transferrin Rattus norvegicus 145-156 12553165-4 2002 Whereas there is good agreement that iron is taken up by means of receptor-mediated uptake of iron-transferrin at the brain barriers, there are contradictory views on how iron is transported further on from the brain barriers and into the brain extracellular space. Iron 37-41 transferrin Rattus norvegicus 99-110 12553165-20 2002 As the choroid plexus is known to synthesize transferrin, a key question is whether transferrin of the CSF might play a role for iron homeostasis by diffusing from the ventricles and subarachnoid space to the brain interstitium. Iron 129-133 transferrin Rattus norvegicus 84-95 12553165-32 2002 Related to these observations, the presence of non-transferrin-bound iron in the brain suggests that glial cells may take it up by a mechanism that does not involve the transferrin receptor. Iron 69-73 transferrin Rattus norvegicus 51-62 12553165-39 2002 For reasons mentioned above, transferrin of the CSF is of little significance for transport and cellular delivery of iron to transferrin receptor-expressing neurons. Iron 117-121 transferrin Rattus norvegicus 125-136 12553165-4 2002 Whereas there is good agreement that iron is taken up by means of receptor-mediated uptake of iron-transferrin at the brain barriers, there are contradictory views on how iron is transported further on from the brain barriers and into the brain extracellular space. Iron 94-98 transferrin Rattus norvegicus 99-110 12553165-40 2002 Instead, transferrin of the CSF probably plays a significant role for neutralization and export to the blood of metals, including iron. Iron 130-134 transferrin Rattus norvegicus 9-20 12553165-43 2002 A developing regulated transfer of iron to the brain was reflected morphologically by a higher content of transferrin receptors and non-heme iron in endothelial cells of the developing rat brain than in the adult. Iron 35-39 transferrin Rattus norvegicus 106-117 12553165-4 2002 Whereas there is good agreement that iron is taken up by means of receptor-mediated uptake of iron-transferrin at the brain barriers, there are contradictory views on how iron is transported further on from the brain barriers and into the brain extracellular space. Iron 94-98 transferrin Rattus norvegicus 99-110 12553165-5 2002 The prevailing hypothesis for transport of iron across the BBB suggests a mechanism that involves detachment of iron from transferrin within barrier cells followed by recycling of apo-transferrin to blood plasma and release of iron as non-transferrin-bound iron into the brain interstitium from where the iron is taken up by neurons and glial cells. Iron 43-47 transferrin Rattus norvegicus 122-133 12553165-5 2002 The prevailing hypothesis for transport of iron across the BBB suggests a mechanism that involves detachment of iron from transferrin within barrier cells followed by recycling of apo-transferrin to blood plasma and release of iron as non-transferrin-bound iron into the brain interstitium from where the iron is taken up by neurons and glial cells. Iron 43-47 transferrin Rattus norvegicus 184-195 12553165-5 2002 The prevailing hypothesis for transport of iron across the BBB suggests a mechanism that involves detachment of iron from transferrin within barrier cells followed by recycling of apo-transferrin to blood plasma and release of iron as non-transferrin-bound iron into the brain interstitium from where the iron is taken up by neurons and glial cells. Iron 43-47 transferrin Rattus norvegicus 184-195 12553165-5 2002 The prevailing hypothesis for transport of iron across the BBB suggests a mechanism that involves detachment of iron from transferrin within barrier cells followed by recycling of apo-transferrin to blood plasma and release of iron as non-transferrin-bound iron into the brain interstitium from where the iron is taken up by neurons and glial cells. Iron 112-116 transferrin Rattus norvegicus 122-133 12553165-5 2002 The prevailing hypothesis for transport of iron across the BBB suggests a mechanism that involves detachment of iron from transferrin within barrier cells followed by recycling of apo-transferrin to blood plasma and release of iron as non-transferrin-bound iron into the brain interstitium from where the iron is taken up by neurons and glial cells. Iron 112-116 transferrin Rattus norvegicus 122-133 12553165-5 2002 The prevailing hypothesis for transport of iron across the BBB suggests a mechanism that involves detachment of iron from transferrin within barrier cells followed by recycling of apo-transferrin to blood plasma and release of iron as non-transferrin-bound iron into the brain interstitium from where the iron is taken up by neurons and glial cells. Iron 112-116 transferrin Rattus norvegicus 122-133 12553165-5 2002 The prevailing hypothesis for transport of iron across the BBB suggests a mechanism that involves detachment of iron from transferrin within barrier cells followed by recycling of apo-transferrin to blood plasma and release of iron as non-transferrin-bound iron into the brain interstitium from where the iron is taken up by neurons and glial cells. Iron 112-116 transferrin Rattus norvegicus 122-133 12553165-6 2002 Another hypothesis claims that iron-transferrin is transported into the brain by means of transcytosis through the BBB. Iron 31-35 transferrin Rattus norvegicus 36-47 12553165-9 2002 The transport of iron and transport into the brain was examined using radiolabeled iron-transferrin. Iron 83-87 transferrin Rattus norvegicus 88-99 12553165-12 2002 It was estimated that the iron-binding capacity of transferrin in CSF was exceeded, suggesting that iron is transported into the brain in a quantity that exceeds that of transferrin. Iron 26-30 transferrin Rattus norvegicus 51-62 12553165-12 2002 It was estimated that the iron-binding capacity of transferrin in CSF was exceeded, suggesting that iron is transported into the brain in a quantity that exceeds that of transferrin. Iron 100-104 transferrin Rattus norvegicus 51-62 12553165-13 2002 Accordingly, it was concluded that the paramount iron transport across the BBB is the result of receptor-mediated endocytosis of iron-containing transferrin by capillary endothelial cells, followed by recycling of transferrin to the blood and transport of non-transferrin-bound iron into the brain. Iron 49-53 transferrin Rattus norvegicus 145-156 12553165-13 2002 Accordingly, it was concluded that the paramount iron transport across the BBB is the result of receptor-mediated endocytosis of iron-containing transferrin by capillary endothelial cells, followed by recycling of transferrin to the blood and transport of non-transferrin-bound iron into the brain. Iron 49-53 transferrin Rattus norvegicus 214-225 12553165-13 2002 Accordingly, it was concluded that the paramount iron transport across the BBB is the result of receptor-mediated endocytosis of iron-containing transferrin by capillary endothelial cells, followed by recycling of transferrin to the blood and transport of non-transferrin-bound iron into the brain. Iron 49-53 transferrin Rattus norvegicus 214-225 12553165-13 2002 Accordingly, it was concluded that the paramount iron transport across the BBB is the result of receptor-mediated endocytosis of iron-containing transferrin by capillary endothelial cells, followed by recycling of transferrin to the blood and transport of non-transferrin-bound iron into the brain. Iron 129-133 transferrin Rattus norvegicus 145-156 12111823-3 2002 It is predominantly located in the white matter and oligodendrocytes, which also actively synthesize the major iron proteins (e.g., ferritin, transferrin). Iron 111-115 transferrin Rattus norvegicus 142-153 12085354-0 2002 Transferrin receptor gene expression and transferrin-bound iron uptake are increased during postischemic rat liver reperfusion. Iron 59-63 transferrin Rattus norvegicus 41-52 12085354-4 2002 We also analyzed transferrin-bound iron uptake into surviving liver slices. Iron 35-39 transferrin Rattus norvegicus 17-28 12085354-9 2002 The increased expression of TfR at the cell surface resulted in increased uptake of transferrin-bound-iron into surviving liver slices; however, iron was not incorporated into ferritin. Iron 102-106 transferrin Rattus norvegicus 84-95 11169456-1 2001 Three mechanisms of iron uptake by rat erythroid cells were identified, two with non-transferrin-bound iron (NTBI) and one with transferrin-bound iron (Fe-Tf). Iron 20-24 transferrin Rattus norvegicus 85-96 11818402-12 2002 Iron accumulation was preceded by Tf degradation, as revealed by immunohistochemistry and Western blot analysis. Iron 0-4 transferrin Rattus norvegicus 34-36 12401947-10 2002 The upregulated expression of transferrin receptors on BCECs in the second and third postnatal week is compatible with a high need for iron at this age. Iron 135-139 transferrin Rattus norvegicus 30-41 12401947-11 2002 The neuronal transferrin receptor expression by P21 coincides with a drop in transferrin-IR and iron transport into the brain at this age, suggesting that neuronal transferrin receptor mRNA is posttranscriptionally regulated by the lowered iron availability from this developmental stage onwards. Iron 96-100 transferrin Rattus norvegicus 13-24 12401947-11 2002 The neuronal transferrin receptor expression by P21 coincides with a drop in transferrin-IR and iron transport into the brain at this age, suggesting that neuronal transferrin receptor mRNA is posttranscriptionally regulated by the lowered iron availability from this developmental stage onwards. Iron 240-244 transferrin Rattus norvegicus 13-24 12401948-4 2002 When expressed as the volume of distribution (Vd), which represents the volume of plasma from which the transferrin and iron were derived, the results for iron were greater than those of transferrin as early as 7 min after injection and the difference increased rapidly with time, especially in the younger animals. Iron 155-159 transferrin Rattus norvegicus 104-115 12401948-5 2002 A very similar time course was found for uptake by bone marrow (femurs) where iron uptake involves receptor-mediated endocytosis of Fe-transferrin, release of iron in the cell and recycling of apo-transferrin to the blood. Iron 78-82 transferrin Rattus norvegicus 135-146 12401948-5 2002 A very similar time course was found for uptake by bone marrow (femurs) where iron uptake involves receptor-mediated endocytosis of Fe-transferrin, release of iron in the cell and recycling of apo-transferrin to the blood. Iron 78-82 transferrin Rattus norvegicus 197-208 12401948-6 2002 It is concluded that, during transport of transferrin-bound plasma iron into the brain, a similar process occurs in brain capillary endothelial cells (BCECs) and that transcytosis of transferrin into the brain interstitium is only a minor pathway. Iron 67-71 transferrin Rattus norvegicus 42-53 12401948-6 2002 It is concluded that, during transport of transferrin-bound plasma iron into the brain, a similar process occurs in brain capillary endothelial cells (BCECs) and that transcytosis of transferrin into the brain interstitium is only a minor pathway. Iron 67-71 transferrin Rattus norvegicus 183-194 12401948-7 2002 Also, the high rate of iron transport into the brain in young animals, when iron requirements are high due to rapid growth of the brain, is a consequence of the level of expression and rate of recycling of transferrin receptors on BCECs. Iron 23-27 transferrin Rattus norvegicus 206-217 12401948-7 2002 Also, the high rate of iron transport into the brain in young animals, when iron requirements are high due to rapid growth of the brain, is a consequence of the level of expression and rate of recycling of transferrin receptors on BCECs. Iron 76-80 transferrin Rattus norvegicus 206-217 11834219-0 2002 Effect of different durations of exercise on transferrin-bound iron uptake by rat erythroblast. Iron 63-67 transferrin Rattus norvegicus 45-56 11834219-3 2002 At the end of experiments, the erythroblasts were isolated for Tf binding assay and transferrin-bound iron (Tf-Fe) uptake. Iron 102-106 transferrin Rattus norvegicus 84-95 11677039-10 2001 In particular, the total iron in the bone marrow was markedly increased at a few hours after the TBI, with a slight increase in transferrin and no increase in ferritin. Iron 25-29 transferrin Rattus norvegicus 128-139 11463361-3 2001 The non-transferrin-bound iron uptake was greater in the NGF-treated cells than in the control, independently of the uptake time, the iron-chelating agents used, the oxidation state of iron (Fe(2+) or Fe(3+)) and the iron concentration tested. Iron 26-30 transferrin Rattus norvegicus 8-19 11331104-1 2001 With alcoholism, there are marked disturbances in iron homeostasis that are linked to alterations in serum transferrin and ferritin concentrations. Iron 50-54 transferrin Rattus norvegicus 107-118 11331104-10 2001 There was a progressive decrease in transferrin iron saturation and ferritin/transferrin ratios for animals fed ethanol in the liquid diet, but not when ethanol was ingested from agar blocks. Iron 48-52 transferrin Rattus norvegicus 36-47 11463361-8 2001 The rate of transferrin-bound iron uptake was less than 1% of the non-transferrin-bound iron uptake and the maximum transferrin-bound iron uptake was also very low. Iron 30-34 transferrin Rattus norvegicus 12-23 11463361-8 2001 The rate of transferrin-bound iron uptake was less than 1% of the non-transferrin-bound iron uptake and the maximum transferrin-bound iron uptake was also very low. Iron 88-92 transferrin Rattus norvegicus 12-23 11463361-8 2001 The rate of transferrin-bound iron uptake was less than 1% of the non-transferrin-bound iron uptake and the maximum transferrin-bound iron uptake was also very low. Iron 88-92 transferrin Rattus norvegicus 70-81 11463361-8 2001 The rate of transferrin-bound iron uptake was less than 1% of the non-transferrin-bound iron uptake and the maximum transferrin-bound iron uptake was also very low. Iron 88-92 transferrin Rattus norvegicus 70-81 11463361-8 2001 The rate of transferrin-bound iron uptake was less than 1% of the non-transferrin-bound iron uptake and the maximum transferrin-bound iron uptake was also very low. Iron 88-92 transferrin Rattus norvegicus 12-23 11463361-8 2001 The rate of transferrin-bound iron uptake was less than 1% of the non-transferrin-bound iron uptake and the maximum transferrin-bound iron uptake was also very low. Iron 88-92 transferrin Rattus norvegicus 70-81 11463361-8 2001 The rate of transferrin-bound iron uptake was less than 1% of the non-transferrin-bound iron uptake and the maximum transferrin-bound iron uptake was also very low. Iron 