PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3605788-0 1987 Relationship between rabbit transferrin electrophoretic patterns and plasma iron concentrations. Iron 76-80 serotransferrin Oryctolagus cuniculus 28-39 3605788-5 1987 The degree of iron saturation of Tf varied among individuals and throughout the individual"s life. Iron 14-18 serotransferrin Oryctolagus cuniculus 33-35 3464611-2 1986 However, results from our laboratory with reticulocytes suggest that the rate of iron uptake from transferrin (Tf), rather than ALA synthase activity, limits the rate of heme synthesis in erythroid cells. Iron 81-85 serotransferrin Oryctolagus cuniculus 98-109 3464611-2 1986 However, results from our laboratory with reticulocytes suggest that the rate of iron uptake from transferrin (Tf), rather than ALA synthase activity, limits the rate of heme synthesis in erythroid cells. Iron 81-85 serotransferrin Oryctolagus cuniculus 111-113 3464611-5 1986 Therefore the possibility was investigated that, in induced cells, iron uptake from Tf limits and controls heme synthesis. Iron 67-71 serotransferrin Oryctolagus cuniculus 84-86 3464611-7 1986 Both induced and uninduced Friend cells take up and utilize Fe for heme synthesis directly from Fe-SIH without the involvement of transferrin and transferrin receptors and to a much greater extent than from saturating levels of Fe-Tf (20 microM). Iron 60-62 serotransferrin Oryctolagus cuniculus 231-233 3464611-11 1986 These results indicate that some step(s) in the pathway of iron from extracellular Tf to protoporphyrin, rather than the activity of ALA synthase, limits and controls the overall rate of heme and possibly hemoglobin synthesis in differentiating Friend erythroleukemia cells. Iron 59-63 serotransferrin Oryctolagus cuniculus 83-85 3792344-8 1986 The results suggest that the two postulated pathways of the transferrin-cell cycle (a fast, iron-donating and a slow, receptor-shedding cycle) are not similarly involved in the cellular processing of Tf and AuTf. Iron 92-96 serotransferrin Oryctolagus cuniculus 60-71 6432569-0 1984 The identification of transferrin, an iron-binding protein in rabbit tears. Iron 38-42 serotransferrin Oryctolagus cuniculus 22-33 3013846-3 1986 The results indicated, however, that both agents acted to 1) retard the internalization of transferrin bound to transferrin receptors on the plasma membrane of reticulocytes, 2) retard the externalization of internalized transferrin, and 3) block the transport into the cytosol of iron released from transferrin. Iron 281-285 serotransferrin Oryctolagus cuniculus 91-102 4016967-3 1985 Since intracellular release of iron from transferrin is believed to involve the protonation of the iron-transferrin complex, the rise in intralysomal pH could account for the inhibitory effect of spermine on iron uptake. Iron 31-35 serotransferrin Oryctolagus cuniculus 41-52 4016967-3 1985 Since intracellular release of iron from transferrin is believed to involve the protonation of the iron-transferrin complex, the rise in intralysomal pH could account for the inhibitory effect of spermine on iron uptake. Iron 31-35 serotransferrin Oryctolagus cuniculus 104-115 4016967-3 1985 Since intracellular release of iron from transferrin is believed to involve the protonation of the iron-transferrin complex, the rise in intralysomal pH could account for the inhibitory effect of spermine on iron uptake. Iron 99-103 serotransferrin Oryctolagus cuniculus 41-52 4016967-3 1985 Since intracellular release of iron from transferrin is believed to involve the protonation of the iron-transferrin complex, the rise in intralysomal pH could account for the inhibitory effect of spermine on iron uptake. Iron 99-103 serotransferrin Oryctolagus cuniculus 104-115 4016967-3 1985 Since intracellular release of iron from transferrin is believed to involve the protonation of the iron-transferrin complex, the rise in intralysomal pH could account for the inhibitory effect of spermine on iron uptake. Iron 99-103 serotransferrin Oryctolagus cuniculus 41-52 4016967-3 1985 Since intracellular release of iron from transferrin is believed to involve the protonation of the iron-transferrin complex, the rise in intralysomal pH could account for the inhibitory effect of spermine on iron uptake. Iron 99-103 serotransferrin Oryctolagus cuniculus 104-115 6746749-4 1984 Treatment of the cells with lysosomotrophic agents, metabolic inhibitors, and ionophores elevated the intravesicular pH and inhibited iron uptake from transferrin. Iron 134-138 serotransferrin Oryctolagus cuniculus 151-162 6746749-6 1984 At pH 5.4 iron release from rabbit iron-bicarbonate transferrin in vitro was much more rapid than from iron-oxalate transferrin. Iron 10-14 serotransferrin Oryctolagus cuniculus 52-63 6746749-6 1984 At pH 5.4 iron release from rabbit iron-bicarbonate transferrin in vitro was much more rapid than from iron-oxalate transferrin. Iron 35-39 serotransferrin Oryctolagus cuniculus 52-63 6746749-8 1984 It is concluded that the acidic conditions within the vesicles provide the mechanism for iron release from the transferrin molecule after its endocytosis and that the low vesicular pH is dependent on cellular metabolism. Iron 89-93 serotransferrin Oryctolagus cuniculus 111-122 6387606-7 1984 Uptake of intravenously injected transferrin-bound iron into muscle of vitamin E-deficient rabbits was not increased in a short term experiment (6 h), but radioiron did accumulate in muscle in a long term experiment (6 days). Iron 51-55 serotransferrin Oryctolagus cuniculus 33-44 24264114-2 1984 In rabbit reticulocytes more than 50% of the transferrin-donated nonheme iron proved to be divalent. Iron 73-77 serotransferrin Oryctolagus cuniculus 45-56 6432569-2 1984 Ouchterlony analysis showed that rabbit tears contain the iron-binding protein transferrin and that tear transferrin has complete antigenic identity with serum and milk transferrin. Iron 58-62 serotransferrin Oryctolagus cuniculus 79-90 6377380-0 1984 [Iron content of