88-92 transferrin Rattus norvegicus 70-81 11472024-3 2001 In vivo studies with rats have shown that the iron transport protein transferrin serves as the major chromic ion transport agent and that this transport is stimulated by insulin. Iron 46-50 transferrin Rattus norvegicus 69-80 11169456-1 2001 Three mechanisms of iron uptake by rat erythroid cells were identified, two with non-transferrin-bound iron (NTBI) and one with transferrin-bound iron (Fe-Tf). Iron 20-24 transferrin Rattus norvegicus 128-139 11044631-0 2000 Changes of transferrin-free iron uptake by bone marrow erythroblasts in strenuously exercised rats. Iron 28-32 transferrin Rattus norvegicus 11-22 11068183-2 2000 In this study, we examined neuronal and glial cells to clarify which contributes most to metal accumulation after internalization through the transferrin-independent iron uptake (Tf-IU) systems in primary neuronal and glial predominant (NP and GP) cells from rat cerebral cortex, which affect the accumulation of transition metals in a variety of cultured cells. Iron 166-170 transferrin Rattus norvegicus 142-153 10889193-1 2000 Intracellular iron homeostasis is regulated, in part, by interactions between iron-regulatory proteins (IRP1 and IRP2) and iron-responsive elements (IREs) in ferritin and transferrin receptor mRNAs. Iron 14-18 transferrin Rattus norvegicus 171-182 11842873-0 2001 Expression of transferrin mRNA in rat oligodendrocytes is iron-independent and changes with increasing age. Iron 58-62 transferrin Rattus norvegicus 14-25 10906140-0 2000 On the Ca2+ dependence of non-transferrin-bound iron uptake in PC12 cells. Iron 48-52 transferrin Rattus norvegicus 30-41 10906140-1 2000 Non-transferrin-bound iron (NTBI) uptake has been reported to follow two pathways, Ca(2+)-dependent and Ca(2+)-independent (Wright, T. L., Brissot, P., Ma, W. L., and Weisiger, R. A. Iron 22-26 transferrin Rattus norvegicus 4-15 10889193-1 2000 Intracellular iron homeostasis is regulated, in part, by interactions between iron-regulatory proteins (IRP1 and IRP2) and iron-responsive elements (IREs) in ferritin and transferrin receptor mRNAs. Iron 78-82 transferrin Rattus norvegicus 171-182 10921422-5 2000 A similar fall in transferrin-bound plasma iron was also seen. Iron 43-47 transferrin Rattus norvegicus 18-29 10859223-1 2000 Regulation of iron absorption is thought to be mediated by the amount of iron taken up by duodenal crypt cells via the transferrin receptor (TfR)-transferrin cycle and the activity of the divalent metal transporter (DMT1), although DMT1 cannot be detected morphologically in crypt cells. Iron 14-18 transferrin Rattus norvegicus 119-130 10859223-1 2000 Regulation of iron absorption is thought to be mediated by the amount of iron taken up by duodenal crypt cells via the transferrin receptor (TfR)-transferrin cycle and the activity of the divalent metal transporter (DMT1), although DMT1 cannot be detected morphologically in crypt cells. Iron 73-77 transferrin Rattus norvegicus 119-130 10859223-2 2000 We investigated the uptake of transferrin-bound iron by duodenal enterocytes in Wistar rats fed different levels of iron and Belgrade (b/b) rats in which iron uptake by the transferrin cycle is defective because of a mutation in DMT1. Iron 48-52 transferrin Rattus norvegicus 30-41 10859223-4 2000 In all groups the uptake of transferrin-bound iron by crypt cells was directly proportional to plasma iron concentration, being highest in iron-loaded Wistar rats and b/b rats. Iron 46-50 transferrin Rattus norvegicus 28-39 10859223-4 2000 In all groups the uptake of transferrin-bound iron by crypt cells was directly proportional to plasma iron concentration, being highest in iron-loaded Wistar rats and b/b rats. Iron 102-106 transferrin Rattus norvegicus 28-39 10859223-4 2000 In all groups the uptake of transferrin-bound iron by crypt cells was directly proportional to plasma iron concentration, being highest in iron-loaded Wistar rats and b/b rats. Iron 102-106 transferrin Rattus norvegicus 28-39 10859223-5 2000 We conclude that the uptake of transferrin-bound iron by developing enterocytes is largely independent of DMT1. Iron 49-53 transferrin Rattus norvegicus 31-42 10921422-10 2000 The similarity in the degree of fall in transferrin-bound iron levels with a change in diet suggests that iron excretion involves the uptake and excretion of transferrin bound-iron, possibly by goblet cells. Iron 58-62 transferrin Rattus norvegicus 40-51 10921422-10 2000 The similarity in the degree of fall in transferrin-bound iron levels with a change in diet suggests that iron excretion involves the uptake and excretion of transferrin bound-iron, possibly by goblet cells. Iron 58-62 transferrin Rattus norvegicus 158-169 10921422-10 2000 The similarity in the degree of fall in transferrin-bound iron levels with a change in diet suggests that iron excretion involves the uptake and excretion of transferrin bound-iron, possibly by goblet cells. Iron 106-110 transferrin Rattus norvegicus 40-51 10921422-10 2000 The similarity in the degree of fall in transferrin-bound iron levels with a change in diet suggests that iron excretion involves the uptake and excretion of transferrin bound-iron, possibly by goblet cells. Iron 106-110 transferrin Rattus norvegicus 158-169 10921422-10 2000 The similarity in the degree of fall in transferrin-bound iron levels with a change in diet suggests that iron excretion involves the uptake and excretion of transferrin bound-iron, possibly by goblet cells. Iron 106-110 transferrin Rattus norvegicus 40-51 10921422-10 2000 The similarity in the degree of fall in transferrin-bound iron levels with a change in diet suggests that iron excretion involves the uptake and excretion of transferrin bound-iron, possibly by goblet cells. Iron 106-110 transferrin Rattus norvegicus 158-169 10872741-2 2000 In this study, we investigated the roles of TfR in transferrin-bound iron (Tf-Fe) as well as transferrin-free iron (Fe II) uptake by the cells. Iron 110-114 transferrin Rattus norvegicus 93-104 10872741-0 2000 Transferrin-bound and transferrin free iron uptake by cultured rat astrocytes. Iron 39-43 transferrin Rattus norvegicus 22-33 10872741-11 2000 The results of transferrin-free iron uptake indicated that the cultured rat cortical astrocytes had the capacity to acquire Fe II. Iron 32-36 transferrin Rattus norvegicus 15-26 10872741-2 2000 In this study, we investigated the roles of TfR in transferrin-bound iron (Tf-Fe) as well as transferrin-free iron (Fe II) uptake by the cells. Iron 69-73 transferrin Rattus norvegicus 51-62 11961585-1 2000 The changes in transferrin(Tf)-bound and non-Tf-bound iron uptake were observed in bone marrow cells from rats with exercise-induced low iron status. Iron 137-141 transferrin Rattus norvegicus 15-26 10741855-6 2000 Mobilization of iron was also indicated by 49% increase in plasma iron and a 77% increase in plasma transferrin saturation. Iron 16-20 transferrin Rattus norvegicus 100-111 10864004-7 2000 The uptake of transferrin-bound iron (Tf-Fe2) into mucosal cells subsequently separated along the crypt-villus axis was compared to the presence of TfR, determined by immunohistochemistry using frozen and wax sections. Iron 32-36 transferrin Rattus norvegicus 14-25 10690503-3 2000 In plasma and interstitial fluids, Fe is carried by transferrin. Iron 35-37 transferrin Rattus norvegicus 52-63 10827345-14 2000 The iron accumulation in spleen and bone marrow may be related to reduced iron transport due to inhibition of transferrin synthesis rather than inhibition of transferrin sialylation. Iron 4-8 transferrin Rattus norvegicus 110-121 10827345-14 2000 The iron accumulation in spleen and bone marrow may be related to reduced iron transport due to inhibition of transferrin synthesis rather than inhibition of transferrin sialylation. Iron 74-78 transferrin Rattus norvegicus 110-121 10690503-4 2000 Iron-containing transferrin has a high affinity for the transferrin receptor, which is present on all cells with a requirement for Fe. Iron 0-4 transferrin Rattus norvegicus 16-27 10690503-4 2000 Iron-containing transferrin has a high affinity for the transferrin receptor, which is present on all cells with a requirement for Fe. Iron 131-133 transferrin Rattus norvegicus 16-27 10690503-5 2000 The degree of expression of transferrin receptors on most types of cells is determined by the level of Fe supply and their rate of proliferation. Iron 103-105 transferrin Rattus norvegicus 28-39 10690503-15 2000 In the second, Fe transport is the result of receptor-mediated endocytosis of Fe-transferrin by capillary endothelial cells, followed by release of Fe from transferrin within the cell, recycling of transferrin to the blood, and transport of Fe into the brain. Iron 15-17 transferrin Rattus norvegicus 81-92 10690503-15 2000 In the second, Fe transport is the result of receptor-mediated endocytosis of Fe-transferrin by capillary endothelial cells, followed by release of Fe from transferrin within the cell, recycling of transferrin to the blood, and transport of Fe into the brain. Iron 15-17 transferrin Rattus norvegicus 156-167 10690503-15 2000 In the second, Fe transport is the result of receptor-mediated endocytosis of Fe-transferrin by capillary endothelial cells, followed by release of Fe from transferrin within the cell, recycling of transferrin to the blood, and transport of Fe into the brain. Iron 15-17 transferrin Rattus norvegicus 156-167 10690503-15 2000 In the second, Fe transport is the result of receptor-mediated endocytosis of Fe-transferrin by capillary endothelial cells, followed by release of Fe from transferrin within the cell, recycling of transferrin to the blood, and transport of Fe into the brain. Iron 78-80 transferrin Rattus norvegicus 81-92 10690503-15 2000 In the second, Fe transport is the result of receptor-mediated endocytosis of Fe-transferrin by capillary endothelial cells, followed by release of Fe from transferrin within the cell, recycling of transferrin to the blood, and transport of Fe into the brain. Iron 78-80 transferrin Rattus norvegicus 81-92 10690503-19 2000 Iron-containing transferrin is transported through the blood-CSF barrier by a mechanism that appears to be regulated by developmental stage and iron status. Iron 0-4 transferrin Rattus norvegicus 16-27 10690503-19 2000 Iron-containing transferrin is transported through the blood-CSF barrier by a mechanism that appears to be regulated by developmental stage and iron status. Iron 144-148 transferrin Rattus norvegicus 16-27 10690503-24 2000 The uptake of transferrin-bound Fe by neurons and glial cells is probably regulated by the number of transferrin receptors present on cells, which changes during development and in conditions with an altered iron status. Iron 32-34 transferrin Rattus norvegicus 14-25 10690503-24 2000 The uptake of transferrin-bound Fe by neurons and glial cells is probably regulated by the number of transferrin receptors present on cells, which changes during development and in conditions with an altered iron status. Iron 32-34 transferrin Rattus norvegicus 101-112 10690503-24 2000 The uptake of transferrin-bound Fe by neurons and glial cells is probably regulated by the number of transferrin receptors present on cells, which changes during development and in conditions with an altered iron status. Iron 208-212 transferrin Rattus norvegicus 14-25 10690503-24 2000 The uptake of transferrin-bound Fe by neurons and glial cells is probably regulated by the number of transferrin receptors present on cells, which changes during development and in conditions with an altered iron status. Iron 208-212 transferrin Rattus norvegicus 101-112 10674272-13 2000 This indicates that TF may have other functions beyond iron transport. Iron 55-59 transferrin Rattus norvegicus 20-22 10644324-10 2000 CONCLUSIONS: Results are consistent with a role for DMT1 in the transmembrane transport of non-transferrin bound iron from the intestinal lumen and from the portal blood. Iron 113-117 transferrin Rattus norvegicus 95-106 10648828-5 2000 This demonstrates that, after its release from transferrin, iron is transported to the cytoplasm directly from the early endosome without the need for fusion of the iron-containing vesicle with a lysosome. Iron 60-64 transferrin Rattus norvegicus 47-58 10424284-0 1999 Differential response of non-transferrin bound iron uptake in rat liver cells on long-term and short-term treatment with iron. Iron 47-51 transferrin Rattus norvegicus 29-40 10591920-7 1999 The binding of rat [(125)I]transferrin could be competitively and specifically inhibited by unlabeled iron-saturated rat and human transferrin, and no difference was found between interaction of rat or human transferrin with this receptor. Iron 102-106 transferrin Rattus norvegicus 27-38 10693977-0 1999 Aluminum uptake and effects on transferrin mediated iron uptake in primary cultures of rat neurons, astrocytes and oligodendrocytes. Iron 52-56 transferrin Rattus norvegicus 31-42 10693977-1 1999 Transferrin (Tf) is known primarily for its role in the transport and cellular uptake of iron (Fe). Iron 89-93 transferrin Rattus norvegicus 0-11 10693977-1 1999 Transferrin (Tf) is known primarily for its role in the transport and cellular uptake of iron (Fe). Iron 95-97 transferrin Rattus norvegicus 0-11 10529482-3 1999 Changing the iron availability resulted in alterations in plasma and cerebrospinal fluid (CSF) levels of transferrin and iron. Iron 13-17 transferrin Rattus norvegicus 105-116 10529482-4 1999 The iron-binding capacity of transferrin in CSF was exceeded in normal and iron-overloaded rats. Iron 4-8 transferrin Rattus norvegicus 29-40 10529482-4 1999 The iron-binding capacity of transferrin in CSF was exceeded in normal and iron-overloaded rats. Iron 75-79 transferrin Rattus norvegicus 29-40 10440210-10 1999 CONCLUSION: The combined findings of this study were that, in the dietary iron-loaded rat model, increased iron stores were localized to periportal hepatocytes and that these same hepatocytes also had increased ferritin, transferrin receptor and transferrin protein expression. Iron 74-78 transferrin Rattus norvegicus 221-232 10440210-10 1999 CONCLUSION: The combined findings of this study were that, in the dietary iron-loaded rat model, increased iron stores were localized to periportal hepatocytes and that these same hepatocytes also had increased ferritin, transferrin receptor and transferrin protein expression. Iron 107-111 transferrin Rattus norvegicus 221-232 10424284-0 1999 Differential response of non-transferrin bound iron uptake in rat liver cells on long-term and short-term treatment with iron. Iron 121-125 