the blood and saturation of serum transferrin with iron as affected by roentgen rays]. Iron 68-72 serotransferrin Oryctolagus cuniculus 51-62 6377380-1 1984 Total-body X-irradiation of rabbits with a dose of 4.5 Gy caused appreciable changes in the iron content of blood and iron saturation of blood serum transferrin over a period from 30 min to 30 days. Iron 118-122 serotransferrin Oryctolagus cuniculus 149-160 6743230-0 1984 The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes. Iron 18-22 serotransferrin Oryctolagus cuniculus 37-48 6743230-3 1984 At 4 degrees C the average value for the association constant for the binding of transferrin to reticulocytes was found to increase with increasing iron content of the protein. Iron 148-152 serotransferrin Oryctolagus cuniculus 81-92 6743230-4 1984 The association constant for apotransferrin binding was 4.6 X 10(6)M-1, for monoferric (C-terminal iron) 2.5 X 10(7)M-1, for monoferric (N-terminal iron) 2.8 X 10(7)M-1 and for diferric transferrin, 1.1 X 10(8)M-1. Iron 148-152 serotransferrin Oryctolagus cuniculus 32-43 7119114-1 1982 Rabbit transferrin in vitro is shown to load ferrous iron at random on its specific binding sites. Iron 53-57 serotransferrin Oryctolagus cuniculus 7-18 6885764-5 1983 During this period, most of the iron originally present in transferrin is donated to the cell. Iron 32-36 serotransferrin Oryctolagus cuniculus 59-70 6885764-6 1983 The half-time of 59Fe release from transferrin was 43 s. After the initial 60 s, transferrin, now devoid of iron, is released into the medium. Iron 108-112 serotransferrin Oryctolagus cuniculus 81-92 6885764-8 1983 The iron released from transferrin could be transiently found in the cell plasma membrane, the cytosol, and the mitochondria. Iron 4-8 serotransferrin Oryctolagus cuniculus 23-34 6885764-10 1983 Finally, the iron was incorporated into heme with a half-time of incorporation of 173 s. We conclude that the release of iron from transferrin is one of the fastest events occurring after the initial binding of transferrin. Iron 13-17 serotransferrin Oryctolagus cuniculus 131-142 6885764-10 1983 Finally, the iron was incorporated into heme with a half-time of incorporation of 173 s. We conclude that the release of iron from transferrin is one of the fastest events occurring after the initial binding of transferrin. Iron 13-17 serotransferrin Oryctolagus cuniculus 211-222 6885764-10 1983 Finally, the iron was incorporated into heme with a half-time of incorporation of 173 s. We conclude that the release of iron from transferrin is one of the fastest events occurring after the initial binding of transferrin. Iron 121-125 serotransferrin Oryctolagus cuniculus 131-142 6885764-10 1983 Finally, the iron was incorporated into heme with a half-time of incorporation of 173 s. We conclude that the release of iron from transferrin is one of the fastest events occurring after the initial binding of transferrin. Iron 121-125 serotransferrin Oryctolagus cuniculus 211-222 6885764-11 1983 The limiting step in the entire process of iron delivery is the dissociation of apotransferrin from its receptor, a step which will enable the latter to undergo another cycle of transferrin binding. Iron 43-47 serotransferrin Oryctolagus cuniculus 83-94 6135697-0 1983 The kinetics of transferrin endocytosis and iron uptake from transferrin in rabbit reticulocytes. Iron 44-48 serotransferrin Oryctolagus cuniculus 61-72 6135697-7 1983 Reticulocytes accumulate iron atoms from diferric transferrin at twice the rate at which transferrin molecules are internalized, implying that iron enters the cell while still bound to transferrin. Iron 25-29 serotransferrin Oryctolagus cuniculus 50-61 6135697-7 1983 Reticulocytes accumulate iron atoms from diferric transferrin at twice the rate at which transferrin molecules are internalized, implying that iron enters the cell while still bound to transferrin. Iron 143-147 serotransferrin Oryctolagus cuniculus 50-61 6135697-7 1983 Reticulocytes accumulate iron atoms from diferric transferrin at twice the rate at which transferrin molecules are internalized, implying that iron enters the cell while still bound to transferrin. Iron 143-147 serotransferrin Oryctolagus cuniculus 89-100 6135697-7 1983 Reticulocytes accumulate iron atoms from diferric transferrin at twice the rate at which transferrin molecules are internalized, implying that iron enters the cell while still bound to transferrin. Iron 143-147 serotransferrin Oryctolagus cuniculus 89-100 6135697-8 1983 The activation energies for iron accumulation from transferrin are similar to those of endocytosis of transferrin. Iron 28-32 serotransferrin Oryctolagus cuniculus 51-62 6135697-8 1983 The activation energies for iron accumulation from transferrin are similar to those of endocytosis of transferrin. Iron 28-32 serotransferrin Oryctolagus cuniculus 102-113 6135697-9 1983 This study provides further evidence that transferrin-iron enters the cell by receptor-mediated endocytosis and that iron release occurs within the cell. Iron 54-58 serotransferrin Oryctolagus cuniculus 42-53 6307387-0 1983 Effect of pH and iron content of transferrin on its binding to reticulocyte receptors. Iron 17-21 serotransferrin Oryctolagus cuniculus 33-44 6307387-5 1983 It is proposed that the high affinity of apotransferrin for its receptor at lower pH values and low affinity at pH 7.0 or above allow transferrin to remain bound to the receptor when it is within acidic intracellular vesicles, even after loss of its iron, but also allow ready release from the cell membrane when it is exteriorized by exocytosis after iron uptake. Iron 250-254 serotransferrin Oryctolagus cuniculus 44-55 6307387-5 1983 It is proposed that the high affinity of apotransferrin for its receptor at lower pH values and low affinity at pH 7.0 or above allow transferrin to remain bound to the receptor when it is within acidic intracellular vesicles, even after loss of its iron, but also allow ready release from the cell membrane when it is exteriorized by exocytosis after iron uptake. Iron 352-356 serotransferrin Oryctolagus cuniculus 44-55 6310669-10 1983 It is concluded that iron-containing transferrin molecules enter the trophoblast cells by endocytosis or via a canalicular system after binding to cell membrane receptors. Iron 21-25 serotransferrin Oryctolagus cuniculus 37-48 6310669-11 1983 The higher affinity of the receptors for diferric transferrin than for apotransferrin explains the difference in amount of transferrin binding found within 15 min of injecting labelled diferric transferrin and that found 45-75 min later when much of the iron had been removed from the transferrin. Iron 254-258 serotransferrin Oryctolagus cuniculus 50-61 6310669-11 1983 The higher affinity of the receptors for diferric transferrin than for apotransferrin explains the difference in amount of transferrin binding found within 15 min of injecting labelled diferric transferrin and that found 45-75 min later when much of the iron had been removed from the transferrin. Iron 254-258 serotransferrin Oryctolagus cuniculus 74-85 6310669-11 1983 The higher affinity of the receptors for diferric transferrin than for apotransferrin explains the difference in amount of transferrin binding found within 15 min of injecting labelled diferric transferrin and that found 45-75 min later when much of the iron had been removed from the transferrin. Iron 254-258 serotransferrin Oryctolagus cuniculus 74-85 6310669-11 1983 The higher affinity of the receptors for diferric transferrin than for apotransferrin explains the difference in amount of transferrin binding found within 15 min of injecting labelled diferric transferrin and that found 45-75 min later when much of the iron had been removed from the transferrin. Iron 254-258 serotransferrin Oryctolagus cuniculus 74-85 6827918-4 1983 The N-terminal monoferric transferrin, however, remained unchanged suggesting that in the process of transferrin uptake by cells, the diferric transferrin releases its iron from the acid-labile site at N-domain first before the other iron from the acid-stable site. Iron 168-172 serotransferrin Oryctolagus cuniculus 101-112 6827918-4 1983 The N-terminal monoferric transferrin, however, remained unchanged suggesting that in the process of transferrin uptake by cells, the diferric transferrin releases its iron from the acid-labile site at N-domain first before the other iron from the acid-stable site. Iron 168-172 serotransferrin Oryctolagus cuniculus 101-112 6827918-4 1983 The N-terminal monoferric transferrin, however, remained unchanged suggesting that in the process of transferrin uptake by cells, the diferric transferrin releases its iron from the acid-labile site at N-domain first before the other iron from the acid-stable site. Iron 234-238 serotransferrin Oryctolagus cuniculus 101-112 6827918-4 1983 The N-terminal monoferric transferrin, however, remained unchanged suggesting that in the process of transferrin uptake by cells, the diferric transferrin releases its iron from the acid-labile site at N-domain first before the other iron from the acid-stable site. Iron 234-238 serotransferrin Oryctolagus cuniculus 101-112 6821651-0 1983 Studies on the partition of transferrin-donated iron in rabbit reticulocytes. Iron 48-52 serotransferrin Oryctolagus cuniculus 28-39 6882755-1 1983 The mechanism by which bipyridine and phenanthroline types of iron chelator inhibit iron uptake from transferrin and iron efflux mediated by pyridoxal isonicotinoyl hydrazone was investigated using rabbit reticulocytes with the aim of providing more information on the normal process of iron uptake by developing erythroid cells. Iron 62-66 serotransferrin Oryctolagus cuniculus 101-112 6882755-1 1983 The mechanism by which bipyridine and phenanthroline types of iron chelator inhibit iron uptake from transferrin and iron efflux mediated by pyridoxal isonicotinoyl hydrazone was investigated using rabbit reticulocytes with the aim of providing more information on the normal process of iron uptake by developing erythroid cells. Iron 84-88 serotransferrin Oryctolagus cuniculus 101-112 6882755-1 1983 The mechanism by which bipyridine and phenanthroline types of iron chelator inhibit iron uptake from transferrin and iron efflux mediated by pyridoxal isonicotinoyl hydrazone was investigated using rabbit reticulocytes with the aim of providing more information on the normal process of iron uptake by developing erythroid cells. Iron 84-88 serotransferrin Oryctolagus cuniculus 101-112 6882755-1 1983 The mechanism by which bipyridine and phenanthroline types of iron chelator inhibit iron uptake from transferrin and iron efflux mediated by pyridoxal isonicotinoyl hydrazone was investigated using rabbit reticulocytes with the aim of providing more information on the normal process of iron uptake by developing erythroid cells. Iron 84-88 serotransferrin Oryctolagus cuniculus 101-112 6882755-2 1983 It was shown that the chelators block cellular uptake by chelating the iron immediately after release from transferrin while it is still in the membrane fraction of the cells. Iron 71-75 serotransferrin Oryctolagus cuniculus 107-118 6882755-3 1983 The iron-chelator is then released from the cells by a process which is very similar to that of transferrin release with respect to kinetics and sensitivity to incubation temperature and the effects of metabolic inhibitors and other chemical reagents. Iron 4-8 serotransferrin Oryctolagus cuniculus 96-107 6305740-0 1983 Binding of transferrin-iron to the plasma membrane of a lactating rabbit mammary gland cell. Iron 23-27 serotransferrin Oryctolagus cuniculus 11-22 7126482-0 1982 Studies on the partition of transferrin-donated iron in rabbit reticulocytes. Iron 48-52 serotransferrin Oryctolagus cuniculus 28-39 7126482-3 1982 The distribution of transferrin-donated iron between the stroma and cytosol compartments of rabbit reticulocytes was studied. Iron 40-44 serotransferrin Oryctolagus cuniculus 20-31 7119114-4 1982 Diferric