transferrin Rattus norvegicus 29-40 10424284-1 1999 BACKGROUND: Uptake of non-transferrin-bound iron by the liver is important as a clearance mechanism in iron overload. Iron 44-48 transferrin Rattus norvegicus 26-37 10424284-1 1999 BACKGROUND: Uptake of non-transferrin-bound iron by the liver is important as a clearance mechanism in iron overload. Iron 103-107 transferrin Rattus norvegicus 26-37 10424284-3 1999 This study compares the influence of long-term and short-term depletion and loading of hepatocytes with iron on the uptake of non-transferrin bound iron, its affinity, specificity and the interaction with the transferrin-mediated pathways. Iron 104-108 transferrin Rattus norvegicus 130-141 10424284-3 1999 This study compares the influence of long-term and short-term depletion and loading of hepatocytes with iron on the uptake of non-transferrin bound iron, its affinity, specificity and the interaction with the transferrin-mediated pathways. Iron 104-108 transferrin Rattus norvegicus 209-220 10424284-3 1999 This study compares the influence of long-term and short-term depletion and loading of hepatocytes with iron on the uptake of non-transferrin bound iron, its affinity, specificity and the interaction with the transferrin-mediated pathways. Iron 148-152 transferrin Rattus norvegicus 130-141 10424284-3 1999 This study compares the influence of long-term and short-term depletion and loading of hepatocytes with iron on the uptake of non-transferrin bound iron, its affinity, specificity and the interaction with the transferrin-mediated pathways. Iron 148-152 transferrin Rattus norvegicus 209-220 10424284-6 1999 Uptake of non-transferrin bound iron was assayed from ferric citrate and from ferric diethylene triammine pentaacetate. Iron 32-36 transferrin Rattus norvegicus 14-25 10424284-7 1999 RESULTS: Uptake of non-transferrin-bound iron in hepatocytes could be seen as consisting of a high-affinity (Km=600 nM) and a low-affinity component. Iron 41-45 transferrin Rattus norvegicus 23-34 10424284-12 1999 In both cases, uptake of non-transferrin bound iron was inhibited by apotransferrin. Iron 47-51 transferrin Rattus norvegicus 29-40 10424284-13 1999 CONCLUSIONS: Non-transferrin bound iron uptake in liver cells is apparently regulated by the iron status of the liver. Iron 35-39 transferrin Rattus norvegicus 17-28 10424284-13 1999 CONCLUSIONS: Non-transferrin bound iron uptake in liver cells is apparently regulated by the iron status of the liver. Iron 93-97 transferrin Rattus norvegicus 17-28 10217256-2 1999 In the present study, we demonstrate that dopamine promotes the selective sequestration of non-transferrin-derived iron by the mitochondrial compartment of cultured rat astroglia and that the mechanism underlying this novel dopamine effect is oxidative in nature. Iron 115-119 transferrin Rattus norvegicus 95-106 10218886-4 1999 It is suggested that the upregulation of transferrin receptor expression coupled with iron uptake by amoeboid microglial cells in the periventricular regions is a protective mechanism to facilitate the sequestration of excess iron that may have been released either from the iron-rich oligodendrocytes, or accumulated due to a disruption of its normal transportation following the hypoxic insult. Iron 86-90 transferrin Rattus norvegicus 41-52 10218886-4 1999 It is suggested that the upregulation of transferrin receptor expression coupled with iron uptake by amoeboid microglial cells in the periventricular regions is a protective mechanism to facilitate the sequestration of excess iron that may have been released either from the iron-rich oligodendrocytes, or accumulated due to a disruption of its normal transportation following the hypoxic insult. Iron 226-230 transferrin Rattus norvegicus 41-52 10218886-4 1999 It is suggested that the upregulation of transferrin receptor expression coupled with iron uptake by amoeboid microglial cells in the periventricular regions is a protective mechanism to facilitate the sequestration of excess iron that may have been released either from the iron-rich oligodendrocytes, or accumulated due to a disruption of its normal transportation following the hypoxic insult. Iron 226-230 transferrin Rattus norvegicus 41-52 9989781-0 1999 Non-transferrin-bound iron uptake in Belgrade and normal rat erythroid cells. Iron 22-26 transferrin Rattus norvegicus 4-15 10203183-7 1999 CONCLUSIONS: Transferrin is involved in the transport of iron into germ cells and in cell differentiation. Iron 57-61 transferrin Rattus norvegicus 13-24 10082971-2 1999 Transferrin-dependent iron uptake is defective because of a mutation in Nramp2 (now DMT1, also called DCT1), the protein responsible for endosomal iron efflux. Iron 22-26 transferrin Rattus norvegicus 0-11 10082971-2 1999 Transferrin-dependent iron uptake is defective because of a mutation in Nramp2 (now DMT1, also called DCT1), the protein responsible for endosomal iron efflux. Iron 147-151 transferrin Rattus norvegicus 0-11 9989781-2 1999 Transferrin (Tf)-dependent iron uptake is defective because of a mutation in DMT1 (Nramp2), blocking endosomal iron efflux. Iron 27-31 transferrin Rattus norvegicus 0-11 9989781-2 1999 Transferrin (Tf)-dependent iron uptake is defective because of a mutation in DMT1 (Nramp2), blocking endosomal iron efflux. Iron 27-31 transferrin Rattus norvegicus 13-15 9989781-2 1999 Transferrin (Tf)-dependent iron uptake is defective because of a mutation in DMT1 (Nramp2), blocking endosomal iron efflux. Iron 111-115 transferrin Rattus norvegicus 0-11 9989781-2 1999 Transferrin (Tf)-dependent iron uptake is defective because of a mutation in DMT1 (Nramp2), blocking endosomal iron efflux. Iron 111-115 transferrin Rattus norvegicus 13-15 9989781-3 1999 This experiment of nature permits the present study to address whether the mutation also affects non-Tf-bound iron (NTBI) uptake and to use NTBI uptake compared to Tf-Fe utilization to increase understanding of the phenotype of the b mutation. Iron 110-114 transferrin Rattus norvegicus 101-103 9989781-3 1999 This experiment of nature permits the present study to address whether the mutation also affects non-Tf-bound iron (NTBI) uptake and to use NTBI uptake compared to Tf-Fe utilization to increase understanding of the phenotype of the b mutation. Iron 167-169 transferrin Rattus norvegicus 164-166 9989781-11 1999 DMT1 serves in both apparent high-affinity NTBI membrane transport and the exit of iron from the endosome during Tf delivery of iron in rat reticulocytes; the low-affinity membrane transporter, however, exhibits little dependence on DMT1. Iron 128-132 transferrin Rattus norvegicus 113-115 9914507-1 1999 Iron regulatory proteins (IRP)-1 and 2 are cytoplasmic mRNA-binding proteins that control intracellular iron homeostasis by regulating the translation of ferritin mRNA and stability of transferrin receptor mRNA in an iron-dependent fashion. Iron 104-108 transferrin Rattus norvegicus 185-196 9972870-1 1999 It has been established that oligodendrocytes, the myelin forming cells, participate in iron homeostasis through the synthesis and secretion of transferrin. Iron 88-92 transferrin Rattus norvegicus 144-155 9914507-1 1999 Iron regulatory proteins (IRP)-1 and 2 are cytoplasmic mRNA-binding proteins that control intracellular iron homeostasis by regulating the translation of ferritin mRNA and stability of transferrin receptor mRNA in an iron-dependent fashion. Iron 217-221 transferrin Rattus norvegicus 185-196 9702705-4 1998 Bound transferrin was 280 micrograms/mg of iron. Iron 43-47 transferrin Rattus norvegicus 6-17 10366015-4 1999 The transferrin receptor has been implicated as a possible mediator of this iron accumulation in the parkinsonian substantia nigra. Iron 76-80 transferrin Rattus norvegicus 4-15 9822159-0 1998 Evidence for low molecular weight, non-transferrin-bound iron in rat brain and cerebrospinal fluid. Iron 57-61 transferrin Rattus norvegicus 39-50 9822159-1 1998 Transferrin (Tf) donates iron (Fe) to the brain by means of receptor-mediated endocytosis of Tf at the brain barriers. Iron 25-29 transferrin Rattus norvegicus 0-11 9822159-1 1998 Transferrin (Tf) donates iron (Fe) to the brain by means of receptor-mediated endocytosis of Tf at the brain barriers. Iron 25-29 transferrin Rattus norvegicus 13-15 9822159-1 1998 Transferrin (Tf) donates iron (Fe) to the brain by means of receptor-mediated endocytosis of Tf at the brain barriers. Iron 25-29 transferrin Rattus norvegicus 93-95 9822159-1 1998 Transferrin (Tf) donates iron (Fe) to the brain by means of receptor-mediated endocytosis of Tf at the brain barriers. Iron 31-33 transferrin Rattus norvegicus 0-11 9822159-1 1998 Transferrin (Tf) donates iron (Fe) to the brain by means of receptor-mediated endocytosis of Tf at the brain barriers. Iron 31-33 transferrin Rattus norvegicus 13-15 9822159-1 1998 Transferrin (Tf) donates iron (Fe) to the brain by means of receptor-mediated endocytosis of Tf at the brain barriers. Iron 31-33 transferrin Rattus norvegicus 93-95 9822159-2 1998 As Tf transport through the brain barriers is restricted, Fe is probably released into the brain extracellular compartment as non-Tf-bound iron (NTBI). Iron 58-60 transferrin Rattus norvegicus 130-132 9822159-6 1998 Measurements of Fe and Tf concentrations in CSF of P20 rats revealed that the Fe-binding capacity of Tf was exceeded. Iron 16-18 transferrin Rattus norvegicus 101-103 9822159-6 1998 Measurements of Fe and Tf concentrations in CSF of P20 rats revealed that the Fe-binding capacity of Tf was exceeded. Iron 78-80 transferrin Rattus norvegicus 23-25 9822159-6 1998 Measurements of Fe and Tf concentrations in CSF of P20 rats revealed that the Fe-binding capacity of Tf was exceeded. Iron 78-80 transferrin Rattus norvegicus 101-103 11186208-0 1998 Characterization of a transferrin-independent iron uptake system in rat primary cultured cortical cells. Iron 46-50 transferrin Rattus norvegicus 22-33 9578471-11 1998 Incubations carried out using 55Fe-labelled citrate in the presence of 59Fe-labelled diferric transferrin indicated that citrate-mediated iron binding by the cells decreased with increasing diferric transferrin concentrations but the citrate iron was not replaced by iron from transferrin during the 15-min incubation period. Iron 138-142 transferrin Rattus norvegicus 199-210 9639675-2 1998 A chlorpromazine stimulatory effect upon iron uptake from 55Fe-citrate and 55Fe-transferrin by cortical synaptosome preparations of rats was recently demonstrated. Iron 41-45 transferrin Rattus norvegicus 80-91 9578471-11 1998 Incubations carried out using 55Fe-labelled citrate in the presence of 59Fe-labelled diferric transferrin indicated that citrate-mediated iron binding by the cells decreased with increasing diferric transferrin concentrations but the citrate iron was not replaced by iron from transferrin during the 15-min incubation period. Iron 138-142 transferrin Rattus norvegicus 199-210 9578471-13 1998 These data suggest that citrate-mediated iron uptake by hepatocytes shares at least one common pathway with transferrin-mediated iron uptake. Iron 129-133 transferrin Rattus norvegicus 108-119 9537448-6 1998 We also demonstrate exchange of iron between DTPA and holo-transferrin, or at least movement from the chelator to the protein, which may have lost its iron to the cell in advance, providing new binding sites for mobilized iron. Iron 32-36 transferrin Rattus norvegicus 59-70 9537448-6 1998 We also demonstrate exchange of iron between DTPA and holo-transferrin, or at least movement from the chelator to the protein, which may have lost its iron to the cell in advance, providing new binding sites for mobilized iron. Iron 151-155 transferrin Rattus norvegicus 59-70 9537448-6 1998 We also demonstrate exchange of iron between DTPA and holo-transferrin, or at least movement from the chelator to the protein, which may have lost its iron to the cell in advance, providing new binding sites for mobilized iron. Iron 151-155 transferrin Rattus norvegicus 59-70 9537448-10 1998 We conclude that this activity represents a hitherto unidentified first step in the movement of iron through the cell membrane and may be relevant for transferrin-bound, as well as for non-transferrin-bound, iron uptake by hepatocytes. Iron 96-100 transferrin Rattus norvegicus 151-162 9537448-10 1998 We conclude that this activity represents a hitherto unidentified first step in the movement of iron through the cell membrane and may be relevant for transferrin-bound, as well as for non-transferrin-bound, iron uptake by hepatocytes. Iron 96-100 transferrin Rattus norvegicus 189-200 9537448-10 1998 We conclude that this activity represents a hitherto unidentified first step in the movement of iron through the cell membrane and may be relevant for transferrin-bound, as well as for non-transferrin-bound, iron uptake by hepatocytes. Iron 208-212 transferrin Rattus norvegicus 189-200 9469483-7 1998 Reduced transferrin receptor internalization may limit lymphocyte expansion by depleting the intracellular iron stores needed for cellular function and proliferation. Iron 107-111 transferrin Rattus norvegicus 8-19 9448300-2 1998 The b reticulocyte defect appears to be failure of iron transport out of endosomes within the transferrin cycle. Iron 51-55 transferrin Rattus norvegicus 94-105 9448300-12 1998 Furthermore, the phenotypic characteristics of these animals indicate that Nramp2 is essential both for normal intestinal iron absorption and for transport of iron out of the transferrin cycle endosome. Iron 159-163 transferrin Rattus norvegicus 175-186 9504407-0 1998 Aluminum taken up by transferrin-independent iron uptake affects the iron metabolism in rat cortical cells. Iron 69-73 transferrin Rattus norvegicus 21-32 9578471-3 1998 Consequently, the liver, which is the major site of iron storage, will be presented with iron in both transferrin-bound and non-transferrin-bound forms and these forms may compete for uptake by hepatocytes. Iron 52-56 transferrin Rattus norvegicus 102-113 9578471-3 1998 Consequently, the liver, which is the major site of iron storage, will be presented with iron in both transferrin-bound and non-transferrin-bound forms and these forms may compete for uptake by hepatocytes. Iron 89-93 transferrin Rattus norvegicus 102-113 9578471-3 1998 Consequently, the liver, which is the major site of iron storage, will be presented with iron in both transferrin-bound and non-transferrin-bound forms and these forms may compete for uptake by hepatocytes. Iron 89-93 transferrin Rattus norvegicus 128-139 9578471-4 1998 The endogenous low-molecular-mass iron chelator, citrate, is considered to be a major