transferrin, while giving a similar tissue distribution of radioiron, has a plasma iron clearance rate approximately twice that of the monoferric transferrins at low plasma iron concentrations. Iron 73-77 serotransferrin Oryctolagus cuniculus 9-20 7119114-4 1982 Diferric transferrin, while giving a similar tissue distribution of radioiron, has a plasma iron clearance rate approximately twice that of the monoferric transferrins at low plasma iron concentrations. Iron 92-96 serotransferrin Oryctolagus cuniculus 9-20 7119114-8 1982 The molecular behavior of transferrin and its iron over this range was investigated using (125)I-transferrin, [(55)Fe]monoferric transferrin, and [(59)Fe]diferric transferrin. Iron 46-50 serotransferrin Oryctolagus cuniculus 26-37 7119114-12 1982 A formula is proposed for correcting the plasma iron turnover, thereby eliminating the effect of plasma iron concentration, so as to reflect directly the number of tissue transferrin receptors. Iron 48-52 serotransferrin Oryctolagus cuniculus 171-182 7150235-0 1982 Removal of iron from diferric rabbit serum transferrin by rabbit reticulocytes. Iron 11-15 serotransferrin Oryctolagus cuniculus 43-54 7150235-1 1982 When radioiron-labelled transferrin with 55Fe located predominantly in the N-terminal iron-binding site and 59Fe predominantly in the C-terminal iron-binding site was incubated with rabbit reticulocytes, both radioisotopes of iron were removed at similar rates. Iron 10-14 serotransferrin Oryctolagus cuniculus 24-35 7150235-2 1982 Electrophoresis of transferrin samples taken during the course of an incubation, in polyacrylamide gels containing 6 M-urea, showed that iron was removed in a pairwise fashion, giving rise to iron-free transferrin. Iron 137-141 serotransferrin Oryctolagus cuniculus 19-30 7150235-2 1982 Electrophoresis of transferrin samples taken during the course of an incubation, in polyacrylamide gels containing 6 M-urea, showed that iron was removed in a pairwise fashion, giving rise to iron-free transferrin. Iron 137-141 serotransferrin Oryctolagus cuniculus 202-213 7150235-2 1982 Electrophoresis of transferrin samples taken during the course of an incubation, in polyacrylamide gels containing 6 M-urea, showed that iron was removed in a pairwise fashion, giving rise to iron-free transferrin. Iron 192-196 serotransferrin Oryctolagus cuniculus 19-30 7150235-2 1982 Electrophoresis of transferrin samples taken during the course of an incubation, in polyacrylamide gels containing 6 M-urea, showed that iron was removed in a pairwise fashion, giving rise to iron-free transferrin. Iron 192-196 serotransferrin Oryctolagus cuniculus 202-213 7115619-0 1982 Molecular aspects of the binding of absorbed iron to transferrin. Iron 45-49 serotransferrin Oryctolagus cuniculus 53-64 6246947-16 1980 On the basis of these studies we propose that transferrin is first bound to a membrane protein and then delivers iron to a membrane component distinct and separate from the transferrin-binding moiety. Iron 113-117 serotransferrin Oryctolagus cuniculus 46-57 7115619-1 1982 To study the molecular aspects of the binding of absorbed iron to plasma transferrin, 59Fe with high specific activity was administered via intragastric tube to iron-deficient rabbits. Iron 58-62 serotransferrin Oryctolagus cuniculus 73-84 7115619-3 1982 Absorbed iron was bound to circulating transferrin one atom at a time. Iron 9-13 serotransferrin Oryctolagus cuniculus 39-50 7115619-5 1982 Thus, the two sites of transferrin may differ in their ability to load absorbed iron. Iron 80-84 serotransferrin Oryctolagus cuniculus 23-34 6283624-2 1982 This complex was shown to bind and donate its iron to the cells in a manner comparable to native iron-transferrin. Iron 97-101 serotransferrin Oryctolagus cuniculus 102-113 6177316-12 1982 An iron-binding protein with an apparent Mr of 80 000 was shown to be immunologically and structurally identical with serum transferrin. Iron 3-7 serotransferrin Oryctolagus cuniculus 124-135 7462336-0 1980 Effect of changes in the ionic environment of reticulocytes on the uptake of transferrin-bound iron. Iron 34-38 serotransferrin Oryctolagus cuniculus 77-88 7462336-7 1980 It was concluded that low ionic strength inhibits iron uptake primarily by blocking the endocytosis of transferrin. Iron 50-54 serotransferrin Oryctolagus cuniculus 103-114 7462336-10 1980 This action was due to an effect on the release of iron from transferrin, which appeared to be taken up by the cells in a normal manner. Iron 51-55 serotransferrin Oryctolagus cuniculus 61-72 7462336-12 1980 However, with CaCl2 concentrations above 10 mM, iron uptake was inhibited, due to inhibition of transferrin uptake, possibly by blocking endocytosis. Iron 48-52 serotransferrin Oryctolagus cuniculus 96-107 7462336-14 1980 The results are discussed in terms of the possible effects of ionic strength, pH, and ionic composition of the extracellular fluid on the three main steps involved in iron uptake by immature erythroid cells: transferrin-receptor interaction, endocytosis, and iron release from transferrin. Iron 167-171 serotransferrin Oryctolagus cuniculus 277-288 6279159-0 1982 Chemical, but not functional, differences between the iron-binding sites of rabbit transferrin. Iron 54-58 serotransferrin Oryctolagus cuniculus 83-94 6800201-0 1982 Effect of iron saturation on transferrin uptake by reticulocytes. Iron 10-14 serotransferrin Oryctolagus cuniculus 29-40 6800201-2 1982 The presence of iron on the transferrin molecule increases its affinity for and sojourn time on the reticulocyte. Iron 16-20 serotransferrin Oryctolagus cuniculus 28-39 6800201-3 1982 This could be due to selective internalization of iron-containing transferrin molecules. Iron 50-54 serotransferrin Oryctolagus cuniculus 66-77 6800201-6 1982 The results showed that (1) both apotransferrin and iron transferrin enter the cell interior and (2) the amount of intracellular transferrin was primarily controlled by the concentration of membrane-bound transferrin and not by its iron saturation. Iron 52-56 serotransferrin Oryctolagus cuniculus 57-68 6800201-6 1982 The results showed that (1) both apotransferrin and iron transferrin enter the cell interior and (2) the amount of intracellular transferrin was primarily controlled by the concentration of membrane-bound transferrin and not by its iron saturation. Iron 52-56 serotransferrin Oryctolagus cuniculus 57-68 7055537-2 1982 When 59Fe-labelled diferric transferrin is injected into normal, anaemic or hypertransfused, polycythaemic rabbits, iron is removed from diferric transferrin in essentially pairwise fashion. Iron 116-120 serotransferrin Oryctolagus cuniculus 28-39 7055537-4 1982 The return of iron from tissue stores to circulating transferrin occurs one atom at a time to either site of the protein and, possibly, in pairwise fashion as well. Iron 14-18 serotransferrin Oryctolagus cuniculus 53-64 7055537-5 1982 The rate of clearance of iron from diferric transferrin differs from that of monoferric transferrins, and the rates at which iron is returned to empty sites of transferrin also differ, so that serum iron is not a kinetically homogeneous pool in the rabbit. Iron 25-29 serotransferrin Oryctolagus cuniculus 44-55 7225374-2 1981 The experiments were performed with rabbit reticulocytes and iron bound to rabbit transferrin. Iron 61-65 serotransferrin Oryctolagus cuniculus 82-93 7225374-15 1981 The results are considered to support the hypothesis that iron release from transferrin in reticulocytes occurs as a result of protonation of the transferrin within intracellular vesicles. Iron 58-62 serotransferrin Oryctolagus cuniculus 76-87 7225374-15 1981 The results are considered to support the hypothesis that iron release from transferrin in reticulocytes occurs as a result of protonation of the transferrin within intracellular vesicles. Iron 58-62 serotransferrin Oryctolagus cuniculus 146-157 6246947-17 1980 Prior to its release, transferrin markedly depleted of iron is still bound to a component in the plasma membrane. Iron 55-59 serotransferrin Oryctolagus cuniculus 22-33 7378455-5 1980 Trypsin digestion considerably reduced the ability of pig and bovine transferrins to donate iron to rabbit reticulocytes, slightly reduced the iron-donating ability of rabbit transferrin, and had almost no effect on that of human or horse transferrins. Iron 92-96 serotransferrin Oryctolagus cuniculus 69-80 471065-1 1979 Plasma transferrin is involved in iron transport within the circulatory system of vertebrates, and provides an iron source for haemoglobin synthesis and other metabolic requirements. Iron 34-38 serotransferrin Oryctolagus cuniculus 7-18 471065-1 1979 Plasma transferrin is involved in iron transport within the circulatory system of vertebrates, and provides an iron source for haemoglobin synthesis and other metabolic requirements. Iron 111-115 serotransferrin Oryctolagus cuniculus 7-18 221049-4 1979 As the reticulocytes matured there was a parallel decline in their ability to take up transferrin and transferrin iron. Iron 114-118 serotransferrin Oryctolagus cuniculus 102-113 281251-0 1978 Use of iron from transferrin and microbial chelates as substrate for heme synthetase in transformed and primary erythroid cell cultures. Iron 7-11 serotransferrin Oryctolagus cuniculus 17-28 4357566-0 1973 Mossbauer spectroscopy of iron in human and rabbit transferrin. Iron 26-30 serotransferrin Oryctolagus cuniculus 51-62 911316-5 1977 In both experiments, iron uptake by reticulocytes corresponded to utilization of a ferric ion from diferric transferrin before utilization of iron from monoferric transferrin. Iron 21-25 serotransferrin Oryctolagus cuniculus 108-119 831800-6 1977 The rate of transferrin uptake was inhibited to a lesser degree than that of iron uptake, and only when the ATP concentration had fallen below that necessary to inhibit iron uptake. Iron 169-173 serotransferrin Oryctolagus cuniculus 12-23 831800-7 1977 It is concluded that the rate of uptake of transferrin-bound iron by immature erythroid cells is dependent on the intracellular concentration of ATP but is independent of the NADH concentration. Iron 61-65 serotransferrin Oryctolagus cuniculus 43-54 23866-1 1978 Rabbit reticulocyte incorporation of iron from rabbit transferrin was independent of transferrin iron saturation but uptake from human transferrin was saturation dependent. Iron 37-41 serotransferrin Oryctolagus cuniculus 54-65 23866-2 1978 Unlike human transferrin, rabbit transferrin does not surrender its iron from any unique preferred iron-binding site and can be described as functionally homogeneic. Iron 99-103 serotransferrin Oryctolagus cuniculus 33-44 588476-6 1977 Transferrin, 80% saturated with iron, was bound to a greater extent than 10 or 50% saturated transferrin; 10% saturated transferrin was bound more readily than the 50% saturated preparation. Iron 32-36 serotransferrin Oryctolagus cuniculus 0-11 588476-7 1977 The findings are consistent with the presence of a transferrin receptor on the cell membrane of the alveolar macrophage and imply that transferrin may interact directly with this cell type in order to remove or donate iron. Iron 218-222 serotransferrin Oryctolagus cuniculus 51-62 588476-7 1977 The findings are consistent with the presence of a transferrin receptor on the cell membrane of the alveolar macrophage and imply that transferrin may interact directly with this cell type in order to remove or donate iron. Iron 218-222 serotransferrin Oryctolagus cuniculus 135-146 911316-0 1977 Preferential utilization in vitro of iron bound to diferric transferrin by rabbit reticulocytes. Iron 37-41 serotransferrin Oryctolagus cuniculus 60-71 864688-3 1977 There was a close correlation between the iron uptake rate and the rate and amount of transferrin uptake and the amount of the lysophospholipids in the membrane. Iron 42-46 serotransferrin Oryctolagus cuniculus 86-97 864688-7 1977 The present investigation provides evidence that the phospholipid composition of the cell