contributing molecule to non-transferrin iron transport. Iron 34-38 transferrin Rattus norvegicus 115-126 9578471-7 1998 Binding and internalisation of both citrate and iron were inhibited in a dose-dependent manner with increasing concentration of diferric transferrin, with iron uptake decreasing to less than 5% of control values. Iron 48-52 transferrin Rattus norvegicus 137-148 9578471-7 1998 Binding and internalisation of both citrate and iron were inhibited in a dose-dependent manner with increasing concentration of diferric transferrin, with iron uptake decreasing to less than 5% of control values. Iron 155-159 transferrin Rattus norvegicus 137-148 9578471-11 1998 Incubations carried out using 55Fe-labelled citrate in the presence of 59Fe-labelled diferric transferrin indicated that citrate-mediated iron binding by the cells decreased with increasing diferric transferrin concentrations but the citrate iron was not replaced by iron from transferrin during the 15-min incubation period. Iron 138-142 transferrin Rattus norvegicus 94-105 9545519-0 1998 Characterisation of non-transferrin-bound iron (ferric citrate) uptake by rat hepatocytes in culture. Iron 42-46 transferrin Rattus norvegicus 24-35 9545519-1 1998 Under conditions of iron overload plasma transferrin can be fully saturated and the plasma can transport non-transferrin-bound Fe which is rapidly cleared by the liver. Iron 20-24 transferrin Rattus norvegicus 41-52 9545519-1 1998 Under conditions of iron overload plasma transferrin can be fully saturated and the plasma can transport non-transferrin-bound Fe which is rapidly cleared by the liver. Iron 127-129 transferrin Rattus norvegicus 109-120 9545519-11 1998 These experiments show that rat hepatocytes in primary culture have a high capacity to take up non-transferrin-bound Fe in the form of Fe-citrate and that uptake occurs by facilitated diffusion. Iron 117-119 transferrin Rattus norvegicus 99-110 9502420-0 1998 Accumulation of iron by primary rat hepatocytes in long-term culture: changes in nuclear shape mediated by non-transferrin-bound forms of iron. Iron 138-142 transferrin Rattus norvegicus 111-122 9502420-2 1998 Hepatocytes in long-term DMSO culture can be iron loaded by exposure to non-transferrin-bound iron (NTBI) in the form of ferrous sulfate (FeSO4), ferric nitrilotriacetate, or trimethylhexanoyl (TMH)-ferrocene. Iron 45-49 transferrin Rattus norvegicus 76-87 9502420-2 1998 Hepatocytes in long-term DMSO culture can be iron loaded by exposure to non-transferrin-bound iron (NTBI) in the form of ferrous sulfate (FeSO4), ferric nitrilotriacetate, or trimethylhexanoyl (TMH)-ferrocene. Iron 94-98 transferrin Rattus norvegicus 76-87 9406656-2 1997 Proximal tubular cell dysfunction in chronic glomerular disease (CGD) has been ascribed, in part, to reabsorption of transferrin-iron from tubular fluid and subsequent cytosolic peroxidative injury. Iron 129-133 transferrin Rattus norvegicus 117-128 9504894-4 1997 As an example, the uptake of transferrin-bound iron by enterocytes was studied. Iron 47-51 transferrin Rattus norvegicus 29-40 9504894-12 1997 Uptake of transferrin-bound iron into enterocytes was highest with feeding an iron-loaded diet compared with control or iron-deficient diets. Iron 28-32 transferrin Rattus norvegicus 10-21 9504894-12 1997 Uptake of transferrin-bound iron into enterocytes was highest with feeding an iron-loaded diet compared with control or iron-deficient diets. Iron 78-82 transferrin Rattus norvegicus 10-21 9504894-12 1997 Uptake of transferrin-bound iron into enterocytes was highest with feeding an iron-loaded diet compared with control or iron-deficient diets. Iron 78-82 transferrin Rattus norvegicus 10-21 9486090-2 1997 The extracellular proteins caeruloplasmin and transferrin have important antioxidant properties by virtue of the fact that they inhibit iron-dependent free radical production, and ensuing damage to cells. Iron 136-140 transferrin Rattus norvegicus 46-57 9432136-8 1997 Since transferrin secreted by Sertoli cells is an important molecule in maintaining the crucial iron level necessary for spermatogenesis, the identification of haptoglobin as a Sertoli and germ cell product adds a new member to the growing family of metal transporters in the testis that are likely to play an important role in iron metabolism in the testis. Iron 96-100 transferrin Rattus norvegicus 6-17 9353884-2 1997 Transferrin and transferrin receptors play an important role in the transport of iron into the brain. Iron 81-85 transferrin Rattus norvegicus 0-11 9353884-2 1997 Transferrin and transferrin receptors play an important role in the transport of iron into the brain. Iron 81-85 transferrin Rattus norvegicus 16-27 9290151-9 1997 In these experiments, there was a close correspondence between the amount of iron accumulated by the embryo and visceral yolk sac in the final 24 h of a 51-h culture and the amount of transferrin converted into acid-soluble products in the same period. Iron 77-81 transferrin Rattus norvegicus 184-195 9316467-5 1997 Transferrin receptor activity was determined by the uptake of intravenously injected transferrin-bound iron and was shown to increase with the level of iron loading. Iron 103-107 transferrin Rattus norvegicus 0-11 9316467-5 1997 Transferrin receptor activity was determined by the uptake of intravenously injected transferrin-bound iron and was shown to increase with the level of iron loading. Iron 103-107 transferrin Rattus norvegicus 85-96 9316467-5 1997 Transferrin receptor activity was determined by the uptake of intravenously injected transferrin-bound iron and was shown to increase with the level of iron loading. Iron 152-156 transferrin Rattus norvegicus 0-11 9316467-5 1997 Transferrin receptor activity was determined by the uptake of intravenously injected transferrin-bound iron and was shown to increase with the level of iron loading. Iron 152-156 transferrin Rattus norvegicus 85-96 9290151-11 1997 The results indicate that transferrin delivers iron for incorporation into both the embryo and the visceral yolk sac, and are consistent with a mechanism involving receptor-mediated endocytosis of iron-laden transferrin by the cells of the visceral yolk sac. Iron 47-51 transferrin Rattus norvegicus 26-37 9290151-11 1997 The results indicate that transferrin delivers iron for incorporation into both the embryo and the visceral yolk sac, and are consistent with a mechanism involving receptor-mediated endocytosis of iron-laden transferrin by the cells of the visceral yolk sac. Iron 197-201 transferrin Rattus norvegicus 26-37 9290151-11 1997 The results indicate that transferrin delivers iron for incorporation into both the embryo and the visceral yolk sac, and are consistent with a mechanism involving receptor-mediated endocytosis of iron-laden transferrin by the cells of the visceral yolk sac. Iron 197-201 transferrin Rattus norvegicus 208-219 9290151-12 1997 The transferrin itself appears to be quantitatively degraded, following delivery of iron to the yolk sac cells, a result that differs from findings in other cell types, in which the protein is not degraded but returns to the plasma membrane to participate in further cycles of iron acquisition and delivery. Iron 84-88 transferrin Rattus norvegicus 4-15 9290151-12 1997 The transferrin itself appears to be quantitatively degraded, following delivery of iron to the yolk sac cells, a result that differs from findings in other cell types, in which the protein is not degraded but returns to the plasma membrane to participate in further cycles of iron acquisition and delivery. Iron 277-281 transferrin Rattus norvegicus 4-15 9278862-2 1997 Because these cells have no direct access to systemic iron, there exists a shuttle system involving production and secretion of the iron-transporting protein transferrin by the Sertoli cells. Iron 54-58 transferrin Rattus norvegicus 158-169 9292281-11 1997 5 As the plasma transferrin concentration did not change over the experimental period, the concentration of absorbed iron in the mesenteric plasma exceeded the iron-binding capacity of plasma transferrin at low blood flow rates. Iron 117-121 transferrin Rattus norvegicus 16-27 9292281-11 1997 5 As the plasma transferrin concentration did not change over the experimental period, the concentration of absorbed iron in the mesenteric plasma exceeded the iron-binding capacity of plasma transferrin at low blood flow rates. Iron 160-164 transferrin Rattus norvegicus 192-203 9231702-6 1997 Iron crosses the luminal membrane of the capillary endothelium by receptor-mediated endocytosis of ferric transferrin. Iron 0-4 transferrin Rattus norvegicus 106-117 9231702-15 1997 Within interstitial fluid, transported iron will bind with any unsaturated transferrin synthesized or transported into the brain-CSF system. Iron 39-43 transferrin Rattus norvegicus 75-86 9278862-2 1997 Because these cells have no direct access to systemic iron, there exists a shuttle system involving production and secretion of the iron-transporting protein transferrin by the Sertoli cells. Iron 132-136 transferrin Rattus norvegicus 158-169 9221832-10 1997 One of the most striking effects of cadmium loading on iron metabolism was increased uptake of [125I]transferrin by the heart, possibly by disrupting the process of receptor-mediated endocytosis and recycling of transferrin by heart muscle. Iron 55-59 transferrin Rattus norvegicus 101-112 9282313-0 1997 Effects of iron chelates on the transferrin-free culture of rat dermal fibroblasts through active oxygen generation. Iron 11-15 transferrin Rattus norvegicus 32-43 9282313-4 1997 Iron may be essential for survival of fibroblasts because subconfluent fibroblasts exposed to 100 microM FeSO4 in combination with transferrin, HEPES, or GG significantly decreased to release lactate dehydrogenase into the medium. Iron 0-4 transferrin Rattus norvegicus 131-142 9252093-0 1997 Novel orally active iron chelators (3-hydroxypyridin-4-ones) enhance the biliary excretion of plasma non-transferrin-bound iron in rats. Iron 20-24 transferrin Rattus norvegicus 105-116 9252093-0 1997 Novel orally active iron chelators (3-hydroxypyridin-4-ones) enhance the biliary excretion of plasma non-transferrin-bound iron in rats. Iron 123-127 transferrin Rattus norvegicus 105-116 9252093-1 1997 BACKGROUND/AIMS: It is well documented that levels of plasma non-transferrin-bound iron (NTBI), a particularly toxic form of iron, are increased in iron overload disorders. Iron 83-87 transferrin Rattus norvegicus 65-76 9252093-1 1997 BACKGROUND/AIMS: It is well documented that levels of plasma non-transferrin-bound iron (NTBI), a particularly toxic form of iron, are increased in iron overload disorders. Iron 125-129 transferrin Rattus norvegicus 65-76 9221832-10 1997 One of the most striking effects of cadmium loading on iron metabolism was increased uptake of [125I]transferrin by the heart, possibly by disrupting the process of receptor-mediated endocytosis and recycling of transferrin by heart muscle. Iron 55-59 transferrin Rattus norvegicus 212-223 8804698-13 1996 These findings, taken together with previously published data on the distribution of ferritin and transferrin, suggests that iron-enriched cells serve as stores of iron for the brain. Iron 125-129 transferrin Rattus norvegicus 98-109 9185768-0 1997 Intestinal absorption and enterohepatic cycling of biliary iron originating from plasma non-transferrin-bound iron in rats. Iron 59-63 transferrin Rattus norvegicus 92-103 9185768-0 1997 Intestinal absorption and enterohepatic cycling of biliary iron originating from plasma non-transferrin-bound iron in rats. Iron 110-114 transferrin Rattus norvegicus 92-103 9185768-1 1997 In iron overload, non-transferrin-bound iron (NTBI) is found in plasma and is rapidly removed by hepatocytes. Iron 3-7 transferrin Rattus norvegicus 22-33 9185768-1 1997 In iron overload, non-transferrin-bound iron (NTBI) is found in plasma and is rapidly removed by hepatocytes. Iron 40-44 transferrin Rattus norvegicus 22-33 9185768-10 1997 We conclude that biliary iron, originating from NTBI, is absorbed from the intestine, and undergoes enterohepatic circulation if transferrin is saturated. Iron 25-29 transferrin Rattus norvegicus 129-140 8915458-0 1996 Effects of dietary iron loading with carbonyl iron and of iron depletion on intestinal growth, morphology, and expression of transferrin receptor in the rat. Iron 19-23 transferrin Rattus norvegicus 125-136 8889033-1 1996 We have reported that di-n-butyl phthalate (DBP) caused the depletion of circulating iron, characterized by the release of iron from both haemoglobin (Hb) and transferrin (Tf). Iron 85-89 transferrin Rattus norvegicus 159-170 8889033-1 1996 We have reported that di-n-butyl phthalate (DBP) caused the depletion of circulating iron, characterized by the release of iron from both haemoglobin (Hb) and transferrin (Tf). Iron 85-89 transferrin Rattus norvegicus 172-174 8889033-1 1996 We have reported that di-n-butyl phthalate (DBP) caused the depletion of circulating iron, characterized by the release of iron from both haemoglobin (Hb) and transferrin (Tf). Iron 123-127 transferrin Rattus norvegicus 159-170 8889033-1 1996 We have reported that di-n-butyl phthalate (DBP) caused the depletion of circulating iron, characterized by the release of iron from both haemoglobin (Hb) and transferrin (Tf). Iron 123-127 transferrin Rattus norvegicus 172-174 8889033-3 1996 In the in vivo study, there were observed depletions of Hb in the blood and of iron in the hepatic Tf fraction, as well as an accumulation of iron in the hepatic hemosiderin (Hs) and splenic Tf fractions. Iron 79-83 transferrin Rattus norvegicus 99-101 8889033-4 1996 In the in vitro study, mono-butyl phthalate (MBP), a metabolite of DBP, caused a depletion of iron in the plasma Tf, although a direct release of iron from Tf was not detectable. Iron 94-98 transferrin Rattus norvegicus 113-115 8889033-4 1996 In the in vitro study, mono-butyl phthalate (MBP), a metabolite of DBP, caused a depletion of iron in the plasma Tf, although a direct release of iron from Tf was not detectable. Iron 146-150 transferrin Rattus norvegicus 156-158 8806910-6 1996 Hyperoxia increased the amount of the nonsedimentable protein, whereas NO increased the iron saturation of transferrin. Iron 88-92 transferrin Rattus norvegicus 107-118 8611022-4 1996 Iron uptake from Fe(III)-DTPA is completely inhibited by trypsinization of the cell surface, by strong impermeant ferric chelators (DTPA, apo-transferrin, polymer-conjugated desferrioxamine), both hexacyanoferrates, copper and zinc, and partly by dipyridyl, manganese, cobalt, N-ethylmaleimide, and