membrane influences the interaction of transferrin with its receptors, the processes of endocytosis and exocytosis whereby transferrin enters and leaves the cells, and the mechanism by which iron is mobilized between its binding to transferrin and incorporation into heme. Iron 281-285 serotransferrin Oryctolagus cuniculus 213-224 864688-7 1977 The present investigation provides evidence that the phospholipid composition of the cell membrane influences the interaction of transferrin with its receptors, the processes of endocytosis and exocytosis whereby transferrin enters and leaves the cells, and the mechanism by which iron is mobilized between its binding to transferrin and incorporation into heme. Iron 281-285 serotransferrin Oryctolagus cuniculus 213-224 831800-2 1977 The mechanism by which the utilization of transferrin-bound iron is linked with cellular metabolism was investigated using rabbit reticulocytes and bone marrow cells. Iron 60-64 serotransferrin Oryctolagus cuniculus 42-53 2617-5 1976 A ferrous iron-transferrin mixture, however, protects only against alpha,alpha-dipyridyl. Iron 10-14 serotransferrin Oryctolagus cuniculus 15-26 1174530-1 1975 The transfer of iron from transferrin to the developing erythrocyte is a research area of high interest and considerable controversy. Iron 16-20 serotransferrin Oryctolagus cuniculus 26-37 1174530-6 1975 The iodotransferrin products exhibit the same iron donation ability, however, evidence was found that the chloramine-T treatment leads to a nonspecific binding of transferrin to the reticulocyte. Iron 46-50 serotransferrin Oryctolagus cuniculus 8-19 1174530-8 1975 Fe(NH4)2(SO4)2 and especially FeCl3 were found to yield nonspecifically bound iron when added to transferrin or serum. Iron 78-82 serotransferrin Oryctolagus cuniculus 97-108 1201218-1 1975 Ethanol, in concentrations of 0.05-0.8 M, inhibited intact human and rabbit reticulocyte protein synthesis in the presence of iron-transferrin for endogenous haem synthesis. Iron 126-130 serotransferrin Oryctolagus cuniculus 131-142 1120101-4 1975 In contrast, diferric and monoferric rabbit transferrin both donated iron to reticulocytes at the same rate, per iron atom. Iron 69-73 serotransferrin Oryctolagus cuniculus 44-55 1120101-4 1975 In contrast, diferric and monoferric rabbit transferrin both donated iron to reticulocytes at the same rate, per iron atom. Iron 113-117 serotransferrin Oryctolagus cuniculus 44-55 5000975-0 1971 A study of iron transfer from rabbit transferrin to reticulocytes using synthetic chelating agents. Iron 11-15 serotransferrin Oryctolagus cuniculus 37-48 4987798-0 1970 The effect of transferrin-free serum on the utilization of iron by rabbit reticulocytes. Iron 59-63 serotransferrin Oryctolagus cuniculus 14-25 4980107-0 1969 The role of iron in the reaction between rabbit transferrin and reticulocytes. Iron 12-16 serotransferrin Oryctolagus cuniculus 48-59 5193731-0 1969 The role of transferrin in placental iron transfer in the rabbit. Iron 37-41 serotransferrin Oryctolagus cuniculus 12-23 5699770-0 1968 Role of transferrin in the placental transfer of iron in the rabbit. Iron 49-53 serotransferrin Oryctolagus cuniculus 8-19 5944900-0 1966 Iron and transferrin distribution and turnover in iron-overloaded rabbits. Iron 50-54 serotransferrin Oryctolagus cuniculus 9-20 21207699-8 2001 Reticulocytes, depleted endogenous-transferrin and then treated by PI-PLC, gave a significant decrease in iron uptake in cytosol and in heme (P < 0.05). Iron 106-110 serotransferrin Oryctolagus cuniculus 35-46 30420554-6 2019 RESULTS: Blast exposure led to a significant fall in iron-bound transferrin in both groups of animals (p<0.001), which remained depressed during the study. Iron 53-57 serotransferrin Oryctolagus cuniculus 64-75 9278258-0 1997 Inhibitory mechanism of lead on transferrin-bound iron uptake by rabbit reticulocytes: a fractal analysis. Iron 50-54 serotransferrin Oryctolagus cuniculus 32-43 9862796-1 1998 BACKGROUND: The translation or stability of the mRNAs from ferritin, maconitase, erythroid aminoevulinate synthase and the transferrin receptor is controlled by the binding of two iron regulatory proteins to a family of hairpin-forming RNA sequences called iron-responsive elements (IREs). Iron 180-184 serotransferrin Oryctolagus cuniculus 123-134 9862796-1 1998 BACKGROUND: The translation or stability of the mRNAs from ferritin, maconitase, erythroid aminoevulinate synthase and the transferrin receptor is controlled by the binding of two iron regulatory proteins to a family of hairpin-forming RNA sequences called iron-responsive elements (IREs). Iron 257-261 serotransferrin Oryctolagus cuniculus 123-134 9448235-6 1997 Infusion of TF caused a dose-dependent increase in the concentration of TF and an increase in the unsaturated iron-binding capacity. Iron 110-114 serotransferrin Oryctolagus cuniculus 12-14 9448235-10 1997 We propose that supplementation of iron-free TF decreases iron-catalyzed redox reactions and may decrease hyperoxic lung injury in the premature. Iron 35-39 serotransferrin Oryctolagus cuniculus 45-47 9448235-10 1997 We propose that supplementation of iron-free TF decreases iron-catalyzed redox reactions and may decrease hyperoxic lung injury in the premature. Iron 58-62 serotransferrin Oryctolagus cuniculus 45-47 9278258-1 1997 Experimental data of transferrin and transferrin-bound iron uptake by rabbit reticulocytes in the presence or absence of extracellular lead is analyzed by means of a fractal model. Iron 55-59 serotransferrin Oryctolagus cuniculus 37-48 9278258-2 1997 A highly significant correlation of fractal dimension (Df) of intracellular transferrin or transferrin-bound iron uptake with varying extracellular concentrations of lead (0 approximately 25 umol/L) was observed (Transferrin: r = 0.897, p = 0.015; transferrin-bound iron: r = 0.947, p = 0.004). Iron 109-113 serotransferrin Oryctolagus cuniculus 91-102 9278258-2 1997 A highly significant correlation of fractal dimension (Df) of