citrate. Iron 0-4 transferrin Rattus norvegicus 142-153 8782865-1 1996 Transferrin (Tf) is a major transport protein for both iron (Fe) and aluminum (Al), as well as manganese (Mn) and it can mediate cellular uptake of these elements via cell surface Tf receptors. Iron 55-59 transferrin Rattus norvegicus 0-11 8782865-1 1996 Transferrin (Tf) is a major transport protein for both iron (Fe) and aluminum (Al), as well as manganese (Mn) and it can mediate cellular uptake of these elements via cell surface Tf receptors. Iron 61-63 transferrin Rattus norvegicus 0-11 8608889-5 1996 Transferrin receptor mRNA was detected in crypt epithelial cells of the small and large intestine in iron-deficient and normal rats. Iron 101-105 transferrin Rattus norvegicus 0-11 8608889-6 1996 In contrast, in iron-loaded rats, transferrin receptor mRNA was also detected in the superficial epithelial cells of the small intestine and colon, which contained increased stores of iron. Iron 16-20 transferrin Rattus norvegicus 34-45 8608889-6 1996 In contrast, in iron-loaded rats, transferrin receptor mRNA was also detected in the superficial epithelial cells of the small intestine and colon, which contained increased stores of iron. Iron 184-188 transferrin Rattus norvegicus 34-45 8608889-8 1996 CONCLUSIONS: In the iron-deficient and normal rat intestine, transferrin receptor mRNA was expressed only by proliferating crypt epithelial cells. Iron 20-24 transferrin Rattus norvegicus 61-72 8608889-9 1996 In iron-loaded rats, however, surface enterocytes of the intestine expressed both transferrin receptor mRNA and increased ferritin mRNA levels. Iron 3-7 transferrin Rattus norvegicus 82-93 8534979-6 1995 On the other hand, iron-saturated transferrin (TF) had cell-growth-stimulating activity, but iron-free TF did not, either in the presence or absence of EGF. Iron 19-23 transferrin Rattus norvegicus 34-45 8573200-8 1996 Chlorpromazine stimulated iron uptake by cortical synaptosomes more efficiently than Ca2+, at physiological levels, from both [55Fe]transferrin (50%) and [55Fe]citrate (68%). Iron 26-30 transferrin Rattus norvegicus 132-143 7485509-0 1995 Evidence for a low Km transporter for non-transferrin-bound iron in isolated rat hepatocytes. Iron 60-64 transferrin Rattus norvegicus 42-53 7485509-1 1995 Non-transferrin-bound iron (NTBI) plays an important role in the hepatocellular injury induced by iron overload. Iron 22-26 transferrin Rattus norvegicus 4-15 7485509-1 1995 Non-transferrin-bound iron (NTBI) plays an important role in the hepatocellular injury induced by iron overload. Iron 98-102 transferrin Rattus norvegicus 4-15 8534979-6 1995 On the other hand, iron-saturated transferrin (TF) had cell-growth-stimulating activity, but iron-free TF did not, either in the presence or absence of EGF. Iron 19-23 transferrin Rattus norvegicus 47-49 7628272-2 1995 The role of transferrin in iron absorption by the duodenal mucosa in rats with iron deficiency and controls was evaluated immunohistochemically. Iron 27-31 transferrin Rattus norvegicus 12-23 7556141-0 1995 Uptake of iron from N-terminal half-transferrin by isolated rat hepatocytes. Iron 10-14 transferrin Rattus norvegicus 36-47 7556141-1 1995 Evidence of transferrin-receptor-independent iron uptake. Iron 45-49 transferrin Rattus norvegicus 12-23 7556141-8 1995 This suggests that iron derived from diferric transferrin competes with the iron derived from the N-fragment for a common transport pathway. Iron 19-23 transferrin Rattus norvegicus 46-57 7556141-8 1995 This suggests that iron derived from diferric transferrin competes with the iron derived from the N-fragment for a common transport pathway. Iron 76-80 transferrin Rattus norvegicus 46-57 7556141-10 1995 The results show that the hepatocyte has an effective transferrin-receptor-independent mechanism for accumulation of iron from transferrin. Iron 117-121 transferrin Rattus norvegicus 54-65 7556141-10 1995 The results show that the hepatocyte has an effective transferrin-receptor-independent mechanism for accumulation of iron from transferrin. Iron 117-121 transferrin Rattus norvegicus 127-138 8554925-6 1995 Addition of extracellular Fe59-transferrin to cultures of ROS 17/2.8 cells resulted in the sequestration of the iron in intracellular ferritin. Iron 112-116 transferrin Rattus norvegicus 31-42 7628272-6 1995 In iron-deficient rats, transferrin was weakly stained after iron administration but was strongly stained after saline administration. Iron 3-7 transferrin Rattus norvegicus 24-35 7628272-6 1995 In iron-deficient rats, transferrin was weakly stained after iron administration but was strongly stained after saline administration. Iron 61-65 transferrin Rattus norvegicus 24-35 7628272-7 1995 In contrast, in controls, transferrin was weakly stained after saline administration but was strongly stained after iron administration. Iron 116-120 transferrin Rattus norvegicus 26-37 7628272-9 1995 In iron-deficient rats, accumulation of electron-dense transferrin-negative microgranules was observed in some of the duodenal columnar epithelium. Iron 3-7 transferrin Rattus norvegicus 55-66 7608520-19 1995 We suggest that transferrin or a transferrin-like substance may have a local role in the transport of iron or other metals or may play a role as growth factor in the three lobes of the pituitary gland. Iron 102-106 transferrin Rattus norvegicus 16-27 7608520-19 1995 We suggest that transferrin or a transferrin-like substance may have a local role in the transport of iron or other metals or may play a role as growth factor in the three lobes of the pituitary gland. Iron 102-106 transferrin Rattus norvegicus 33-44 8527044-1 1995 Transferrin receptor (TR) performs the major function of binding and internalizing its specific iron-loaded ligand, transferrin, and its expression is closely linked to the proliferation status of the cell. Iron 96-100 transferrin Rattus norvegicus 116-127 7705780-9 1995 Double-labeled (125I, 59Fe) transferrin was used to measure recovery of iron (Fe) relative to the protein (P) in bile. Iron 72-76 transferrin Rattus norvegicus 28-39 7782907-0 1995 Brain iron, transferrin and ferritin concentrations are altered in developing iron-deficient rats. Iron 78-82 transferrin Rattus norvegicus 12-23 7782907-8 1995 This study extends previous research by demonstrating that the brain responds to changes in body iron status with a change in transferrin concentration. Iron 97-101 transferrin Rattus norvegicus 126-137 7782907-11 1995 The concept that iron enters the brain through a highly regulated endocytotic process at the blood brain barrier, that undoubtedly involves the regulation of transferrin receptors in capillary endothelial cell, is supported by our observation of elevated transferrin concentrations in brain of iron-deficient rats. Iron 17-21 transferrin Rattus norvegicus 158-169 7782907-11 1995 The concept that iron enters the brain through a highly regulated endocytotic process at the blood brain barrier, that undoubtedly involves the regulation of transferrin receptors in capillary endothelial cell, is supported by our observation of elevated transferrin concentrations in brain of iron-deficient rats. Iron 17-21 transferrin Rattus norvegicus 255-266 7782907-11 1995 The concept that iron enters the brain through a highly regulated endocytotic process at the blood brain barrier, that undoubtedly involves the regulation of transferrin receptors in capillary endothelial cell, is supported by our observation of elevated transferrin concentrations in brain of iron-deficient rats. Iron 294-298 transferrin Rattus norvegicus 158-169 7782907-11 1995 The concept that iron enters the brain through a highly regulated endocytotic process at the blood brain barrier, that undoubtedly involves the regulation of transferrin receptors in capillary endothelial cell, is supported by our observation of elevated transferrin concentrations in brain of iron-deficient rats. Iron 294-298 transferrin Rattus norvegicus 255-266 7579915-9 1995 These data support the contention that some radionuclides may cross the blood-testis barrier by utilisation of the physiologic iron-transferrin pathway, which may lead to greater testicular damage in adult compared to neonatal animals. Iron 127-131 transferrin Rattus norvegicus 132-143 7893739-2 1995 When, after the initial preincubation with the chelators and prior to the addition of 3-methylmargaric acid, iron-saturated transferrin and Fe3+ were added, a partial restitution of the CO2-production rates was obtained. Iron 109-113 transferrin Rattus norvegicus 124-135 7788730-4 1995 TfR and Tf were mainly distributed in the peripheral part of the lobule (zone 1) in the normal, iron deficient and iron-overloaded rats. Iron 96-100 transferrin Rattus norvegicus 0-2 7788730-4 1995 TfR and Tf were mainly distributed in the peripheral part of the lobule (zone 1) in the normal, iron deficient and iron-overloaded rats. Iron 115-119 transferrin Rattus norvegicus 0-2 7788730-8 1995 In the iron-overloaded rats, the staining intensity of iron was stronger in zone 1 than in zone 2 and 3, similar to the distribution pattern of TfR and Tf. Iron 7-11 transferrin Rattus norvegicus 144-146 7788730-9 1995 These findings suggest that (1) iron uptake in hepatic cells in vivo is regulated and mediated by TfR and Tf, (2) the expression pattern of TfR and Tf in zone 1 to zone 3 liver cells may result in the progressive decrease of iron deposition in the hepatic lobules of the iron overloaded rats. Iron 32-36 transferrin Rattus norvegicus 98-100 7788730-9 1995 These findings suggest that (1) iron uptake in hepatic cells in vivo is regulated and mediated by TfR and Tf, (2) the expression pattern of TfR and Tf in zone 1 to zone 3 liver cells may result in the progressive decrease of iron deposition in the hepatic lobules of the iron overloaded rats. Iron 32-36 transferrin Rattus norvegicus 106-108 7783403-0 1995 Non-iron mediated alteration in hepatic transferrin gene expression in the nephrotic rat. Iron 4-8 transferrin Rattus norvegicus 40-51 7766029-7 1995 The transferrin saturation with iron was significantly greater in SeD rats than in SeA rats (57-60% versus 30-31%). Iron 32-36 transferrin Rattus norvegicus 4-15 7787990-0 1995 Transferrin receptor distribution and iron deposition in the hepatic lobule of iron-overloaded rats. Iron 79-83 transferrin Rattus norvegicus 0-11 7787990-8 1995 The staining intensity of TfR, Tf and Ft increased in hepatocytes of iron-deficient rats and decreased in that of the iron-overloaded in comparison with the control rats. Iron 69-73 transferrin Rattus norvegicus 26-28 7787990-8 1995 The staining intensity of TfR, Tf and Ft increased in hepatocytes of iron-deficient rats and decreased in that of the iron-overloaded in comparison with the control rats. Iron 118-122 transferrin Rattus norvegicus 26-28 7550090-0 1995 Nonenzymatic glycation of transferrin: decrease of iron-binding capacity and increase of oxygen radical production. Iron 51-55 transferrin Rattus norvegicus 26-37 7550090-10 1995 These results suggest that iron ions in the glycated transferrin molecule are bound loosely to the protein and are redox-active and the glycated holotransferrin produces oxygen radicals including O2- and OH. Iron 27-31 transferrin Rattus norvegicus 53-64 8083587-6 1994 Iron delocalization occurred during ischemia, as indicated by a significant rise in percent saturation of transferrin over that of the corresponding sham group (35% +/- 2% vs 25% +/- 2%; p < 0.05) and persisted during reperfusion (39% +/- 5% vs 27% +/- 3%; p < 0.05). Iron 0-4 transferrin Rattus norvegicus 106-117 8597311-3 1995 At the same time, these two inflammations induce in plasma: a significant increase in ceruloplasmin (respectively 70 and 42%); a decrease in iron transferrin (48 and 53%) and iron saturation (%) of transferrin (53 and 68%); an increase in the protein level of 45% for croton oil treated animals. Iron 141-145 transferrin Rattus norvegicus 146-157 8597311-3 1995 At the same time, these two inflammations induce in plasma: a significant increase in ceruloplasmin (respectively 70 and 42%); a decrease in iron transferrin (48 and 53%) and iron saturation (%) of transferrin (53 and 68%); an increase in the protein level of 45% for croton oil treated animals. Iron 175-179 transferrin Rattus norvegicus 198-209 7753436-5 1995 3) transferrin receptor route, very important for cellular uptake of iron and zinc. Iron 69-73 transferrin Rattus norvegicus 3-14 8035195-3 1994 In this study the spatial and temporal pattern of iron and its regulatory proteins transferrin and ferritin are quantitatively examined in the rat CNS during the first 3 weeks of postnatal life and in adults and aged animals. Iron 50-54 transferrin Rattus norvegicus 83-94 7919266-0 1994 [Change in level and saturation by iron of blood plasma transferrin in hereditary retinal degeneration in rats]. Iron 35-39 transferrin Rattus norvegicus 56-67 7912169-1 1994 The effects of a xanthine oxidase-mediated free radical-generating system containing purine and iron-loaded transferrin or solutions containing hydrogen peroxide and iron-loaded transferrin on substrate utilization and high-energy phosphates were evaluated by nuclear magnetic resonance (NMR) spectroscopy in isolated perfused rat hearts. Iron 166-170 transferrin Rattus norvegicus 178-189 8188178-8 1994 By ferrokinetic study with plasma that contained iron 59-labeled transferrin, the plasma iron disappearance half time, calculated from the disappearance curve, was significantly shortened from 55 min to 22 min by IL-6 treatment (p < 0.01). Iron 49-53 transferrin Rattus norvegicus 65-76 8048526-0 1994 Biliary excretion of plasma non-transferrin-bound iron in rats: pathogenetic importance in iron-overload disorders. Iron 50-54 transferrin Rattus norvegicus 32-43 8048526-1 1994 Plasma non-transferrin-bound iron (NTB-iron) is a potentially toxic form of iron, which is efficiently taken up by the normal, as well as the chronically iron-overloaded liver. Iron 29-33 transferrin Rattus norvegicus 11-22 8048526-1 1994 Plasma non-transferrin-bound iron (NTB-iron) is a potentially toxic form of iron, which is efficiently taken up by the normal, as well as the chronically iron-overloaded liver. Iron 39-43 transferrin Rattus norvegicus 11-22 8048526-1 1994 Plasma non-transferrin-bound iron (NTB-iron) is a potentially toxic form of iron, which is efficiently taken up by the normal, as well as the chronically iron-overloaded liver. Iron 39-43 transferrin Rattus norvegicus 11-22 8048526-1 1994 Plasma non-transferrin-bound iron (NTB-iron) is a potentially toxic form of iron, which is efficiently taken up by the normal, as well as the chronically iron-overloaded liver. Iron 39-43 transferrin Rattus norvegicus 11-22 7997450-1 1994 Recent demonstrations of transferrin (TF) mRNA in placental tissue raised the possibility that the placenta may serve as an extra-hepatic source of this iron-binding protein during development. Iron 153-157 transferrin Rattus norvegicus 25-36 7997450-1 1994 Recent demonstrations of transferrin (TF) mRNA in placental tissue raised the possibility that the placenta may serve as an extra-hepatic source of this iron-binding protein during development. Iron 153-157 transferrin Rattus norvegicus 38-40 8188178-8 1994 By ferrokinetic study with plasma that contained iron 59-labeled transferrin, the plasma iron disappearance half time, calculated from the disappearance curve, was significantly shortened from 55 min to 22 min by IL-6 treatment (p < 0.01). Iron 89-93 transferrin Rattus norvegicus 65-76 8396885-4 1993 The reaction was inhibited by sulfhydryl reagents, was heat labile, and may account for reduction of ferric to ferrous iron during hepatic iron uptake from transferrin or from other iron sources. Iron 139-143 transferrin Rattus norvegicus 156-167 8200334-0 1994 The process of cellular uptake of iron from transferrin. Iron 34-38 transferrin Rattus norvegicus 44-55 8200334-2 1994 In an attempt to improve our understanding of the complex interplay between cell compartments and chemical species during cellular uptake of iron from transferrin, we designed a computer simulation program based on current models of receptor-mediated endocytosis and pinocytosis. Iron 141-145 transferrin Rattus norvegicus 151-162 8200334-3 1994 The program calculates and visualizes, as a function of time, the changes in transferrin, apotransferrin, and iron concentrations occurring in all relevant cellular compartments during cellular iron acquisition from transferrin. Iron 194-198 transferrin Rattus norvegicus 77-88 8200334-3 1994 The program calculates and visualizes, as a function of time, the changes in transferrin, apotransferrin, and iron concentrations occurring in all relevant cellular compartments during cellular iron acquisition from transferrin. Iron 194-198 transferrin Rattus norvegicus 93-104 8300902-2 1993 The regulation of systemic iron is through the proteins transferrin (iron mobilization) and ferritin (iron sequestration). Iron 27-31 transferrin Rattus norvegicus 56-67 8300902-2 1993 The regulation of systemic iron is through the proteins transferrin (iron mobilization) and ferritin (iron sequestration). Iron 69-73 transferrin Rattus norvegicus 56-67 8300902-2 1993 The regulation of systemic iron is through the proteins transferrin (iron mobilization) and ferritin (iron sequestration). Iron 69-73 transferrin Rattus norvegicus 56-67 8204100-1 1994 The uptake of iron by the liver and cerebellum was measured in rats using [59Fe]transferrin. Iron 14-18 transferrin Rattus norvegicus 80-91 8299907-9 1994 Transferrin may play an important role in iron delivery to and/or as a growth factor for the rapidly proliferating intestinal epithelium. Iron 42-46 transferrin Rattus norvegicus 0-11 8301587-3 1994 Transferrin receptors are highly concentrated on brain blood vessels and participate in the transport of iron across the BBB. Iron 105-109 transferrin Rattus norvegicus 0-11 8139766-8 1994 It is concluded that during the passage of transferrin-bound iron into the brain the iron is released from transferrin within endothelial cells after endocytosis of transferrin. Iron 61-65 transferrin Rattus norvegicus 43-54 8139766-8 1994 It is concluded that during the passage of transferrin-bound iron into the brain the iron is released from transferrin within endothelial cells after endocytosis of transferrin. Iron 61-65 transferrin Rattus norvegicus 107-118 8139766-8 1994 It is concluded that during the passage of transferrin-bound iron into the brain the iron is released from transferrin within endothelial cells after endocytosis of transferrin. Iron 61-65 transferrin Rattus norvegicus 107-118 8139766-8 1994 It is concluded that during the passage of transferrin-bound iron into the brain the iron is released from transferrin within endothelial cells after endocytosis of transferrin. Iron 85-89 transferrin Rattus norvegicus 43-54 8139766-8 1994 It is concluded that during the passage of transferrin-bound iron into the brain the iron is released from transferrin within endothelial cells after endocytosis of transferrin. Iron 85-89 transferrin Rattus norvegicus 107-118 8139766-8 1994 It is concluded that during the passage of transferrin-bound iron into the brain the iron is released from transferrin within endothelial cells after endocytosis of transferrin. Iron 85-89 transferrin Rattus norvegicus 107-118 8396885-4 1993 The reaction was inhibited by sulfhydryl reagents, was heat labile, and may account for reduction of ferric to ferrous iron during hepatic iron uptake from transferrin or from other iron sources. Iron 119-123 transferrin Rattus norvegicus 156-167 8396885-4 1993 The reaction was inhibited by sulfhydryl reagents, was heat labile, and may account for reduction of ferric to ferrous iron during hepatic iron uptake from transferrin or from other iron sources. Iron 139-143 transferrin Rattus norvegicus 156-167 8360262-5 1993 Diferric transferrin (2Fe.Tf) also is necessary as an iron source (Eby et al. Iron 54-58 transferrin Rattus norvegicus 9-20 8507877-4 1993 When succinylacetone is used to inhibit Belgrade heme synthesis, iron from diferric transferrin does not accumulate in the stromal fraction that contains mitochondria, nor does 59Fe accumulate in the nonheme cytosolic fraction. Iron 65-69 transferrin Rattus norvegicus 84-95 8325865-12 1993 Iron unloading is ineffective inside the Belgrade vesicle; 85% of iron that entered on transferrin returned to the medium after exocytosis, whereas only 45% of iron entering normal reticulocytes exits. Iron 66-70 transferrin Rattus norvegicus 87-98 8507877-6 1993 Therefore, the mutation affects either the release of iron from transferrin or iron transport from the vesicle to the mitochondrion. Iron 54-58 transferrin Rattus norvegicus 64-75 8387476-4 1993 Increased hepatic iron is normally associated with decreased serum transferrin and total iron binding capacity in hepatic iron overload. Iron 18-22 transferrin Rattus norvegicus 67-78 8333587-1 1993 Transferrin is N-glycosylated glycoprotein and plays an important role in iron transport from sites of absorption and storage to sites of utilization. Iron 74-78 transferrin Rattus norvegicus 0-11 8361638-1 1993 The role of oligodendrocyte-derived transferrin in the transport and regional accumulation of iron has been studied in myelin-deficient (md) rats, which lack functional oligodendrocytes and have an almost complete depletion of transferrin in the brain, although they have normal peripheral levels of transferrin. Iron 94-98 transferrin Rattus norvegicus 36-47 8361638-5 1993 The choroid plexus contains high levels of transferrin mRNA and it is therefore likely that transferrin synthesized by choroid plexus epithelial cells can mediate the transport of iron within the brain. Iron 180-184 transferrin Rattus norvegicus 43-54 8361638-5 1993 The choroid plexus contains high levels of transferrin mRNA and it is therefore likely that transferrin synthesized by choroid plexus epithelial cells can mediate the transport of iron within the brain. Iron 180-184 transferrin Rattus norvegicus 92-103 8387476-5 1993 In LEC rats, however, both serum transferrin and total iron binding capacity increased with increasing hepatic iron. Iron 111-115 transferrin Rattus norvegicus 33-44 8505377-11 1993 The evidence supports an iron transport model in which iron-loaded transferrin is taken up by receptor-mediated endocytosis at the luminal membrane of brain capillaries. Iron 55-59 transferrin Rattus norvegicus 67-78 8505377-11 1993 The evidence supports an iron transport model in which iron-loaded transferrin is taken up by receptor-mediated endocytosis at the luminal membrane of brain capillaries. Iron 25-29 transferrin Rattus norvegicus 67-78 8444319-0 1993 Non-transferrin-bound-iron in serum and low-molecular-weight-iron in the liver of dietary iron-loaded rats. Iron 22-26 transferrin Rattus norvegicus 4-15 8444319-4 1993 High concentrations of an iron-rich ferritin (up to 250 mg/l) were detected in serum of heavily iron-loaded rats forming a large fraction of non-transferrin-bound-iron (5000 micrograms/dl in maximum). Iron 26-30 transferrin Rattus norvegicus 145-156 8505377-12 1993 The iron then dissociates from transferrin in endosomal compartments and is transcytosed by unknown mechanisms, while the transferrin is retroendocytosed. Iron 4-8 transferrin Rattus norvegicus 31-42 1450923-4 1992 Iron and transferrin uptake into the brain and CSF decreased with increasing age and was greater in the iron-deficient than in the control 21-day rats. Iron 104-108 transferrin Rattus norvegicus 9-20 8435091-6 1993 After intestinal absorption, TMH-ferrocene iron in the portal blood is transported to the liver independently from transferrin. Iron 43-47 transferrin Rattus norvegicus 115-126 1334504-1 1992 Choroid plexus epithelial cells are enriched in mRNA for proteins such as the iron carrier transferrin, which acts as a trophic factor in the brain. Iron 78-82 transferrin Rattus norvegicus 91-102 8430794-0 1993 Lactoferrin interferes with uptake of iron from transferrin and asialotransferrin by the rat liver. Iron 38-42 transferrin Rattus norvegicus 48-59 8430794-3 1993 At this dose level, iron uptake from transferrin was reduced by 28% and from asialotransferrin by 43% in experiments lasting 90 min. Iron 20-24 transferrin Rattus norvegicus 37-48 8430794-9 1993 The data obtained are compatible with the hypothesis that lactoferrin and other proteins with similarly high affinity for hepatic heparan sulfate exert their negative effect on iron uptake by preventing transferrin binding to the proteoglycan. Iron 177-181 transferrin Rattus norvegicus 203-214 20732171-3 1993 One day after iron treatment, significant increases in aspartate aminotransferase and lactate dehydrogenase in the culture medium were measured; under similar conditions, albumin and transferrin secretions were decreased. Iron 14-18 transferrin Rattus norvegicus 183-194 1450923-5 1992 The quantity of 125I-transferrin recovered in the CSF could account for only a small proportion of the iron taken up by the brain. Iron 103-107 transferrin Rattus norvegicus 21-32 1450923-8 1992 It is concluded that iron uptake by the brain is dependent on iron release from transferrin at the cerebral capillary endothelial cells with recycling of transferrin to the plasma and transfer of the iron into the brain interstitium. Iron 21-25 transferrin Rattus norvegicus 80-91 1450923-8 1992 It is concluded that iron uptake by the brain is dependent on iron release from transferrin at the cerebral capillary endothelial cells with recycling of transferrin to the plasma and transfer of the iron into the brain interstitium. Iron 21-25 transferrin Rattus norvegicus 154-165 1450923-8 1992 It is concluded that iron uptake by the brain is dependent on iron release from transferrin at the cerebral capillary endothelial cells with recycling of transferrin to the plasma and transfer of the iron into the brain interstitium. Iron 62-66 transferrin Rattus norvegicus 80-91 1450923-8 1992 It is concluded that iron uptake by the brain is dependent on iron release from transferrin at the cerebral capillary endothelial cells with recycling of transferrin to the plasma and transfer of the iron into the brain interstitium. Iron 62-66 transferrin Rattus norvegicus 80-91 1644834-0 1992 Mutagenesis of the iron-regulatory element further defines a role for RNA secondary structure in the regulation of ferritin and transferrin receptor expression. Iron 19-23 transferrin Rattus norvegicus 128-139 1384359-6 1992 It is suggested that iron presented to the tubule fluid as a result of the glomerular leak for transferrin is dissociated from transferrin. Iron 21-25 transferrin Rattus norvegicus 95-106 1415806-0 1992 Iron uptake in relation to transferrin degradation in brain and other tissues of rats. Iron 0-4 transferrin Rattus norvegicus 27-38 1415806-1 1992 The possibility that iron uptake by the brain involves transcytosis of the iron-transferrin complex across the brain capillaries, followed by degradation of the transferrin (Tf) within the brain, was investigated using diferric 125I-[59Fe]Tf and [59Fe]Tf coupled to 125I-tyramine cellobiose (TC). Iron 21-25 transferrin Rattus norvegicus 80-91 1415806-1 1992 The possibility that iron uptake by the brain involves transcytosis of the iron-transferrin complex across the brain capillaries, followed by degradation of the transferrin (Tf) within the brain, was investigated using diferric 125I-[59Fe]Tf and [59Fe]Tf coupled to 125I-tyramine cellobiose (TC). Iron 21-25 transferrin Rattus norvegicus 161-172 1415806-1 1992 The possibility that iron uptake by the brain involves transcytosis of the iron-transferrin complex across the brain capillaries, followed by degradation of the transferrin (Tf) within the brain, was investigated using diferric 125I-[59Fe]Tf and [59Fe]Tf coupled to 125I-tyramine cellobiose (TC). Iron 75-79 transferrin Rattus norvegicus 80-91 1419828-1 1992 The uptake of transferrin by macrophages was studied in relation to the degree of iron saturation. Iron 82-86 transferrin Rattus norvegicus 14-25 1527027-2 1992 The iron-responsive element binding protein (IRE-BP) is a cytosolic protein that binds a highly conserved sequence in the untranslated regions of mRNAs involved in iron metabolism including ferritin, transferrin receptor, and erythroid 5-aminolevulinate acid synthase. Iron 4-8 transferrin Rattus norvegicus 200-211 1527027-2 1992 The iron-responsive element binding protein (IRE-BP) is a cytosolic protein that binds a highly conserved sequence in the untranslated regions of mRNAs involved in iron metabolism including ferritin, transferrin receptor, and erythroid 5-aminolevulinate acid synthase. Iron 164-168 transferrin Rattus norvegicus 200-211 1445180-0 1992 The relationship between homozygosity level and animal physiology: iron content of plasma and whole blood as well as total iron binding capacity by transferrin (TIBC) in rats of various inbreeding coefficient. Iron 123-127 transferrin Rattus norvegicus 148-159 1622403-6 1992 The 59Fe-labelling profiles of mucosal ferritin and transferrin from a test dose also were changed substantially in response to very-short-term alterations in dietary iron. Iron 167-171 transferrin