intracellular transferrin or transferrin-bound iron uptake with varying extracellular concentrations of lead (0 approximately 25 umol/L) was observed (Transferrin: r = 0.897, p = 0.015; transferrin-bound iron: r = 0.947, p = 0.004). Iron 109-113 serotransferrin Oryctolagus cuniculus 213-224 9278258-2 1997 A highly significant correlation of fractal dimension (Df) of intracellular transferrin or transferrin-bound iron uptake with varying extracellular concentrations of lead (0 approximately 25 umol/L) was observed (Transferrin: r = 0.897, p = 0.015; transferrin-bound iron: r = 0.947, p = 0.004). Iron 109-113 serotransferrin Oryctolagus cuniculus 91-102 9278258-2 1997 A highly significant correlation of fractal dimension (Df) of intracellular transferrin or transferrin-bound iron uptake with varying extracellular concentrations of lead (0 approximately 25 umol/L) was observed (Transferrin: r = 0.897, p = 0.015; transferrin-bound iron: r = 0.947, p = 0.004). Iron 266-270 serotransferrin Oryctolagus cuniculus 76-87 9278258-2 1997 A highly significant correlation of fractal dimension (Df) of intracellular transferrin or transferrin-bound iron uptake with varying extracellular concentrations of lead (0 approximately 25 umol/L) was observed (Transferrin: r = 0.897, p = 0.015; transferrin-bound iron: r = 0.947, p = 0.004). Iron 266-270 serotransferrin Oryctolagus cuniculus 213-224 8856799-0 1996 Transferrin modifies surfactant responsiveness in acute respiratory failure: role of iron-free transferrin as an antioxidant. Iron 85-89 serotransferrin Oryctolagus cuniculus 95-106 8856799-11 1996 In animals exposed to hyperoxia, treatment with iron-free TF decreased malondialdehyde content of BAL. Iron 48-52 serotransferrin Oryctolagus cuniculus 58-60 8856799-1 1996 In respiratory failure, transferrin (TF) with variable iron saturation accumulates in the alveolar space. Iron 55-59 serotransferrin Oryctolagus cuniculus 24-35 8856799-12 1996 We propose that low iron saturation of TF decreases oxidant stress and favors the recovery from respiratory failure. Iron 20-24 serotransferrin Oryctolagus cuniculus 39-41 8856799-1 1996 In respiratory failure, transferrin (TF) with variable iron saturation accumulates in the alveolar space. Iron 55-59 serotransferrin Oryctolagus cuniculus 37-39 8856799-2 1996 Binding free iron to TF may inhibit metal-catalyzed formation of free radicals. Iron 13-17 serotransferrin Oryctolagus cuniculus 21-23 8856799-3 1996 The aim of this study was to evaluate whether the degree of the iron-saturation of TF influences the severity of respiratory failure and surfactant responsiveness. Iron 64-68 serotransferrin Oryctolagus cuniculus 83-85 8856799-7 1996 Administration of Iron-free TF significantly decreased the iron saturation of TF in BAL. Iron 18-22 serotransferrin Oryctolagus cuniculus 28-30 8856799-7 1996 Administration of Iron-free TF significantly decreased the iron saturation of TF in BAL. Iron 18-22 serotransferrin Oryctolagus cuniculus 78-80 8856799-7 1996 Administration of Iron-free TF significantly decreased the iron saturation of TF in BAL. Iron 59-63 serotransferrin Oryctolagus cuniculus 28-30 8856799-7 1996 Administration of Iron-free TF significantly decreased the iron saturation of TF in BAL. Iron 59-63 serotransferrin Oryctolagus cuniculus 78-80 8856799-9 1996 By contrast, in respiratory failure induced by hyperoxia and BAL, iron-free TF improved the efficacy of exogenous surfactant, but Fe(2+)-TF had no effect. Iron 66-70 serotransferrin Oryctolagus cuniculus 76-78 8856799-10 1996 After administration of iron-free TF, surfactant isolated from BAL was more surface-active than surfactant from BAL of the other hyperoxia-treated animals. Iron 24-28 serotransferrin Oryctolagus cuniculus 34-36 8599607-0 1996 Effect of lipid peroxidation on transferrin-free iron uptake by rabbit reticulocytes. Iron 49-53 serotransferrin Oryctolagus cuniculus 32-43 8679654-1 1996 Rabbit erythroid cells can take up non-transferrin-bound iron by a high-affinity and a low-affinity transport mechanism (Hodgson et al. Iron 57-61 serotransferrin Oryctolagus cuniculus 39-50 1535218-1 1992 The reductant dependence of iron mobilization from isolated rabbit reticulocyte endosomes containing diferric transferrin is reported. Iron 28-32 serotransferrin Oryctolagus cuniculus 110-121 7745438-3 1995 Serum transferrin is largely biosynthesized in the liver, and its established physiological role is the transport of iron to tissue sites and delivery of the metal to the interior of cells that have transferrin receptors on their surfaces. Iron 117-121 serotransferrin Oryctolagus cuniculus 6-17 7711032-3 1995 In this report, the effect of H(+)-ATPase inhibitors on iron mobilization is investigated at pH 6.0 in the presence of 15 microM FCCP in order to dissociate 59Fe(III) from transferrin and eliminate the kinetic effects of acidification by the ATPase. Iron 56-60 serotransferrin Oryctolagus cuniculus 172-183 8002525-0 1994 Interaction of transferrin saturated with iron with lung surfactant in respiratory failure. Iron 42-46 serotransferrin Oryctolagus cuniculus 15-26 8002525-4 1994 Unlike serum TF, TF recovered in respiratory failure was saturated with iron (Fe(3+)-TF). Iron 72-76 serotransferrin Oryctolagus cuniculus 17-19 8002525-4 1994 Unlike serum TF, TF recovered in respiratory failure was saturated with iron (Fe(3+)-TF). Iron 72-76 serotransferrin Oryctolagus cuniculus 17-19 8002525-5 1994 Fe(3+)-TF decreased the surface activity of normal surfactant in vitro, whereas iron-free TF had no effect. Iron 80-84 serotransferrin Oryctolagus cuniculus 90-92 8002525-8 1994 In respiratory failure induced by BAL, Fe(3+)-TF deteriorated respiratory failure, whereas iron-free TF had no effect. Iron 91-95 serotransferrin Oryctolagus cuniculus 101-103 8002525-9 1994 In respiratory failure induced by hyperoxia for 48 h, administration of iron-free TF ameliorated the respiratory failure and improved the surface activity in BAL. Iron 72-76 serotransferrin Oryctolagus cuniculus 