Rattus norvegicus 52-63 1530145-0 1992 Iron uptake from transferrin and asialotransferrin by hepatocytes from chronically alcohol-fed rats. Iron 0-4 transferrin Rattus norvegicus 17-28 1530145-2 1992 As the liver is a major iron storage site and also synthesizes transferrin, the normal serum iron transport protein, the aim of this study was to test the hypothesis that these disturbances in iron homeostasis were caused by altered hepatocyte iron uptake from the abnormal transferrin. Iron 93-97 transferrin Rattus norvegicus 63-74 1530145-2 1992 As the liver is a major iron storage site and also synthesizes transferrin, the normal serum iron transport protein, the aim of this study was to test the hypothesis that these disturbances in iron homeostasis were caused by altered hepatocyte iron uptake from the abnormal transferrin. Iron 93-97 transferrin Rattus norvegicus 63-74 1530145-2 1992 As the liver is a major iron storage site and also synthesizes transferrin, the normal serum iron transport protein, the aim of this study was to test the hypothesis that these disturbances in iron homeostasis were caused by altered hepatocyte iron uptake from the abnormal transferrin. Iron 93-97 transferrin Rattus norvegicus 63-74 1530145-3 1992 To achieve this, we have investigated iron uptake from both transferrin and asialotransferrin by hepatocytes from male Sprague-Dawley rats fed the De Carli and Lieber alcohol diet. Iron 38-42 transferrin Rattus norvegicus 60-71 1530145-4 1992 Iron uptake from transferrin by hepatocytes from alcoholic rats was less than 60% that of control values, and in the presence of 50 mM ethanol decreased still further to 35% of the uptake by the corresponding control cells. Iron 0-4 transferrin Rattus norvegicus 17-28 1530145-5 1992 Iron uptake from rat asialotransferrin was reduced in both groups when compared to that observed from normal transferrin; 13% by control cells and 39% by hepatocytes from alcohol-fed rats. Iron 0-4 transferrin Rattus norvegicus 27-38 1449722-4 1992 In the presence of the proteoglycan at pH 5.6, the release of iron from the N-lobe of transferrin was accelerated. Iron 62-66 transferrin Rattus norvegicus 86-97 1613505-8 1992 It is proposed that the uptake of iron into brain involves the entry of iron-loaded transferrin to the cerebral capillaries, deposition of iron within the endothelial cells, followed by recycling of apotransferrin to the circulation. Iron 34-38 transferrin Rattus norvegicus 84-95 1613505-8 1992 It is proposed that the uptake of iron into brain involves the entry of iron-loaded transferrin to the cerebral capillaries, deposition of iron within the endothelial cells, followed by recycling of apotransferrin to the circulation. Iron 72-76 transferrin Rattus norvegicus 84-95 1613505-8 1992 It is proposed that the uptake of iron into brain involves the entry of iron-loaded transferrin to the cerebral capillaries, deposition of iron within the endothelial cells, followed by recycling of apotransferrin to the circulation. Iron 72-76 transferrin Rattus norvegicus 84-95 1613505-9 1992 The deposited iron is then delivered to brain-derived transferrin for extracellular transport within the brain, and subsequently taken up via transferrin receptors on neurones and glia for usage or storage. Iron 14-18 transferrin Rattus norvegicus 54-65 1613505-9 1992 The deposited iron is then delivered to brain-derived transferrin for extracellular transport within the brain, and subsequently taken up via transferrin receptors on neurones and glia for usage or storage. Iron 14-18 transferrin Rattus norvegicus 142-153 1622403-7 1992 Even though changes in dietary iron rapidly altered iron uptake by brush-border membrane vesicles and the incorporation of 59Fe from the test dose into mucosal transferrin, changes in the incorporation of 59Fe into mucosal ferritin best reflected the actual changes in the transfer of iron from dose to plasma. Iron 31-35 transferrin Rattus norvegicus 160-171 1536148-1 1992 The mechanism underlying the impaired uptake of iron from transferrin by reticulocytes from the Belgrade laboratory rat was investigated using 125I- and 59Fe-labeled transferrin isolated from homozygous Belgrade rats and from Wistar rats, nontransferrin-bound Fe(II) in an isotonic sucrose solution, and reticulocytes from Belgrade and Wistar rats. Iron 48-52 transferrin Rattus norvegicus 58-69 1640494-2 1992 Most cells acquire iron through a specific receptor mediated process involving transferrin, the iron mobilization protein. Iron 19-23 transferrin Rattus norvegicus 79-90 1640494-2 1992 Most cells acquire iron through a specific receptor mediated process involving transferrin, the iron mobilization protein. Iron 96-100 transferrin Rattus norvegicus 79-90 1298300-5 1992 Myocytes maintained in HEPES buffer or the HEPES buffer containing purine and iron-loaded transferrin continued to stimulate, exhibited relatively uniform 340/380 nm ratios and maintained a rod shape. Iron 78-82 transferrin Rattus norvegicus 90-101 1416028-0 1992 Preparation of iron-deficient tissue culture medium by deferoxamine-sepharose treatment and application to the differential actions of apotransferrin and diferric transferrin. Iron 15-19 transferrin Rattus norvegicus 138-149 1539729-1 1992 Iron uptake from transferrin by a variety of cells and tissues of homozygous Belgrade laboratory rats was compared with heterozygotes, and normal and iron-deficient Wistar rats. Iron 0-4 transferrin Rattus norvegicus 17-28 1536148-2 1992 The Belgrade rat transferrin had the same molecular weight and net charge as Wistar rat transferrin, donated iron equally well to both types of reticulocytes, and competed equally for transferrin binding sites on the cells. Iron 109-113 transferrin Rattus norvegicus 17-28 1510380-2 1992 Iron in blood plasma is totally bound to transferrin (Tf), a major plasma glycoprotein. Iron 0-4 transferrin Rattus norvegicus 41-52 1510380-2 1992 Iron in blood plasma is totally bound to transferrin (Tf), a major plasma glycoprotein. Iron 0-4 transferrin Rattus norvegicus 54-56 1510380-8 1992 It is likely that iron separates from Tf in early endosomes, which are assumed to be acidic, as they are in other cells, and enters the brain by an as yet undefined pathway. Iron 18-22 transferrin Rattus norvegicus 38-40 1510380-9 1992 A clonal line of brain capillary endothelial cells that mimics the BBB when grown on permeabilized membranes can transcytose iron provided as Fe55-Tf. Iron 125-129 transferrin Rattus norvegicus 147-149 1747455-1 1991 Transferrin (Tf) was found immunologically in pancreatic juice of normal rats at a concentration of 0.28 +/- 0.10 mg/ml but was found to be approximately 4-times higher in iron-deficient rats. Iron 172-176 transferrin Rattus norvegicus 0-11 1735118-1 1992 The present study examines events of the Sertoli cell iron delivery pathway following the secretion of diferric testicular transferrin (tTf) into the adluminal compartment of the rat seminiferous epithelium. Iron 54-58 transferrin Rattus norvegicus 123-134 1359698-1 1992 The expression of the gene for the iron transport protein transferrin was found to be altered in preneoplastic and neoplastic lesions induced in the rat liver by N-nitrosomorpholine. Iron 35-39 transferrin Rattus norvegicus 58-69 1919575-0 1991 Transferrin and iron uptake by the brain: effects of altered iron status. Iron 61-65 transferrin Rattus norvegicus 0-11 1919575-5 1991 Both Tf and iron uptake were significantly greater in the iron-deficient rats than in their controls and lower in the iron-loaded rats than in the corresponding controls. Iron 58-62 transferrin Rattus norvegicus 5-7 1919575-5 1991 Both Tf and iron uptake were significantly greater in the iron-deficient rats than in their controls and lower in the iron-loaded rats than in the corresponding controls. Iron 58-62 transferrin Rattus norvegicus 5-7 1919575-8 1991 125I-Tf uptake by the brains of the iron-deficient rats increased very rapidly after injection of the labelled proteins, within 15 min reaching a plateau level which was maintained for at least 6 h. The uptake of 59Fe, however, increased rapidly for 1 h and then more slowly, and in terms of percentage of injected dose reached much higher values than did 125I-Tf uptake. Iron 36-40 transferrin Rattus norvegicus 5-7 1776464-0 1991 Transferrin receptors and selective iron deposition in pancreatic B cells of iron-overloaded rats. Iron 77-81 transferrin Rattus norvegicus 0-11 1878368-5 1991 But also at lowered temperature only a part of the iron in endosomal fractions can be assigned to transferrin. Iron 51-55 transferrin Rattus norvegicus 98-109 1878368-6 1991 A considerable part of the total uptake of transferrin and iron can be attributed to low-affinity mechanisms even at very low transferrin concentrations. Iron 59-63 transferrin Rattus norvegicus 126-137 1791188-5 1991 Electrophoretically separated holo-rat transferrin and rat lung-derived growth factor displayed similar positive stains for iron. Iron 124-128 transferrin Rattus norvegicus 39-50 1747455-1 1991 Transferrin (Tf) was found immunologically in pancreatic juice of normal rats at a concentration of 0.28 +/- 0.10 mg/ml but was found to be approximately 4-times higher in iron-deficient rats. Iron 172-176 transferrin Rattus norvegicus 13-15 1747455-2 1991 Iron saturation of pancreatic Tf of normal rats was 40% and similar to that of serum Tf. Iron 0-4 transferrin Rattus norvegicus 30-32 1747455-3 1991 Approximately 27% of a dose of iron from 59Fe-diferric Tf was absorbed through the ligated segments of proximal intestine in normal rats. Iron 31-35 transferrin Rattus norvegicus 55-57 1747455-4 1991 The iron absorption ratio of 59Fe-diferric Tf was higher from the duodenal and jejunal segments than the ileum and significantly inhibited by monodansylcadaverine (MDC) or 20-times excess of unlabeled diferric Tf. Iron 4-8 transferrin Rattus norvegicus 43-45 1747455-4 1991 The iron absorption ratio of 59Fe-diferric Tf was higher from the duodenal and jejunal segments than the ileum and significantly inhibited by monodansylcadaverine (MDC) or 20-times excess of unlabeled diferric Tf. Iron 4-8 transferrin Rattus norvegicus 210-212 1747455-9 1991 These results suggested that some iron was absorbed as diferric Tf into enterocytes through receptor-mediated endocytosis. Iron 34-38 transferrin Rattus norvegicus 64-66 2018119-3 1991 Because Al as well as iron (Fe) can bind to transferrin (TF) in plasma, the role of TF as a modifier of osteoblast proliferation was examined in UMR-106-01 osteoblast-like cells by measuring the incorporation of tritiated thymidine ([3H]-TdR) into DNA (counts.min-1.microgram cell protein-1, means +/- SE) during 48-h incubations in serum-free medium (SFM). Iron 28-30 transferrin Rattus norvegicus 44-55 2019882-3 1991 Hemoglobin, liver iron and transferrin saturation were significantly lower in the 4 and 6 mg Fe/kg diet groups relative to the other groups and were indicative of anemia, low tissue iron stores and impaired erythropoiesis. Iron 93-95 transferrin Rattus norvegicus 27-38 2022700-3 1991 We have investigated the role of the transferrin cycle in this mutant by bypassing transferrin iron delivery with the iron chelate ferric salicylaldehyde isonicotinoyl hydrazone (Fe-SIH). Iron 95-99 transferrin Rattus norvegicus 83-94 2022700-12 1991 The Belgrade defect occurs in the movement of iron from transferrin to a step prior to the ferrous state and insertion into heme. Iron 46-50 transferrin Rattus norvegicus 56-67 1996102-2 1991 For example, transferrin synthesized by the Sertoli cell is important in delivering iron from the serum to the developing germ cells. Iron 84-88 transferrin Rattus norvegicus 13-24 2004025-7 1991 These data suggest that the most likely role of the transferrin receptor in the neonatal intestine is in the supply of iron to the developing epithelial cells in the crypts, and that the receptor does not play a direct role in iron transit across the intestinal epithelium. Iron 119-123 transferrin Rattus norvegicus 52-63 1931436-8 1991 These values imply that, in the physiological range of Tf concentrations, about 75% of the Fe taken up by hepatocytes may be due to a pinocytic mechanism (fluid-phase or mixed). Iron 91-93 transferrin Rattus norvegicus 55-57 1675959-0 1991 Specificity of hepatic iron uptake from plasma transferrin in the rat. Iron 23-27 transferrin Rattus norvegicus 47-58 1675959-2 1991 The role of specific interaction between transferrin and its receptors in iron uptake by the liver in vivo was investigated using 59Fe-125I-labelled transferrins from several animal species, and adult and 15-day rats. Iron 74-78 transferrin Rattus norvegicus 41-52 1675959-11 1991 It is concluded that iron uptake by the liver from plasma transferrin in vivo is largely or completely dependent on specific transferrin-receptor interaction. Iron 21-25 transferrin Rattus norvegicus 58-69 1675959-11 1991 It is concluded that iron uptake by the liver from plasma transferrin in vivo is largely or completely dependent on specific transferrin-receptor interaction. Iron 21-25 transferrin Rattus norvegicus 125-136 1671034-2 1991 Both EGF and its receptor are thought to be targeted for destruction in lysosomes, leading to down-regulation of the receptor, whereas transferrin, after unloading iron within the cell, is thought to recycle to the cell surface bound to its receptor. Iron 164-168 transferrin Rattus norvegicus 135-146 1991464-0 1991 Fe3+(2)-transferrin and Fe3+(2)-asialotransferrin deliver iron to hepatocytes by an identical mechanism. Iron 58-62 transferrin Rattus norvegicus 8-19 1991464-8 1991 Despite the different properties of the two ligands, the rates of iron uptake from 59Fe3+(2)-transferrin and 59Fe3+(2)-asialotransferrin were identical, suggesting a common mechanism for the translocation of iron across the plasma (or possibly endosomal) membrane such as a transmembrane oxidoreductase. Iron 66-70 transferrin Rattus norvegicus 93-104 12106249-1 1991 Iron-saturated transferrin is a ubiquitous growth factor that plays a critical role in cellular iron uptake, growth and proliferation. Iron 0-4 transferrin Rattus norvegicus 15-26 1991464-11 1991 The release of iron at the hepatocyte cell surface would effectively uncouple the two functions and render the hepatocyte unresponsive to growth stimulation by transferrin. Iron 15-19 transferrin Rattus norvegicus 160-171 12106249-1 1991 Iron-saturated transferrin is a ubiquitous growth factor that plays a critical role in cellular iron uptake, growth and proliferation. Iron 96-100 transferrin Rattus norvegicus 15-26 2207126-1 1990 A transferrin binding protein was isolated from normal rat placenta and from iron-deficient rat plasma using a human transferrin affinity column. Iron 77-81 transferrin Rattus norvegicus 2-13 12106249-6 1991 In addition, studies using intravenously injected radioactive iron (59Fe3+) showed a massive increase in endoneural iron uptake confined to the lesion site and to the distal part of the axotomised sciatic nerve, parallel to the time course of reactive transferrin receptor expression. Iron 62-66 transferrin Rattus norvegicus 252-263 12106249-6 1991 In addition, studies using intravenously injected radioactive iron (59Fe3+) showed a massive increase in endoneural iron uptake confined to the lesion site and to the distal part of the axotomised sciatic nerve, parallel to the time course of reactive transferrin receptor expression. Iron 116-120 transferrin Rattus norvegicus 252-263 12106249-7 1991 Since iron is an essential cofactor of a number of key enzymes needed in energy metabolism and DNA synthesis, these data suggest that the induction of transferrin receptor expression may play an important role in the regulation of cellular growth and proliferation during peripheral nerve regeneration. Iron 6-10 transferrin Rattus norvegicus 151-162 2209759-9 1990 Conversely, binding of iron to transferrin was minimal. Iron 23-27 transferrin Rattus norvegicus 31-42 2221071-1 1990 The effect of intracellular iron content on transferrin and iron uptake by cultured hepatocytes isolated from fetal rat liver was examined with ferric ammonium citrate and the iron chelator desferrioxamine (DFO). Iron 28-32 transferrin Rattus norvegicus 44-55 2221071-3 1990 In contrast, when iron-treated cells were incubated with DFO for 24 h, the cellular nonheme iron level was not altered, but the number of transferrin binding sites was increased. Iron 18-22 transferrin Rattus norvegicus 138-149 2221071-5 1990 These results indicated that, in cultured hepatocytes, transferrin receptor expression and the subsequent uptake of transferrin and iron are regulated by the size of an intracellular, chelatable iron pool, whereas the uptake of iron by the nonsaturable processes is dependent on the extracellular transferrin concentration. Iron 132-136 transferrin Rattus norvegicus 55-66 2221071-5 1990 These results indicated that, in cultured hepatocytes, transferrin receptor expression and the subsequent uptake of transferrin and iron are regulated by the size of an intracellular, chelatable iron pool, whereas the uptake of iron by the nonsaturable processes is dependent on the extracellular transferrin concentration. Iron 195-199 transferrin Rattus norvegicus 55-66 2221071-5 1990 These results indicated that, in cultured hepatocytes, transferrin receptor expression and the subsequent uptake of transferrin and iron are regulated by the size of an intracellular, chelatable iron pool, whereas the uptake of iron by the nonsaturable processes is dependent on the extracellular transferrin concentration. Iron 195-199 transferrin Rattus norvegicus 116-127 2221071-5 1990 These results indicated that, in cultured hepatocytes, transferrin receptor expression and the subsequent uptake of transferrin and iron are regulated by the size of an intracellular, chelatable iron pool, whereas the uptake of iron by the nonsaturable processes is dependent on the extracellular transferrin concentration. Iron 195-199 transferrin Rattus norvegicus 116-127 2221071-5 1990 These results indicated that, in cultured hepatocytes, transferrin receptor expression and the subsequent uptake of transferrin and iron are regulated by the size of an intracellular, chelatable iron pool, whereas the uptake of iron by the nonsaturable processes is dependent on the extracellular transferrin concentration. Iron 195-199 transferrin Rattus norvegicus 55-66 2221071-5 1990 These results indicated that, in cultured hepatocytes, transferrin receptor expression and the subsequent uptake of transferrin and iron are regulated by the size of an intracellular, chelatable iron pool, whereas the uptake of iron by the nonsaturable processes is dependent on the extracellular transferrin concentration. Iron 195-199 transferrin Rattus norvegicus 116-127 2221071-5 1990 These results indicated that, in cultured hepatocytes, transferrin receptor expression and the subsequent uptake of transferrin and iron are regulated by the size of an intracellular, chelatable iron pool, whereas the uptake of iron by the nonsaturable processes is dependent on the extracellular transferrin concentration. Iron 195-199 transferrin Rattus norvegicus 116-127 1744249-0 1991 Role of transferrin in iron uptake by the brain: a comparative study. Iron 23-27 transferrin Rattus norvegicus 8-19 1744249-1 1991 The role of specific transferrin (Tf) and Tf receptor interaction on brain capillary endothelial cells in iron transport from the plasma to the brain was investigated by using Tf from several species of animals labeled with 59Fe and 125I, and 15-day and adult rats. Iron 106-110 transferrin Rattus norvegicus 42-44 1744249-1 1991 The role of specific transferrin (Tf) and Tf receptor interaction on brain capillary endothelial cells in iron transport from the plasma to the brain was investigated by using Tf from several species of animals labeled with 59Fe and 125I, and 15-day and adult rats. Iron 106-110 transferrin Rattus norvegicus 42-44 1744249-6 1991 It is concluded that iron transport into the brain is dependent on the function of Tf receptors, probably on capillary endothelial cells, and that these receptors show the same type of species specificity as the receptors on immature erythroid cells. Iron 21-25 transferrin Rattus norvegicus 83-85 15539176-3 1990 Recently, transferrin receptors have been identified on lactating rat mammary plasma membranes, which may regulate iron entry into mammary tissue, potentiating its availability for subsequent transport into milk. Iron 115-119 transferrin Rattus norvegicus 10-21 2207126-6 1990 Immunoblotting of both normal and iron deficient rat plasma showed that the transferrin binding protein had a molecular mass of 85 kDa. Iron 34-38 transferrin Rattus norvegicus 76-87 2312055-11 1990 Immunohistochemistry showed decreased parenchymal but increased reticuloendothelial transferrin receptor expression with iron load. Iron 121-125 transferrin Rattus norvegicus 84-95 2126294-5 1990 Control myocytes superfused with a physiological buffer or buffer containing purine and iron-loaded transferrin exhibited Ca2+ transients associated with spontaneous contractions. Iron 88-92 transferrin Rattus norvegicus 100-111 2375400-7 1990 In lungs pretreated with the iron binding protein transferrin the Kfc increased 0.31 +/- 0.11 and 0.19 +/- 0.03 ml.min-1.cmH2O-1.100 g lung tissue-1 following IR and t-buOOH challenge, respectively. Iron 29-33 transferrin Rattus norvegicus 50-61 15539210-3 1990 It is known that iron enters other cells via transferrin receptor-mediated endocytosis. Iron 17-21 transferrin Rattus norvegicus 45-56 15539210-10 1990 The presence of transferrin receptors in normal lactating rat mammary tissue is likely to explain iron transport into mammary tissue for both cellular metabolism and milk iron secretion. Iron 98-102 transferrin Rattus norvegicus 16-27 15539210-10 1990 The presence of transferrin receptors in normal lactating rat mammary tissue is likely to explain iron transport into mammary tissue for both cellular metabolism and milk iron secretion. Iron 171-175 transferrin Rattus norvegicus 16-27 2186821-3 1990 In vivo reticulocyte uptake and release of labelled diferric transferrin injected in the iron-deficient rat averaged 1.7 min. Iron 89-93 transferrin Rattus norvegicus 61-72 2298364-2 1990 A combination of biochemical quantitation and immunohistochemistry has been used to examine in detail transferrin receptor distribution and expression in the rat small intestine and its relationship to iron absorption. Iron 202-206 transferrin Rattus norvegicus 102-113 2298364-6 1990 Dietary or parenteral iron loading of animals produced a significant decline in transferrin binding, whereas binding was increased in iron deficiency. Iron 22-26 transferrin Rattus norvegicus 80-91 2298364-9 1990 These data indicate that intestinal transferrin receptors may be regulated by body iron stores but suggest that they are not directly involved in iron absorption. Iron 83-87 transferrin Rattus norvegicus 36-47 2375965-3 1990 The increased mucosal uptake of ionized iron was not the result of increased adsorption, but instead appeared related to a metabolically active uptake process, whereas the increased mucosal uptake of transferrin iron was associated with increased numbers of mucosal cell membrane transferrin receptors. Iron 212-216 transferrin Rattus norvegicus 200-211 2375965-6 1990 Iron loading of the mucosal cell from circulating plasma transferrin was proportionate to the plasma iron concentration. Iron 0-4 transferrin Rattus norvegicus 57-68 2375965-7 1990 Mucosal iron content was the composite of iron loading from the lumen and loading from plasma transferrin versus release of iron into the body. Iron 8-12 transferrin Rattus norvegicus 94-105 2157501-0 1990 Release of iron from diferric transferrin in the presence of rat liver plasma membranes: no evidence of a plasma membrane diferric transferrin reductase. Iron 11-15 transferrin Rattus norvegicus 30-41 2157501-1 1990 The transfer of iron from diferric transferrin to bathophenanthroline disulfonate was measured under varying conditions by spectrophotometry and EPR spectroscopy. Iron 16-20 transferrin Rattus norvegicus 35-46 2157501-6 1990 Our results, together with theoretical considerations, show that the ability (or inability) of intact cells or isolated plasma membranes to facilitate the transfer of iron from transferrin to strong diferric iron chelators does not allow interferences about the existence of an iron reduction step as part of the process of cellular uptake of iron from transferrin. Iron 167-171 transferrin Rattus norvegicus 177-188 2333967-0 1990 Iron uptake from transferrin and lactoferrin by rat intestinal brush-border membrane vesicles. Iron 0-4 transferrin Rattus norvegicus 17-28 2126342-2 1990 The rat transferrin receptor nucleotide sequence was shown to be 82% similar to the human transferrin receptor sequence over the amino acid coding region and over 90% similar in the sequences known to be responsible for iron regulation in the human mRNA. Iron 220-224 transferrin Rattus norvegicus 8-19 2307125-4 1990 Tf receptor expression increases during iron depletion and decreases with iron supplementation; the number of Tf receptors was also inversely related to both cell density and the rate of cell proliferation in vitro. Iron 40-44 transferrin Rattus norvegicus 0-2 2307125-4 1990 Tf receptor expression increases during iron depletion and decreases with iron supplementation; the number of Tf receptors was also inversely related to both cell density and the rate of cell proliferation in vitro. Iron 74-78 transferrin Rattus norvegicus 0-2 2307125-7 1990 Decreases in the incorporation of [3H] thymidine into DNA were also noted in osteoblast-like cells incubated for 48 h with 3 microM partially saturated iron Tf or gallium Tf. Iron 152-156 transferrin Rattus norvegicus 157-159 2312055-14 1990 These findings support down-regulation of parenchymal transferrin receptor resulting from iron storage. Iron 90-94 transferrin Rattus norvegicus 54-65 2294524-11 1990 When the saturation of transferrin is raised, a significant proportion of the iron is transported from the spleen to the liver either in small molecular weight complexes or in ferritin. Iron 78-82 transferrin Rattus norvegicus 23-34 2342475-8 1990 These studies demonstrate that germ cell secretions may interact with Sertoli cells to specifically increase the level of transferrin mRNA and that this interaction may be a mechanism by which germ cells regulate the flow of iron across the seminiferous epithelium. Iron 225-229 transferrin Rattus norvegicus 122-133 2310376-3 1990 These studies examined the effects of various inhibitors on receptor-mediated transferrin iron delivery in order to define critical steps and events necessary to maintain the functional integrity of the pathway. Iron 90-94 transferrin Rattus norvegicus 78-89 2310376-4 1990 Dansylcadaverine inhibited iron uptake by blocking exocytic release of transferrin and return of receptors to the cell surface, but did not affect transferrin endocytosis; this action served to deplete the surface pool of transferrin receptors, leading to shutdown of iron uptake. Iron 27-31 transferrin Rattus norvegicus 71-82 2328142-6 1990 It is concluded from these results that there are Tf-receptors in the liver cell membrane to which iron transferrin may bind. Iron 99-103 transferrin Rattus norvegicus 104-115 2294524-2 1990 Raising the saturation of transferrin with oral carbonyl iron had little effect on splenic release of 59Fe but markedly inhibited hepatic release. Iron 57-61 transferrin Rattus norvegicus 26-37 34998864-5 2022 Oral iron supplementation (20.56 mg elemental Fe/kg bw) to aloin-treated rats normalized red blood corpuscles count, hemoglobin concentration, and serum levels of total iron binding capacity and saturated transferrin, as well as hepatic iron content, hepcidin level, and mRNA expression of ferritin heavy chain (Ferr-H) and transferrin receptor-1 (TfR-1) genes. Iron 5-9 transferrin Rattus norvegicus 205-216 35487763-1 2022 Belgrade rats have a defect in divalent metal transport 1 (DMT1) with a reduced heart iron, indicating that DMT1 plays a physiological role in non-transferrin-bound iron (NTBI) uptake by cardiomyocytes. Iron 165-169 transferrin Rattus norvegicus 147-158 34998864-8 2022 On other hand, oral iron supplementation to rats treated with doxorubicin (15 mg/kg bw) lessened the increase in the spleen iron content concomitantly with hepatic hepcidin level, rebound hepatic iron content to normal level, and by contrast augmented serum levels of iron and transferrin saturation. Iron 20-24 transferrin Rattus norvegicus 277-288 34998864-5 2022 Oral iron supplementation (20.56 mg elemental Fe/kg bw) to aloin-treated rats normalized red blood corpuscles count, hemoglobin concentration, and serum levels of total iron binding capacity and saturated transferrin, as well as hepatic iron content, hepcidin level, and mRNA expression of ferritin heavy chain (Ferr-H) and transferrin receptor-1 (TfR-1) genes. Iron 46-48 transferrin Rattus norvegicus 205-216 35033194-6 2022 Blood count parameters, serum ferritin, and liver transferrin bound iron were determined by automated counter. Iron 68-72 transferrin Rattus norvegicus 50-61