82-84 8163564-0 1994 Role of membrane surface potential and other factors in the uptake of non-transferrin-bound iron by reticulocytes. Iron 92-96 serotransferrin Oryctolagus cuniculus 74-85 8163564-1 1994 Reticulocytes suspended in low ionic strength media such as isotonic sucrose solution efficiently take up non-transferrin-bound iron and utilize it for heme synthesis. Iron 128-132 serotransferrin Oryctolagus cuniculus 110-121 7685392-1 1993 Ferritin and transferrin receptors are co-ordinately regulated by the same RNA-protein interaction: the conserved iron regulatory element (IRE) in mRNA and the IRE-binding protein (IRE-BP/IRP/FRP/P-90). Iron 114-118 serotransferrin Oryctolagus cuniculus 13-24 1591271-0 1992 Changes in the uptake of transferrin-free and transferrin-bound iron during reticulocyte maturation in vivo and in vitro. Iron 64-68 serotransferrin Oryctolagus cuniculus 25-36 1591271-1 1992 The uptake of non-transferrin-bound iron, Fe(II), transferrin-bound iron, Tf-Fe and transferrin was studied in reticulocytes from anaemic rabbits during maturation and then synchronized regeneration in vivo (following injection of actinomycin D) and while maturing during in vitro incubation. Iron 68-72 serotransferrin Oryctolagus cuniculus 50-61 1591271-0 1992 Changes in the uptake of transferrin-free and transferrin-bound iron during reticulocyte maturation in vivo and in vitro. Iron 64-68 serotransferrin Oryctolagus cuniculus 46-57 1591271-1 1992 The uptake of non-transferrin-bound iron, Fe(II), transferrin-bound iron, Tf-Fe and transferrin was studied in reticulocytes from anaemic rabbits during maturation and then synchronized regeneration in vivo (following injection of actinomycin D) and while maturing during in vitro incubation. Iron 68-72 serotransferrin Oryctolagus cuniculus 50-61 1591271-2 1992 The uptake of Fe(II) and Tf-Fe decreased in parallel with each other and with the reticulocyte count and transferrin uptake during maturation in vivo and in vitro. Iron 14-16 serotransferrin Oryctolagus cuniculus 105-116 2716041-3 1989 The iron binding moiety coincided with the major nontransferrin iron-containing material of endocytic vesicles labeled in vivo by incubation of cells with 59Fe, 125I-labeled transferrin. Iron 4-8 serotransferrin Oryctolagus cuniculus 52-63 1591271-6 1992 The loss of transferrin receptors and the uptake of iron from transferrin during reticulocyte maturation was not associated with a change in the affinity of the receptors for transferrin, in the relative distribution of the receptors between the outer cell membrane and intracellular sites or in the ability of the transferrin molecule to donate two iron atoms to the cell with each intracellular cycle, but the average duration of the cycle increased. Iron 52-56 serotransferrin Oryctolagus cuniculus 62-73 1591271-6 1992 The loss of transferrin receptors and the uptake of iron from transferrin during reticulocyte maturation was not associated with a change in the affinity of the receptors for transferrin, in the relative distribution of the receptors between the outer cell membrane and intracellular sites or in the ability of the transferrin molecule to donate two iron atoms to the cell with each intracellular cycle, but the average duration of the cycle increased. Iron 52-56 serotransferrin Oryctolagus cuniculus 62-73 1591271-6 1992 The loss of transferrin receptors and the uptake of iron from transferrin during reticulocyte maturation was not associated with a change in the affinity of the receptors for transferrin, in the relative distribution of the receptors between the outer cell membrane and intracellular sites or in the ability of the transferrin molecule to donate two iron atoms to the cell with each intracellular cycle, but the average duration of the cycle increased. Iron 52-56 serotransferrin Oryctolagus cuniculus 62-73 2015269-0 1991 Effect of metabolic inhibitors on uptake of non-transferrin-bound iron by reticulocytes. Iron 66-70 serotransferrin Oryctolagus cuniculus 48-59 2015269-1 1991 The relationship between transferrin-free iron uptake and cellular metabolism was investigated using rabbit reticulocytes in which energy metabolism was altered by incubation with metabolic inhibitors (antimycin A, 2,4-dinitrophenol, NaCN, NaN3 and rotenone) or substrates. Iron 42-46 serotransferrin Oryctolagus cuniculus 25-36 2015269-6 1991 It is concluded that the uptake of transferrin-free iron by reticulocytes is dependent on the cellular concentration of ATP and that it crosses the cell membrane by an active, carrier-mediated transport process. Iron 52-56 serotransferrin Oryctolagus cuniculus 35-46 2015269-7 1991 Additional studies were performed using transferrin-bound iron. Iron 58-62 serotransferrin Oryctolagus cuniculus 40-51 2015269-8 1991 The metabolic inhibitors also reduced the uptake of this form of iron but the inhibition could be accounted for entirely by reduction in the rate of transferrin endocytosis. Iron 65-69 serotransferrin Oryctolagus cuniculus 149-160 2046086-6 1991 Apparent rate constants of 0.0075 +/- 0.002 sec-1 and 0.0343 +/- 0.0118 sec-1 were obtained for iron dissociation from transferrin and iron mobilization into the cytosol, respectively. Iron 96-100 serotransferrin Oryctolagus cuniculus 119-130 2046086-7 1991 Iron dissociation from transferrin is the rate-limiting step. Iron 0-4 serotransferrin Oryctolagus cuniculus 23-34 2046086-10 1991 These data indicate that the uptake of iron in reticulocytes is a sequential process, with steps after the internalization of Fe2(III)-transferrin that are distinct from the handling of transferrin. Iron 39-43 serotransferrin Oryctolagus cuniculus 135-146 2390101-0 1990 Effect of lead on the transport of transferrin-free and transferrin-bound iron into rabbit reticulocytes. Iron 74-78 serotransferrin Oryctolagus cuniculus 56-67 2390101-7 1990 Pb also inhibited the uptake of transferrin-bound iron but at higher concentrations (IC50, 4 microM) and the inhibition was less readily reversible. Iron 50-54 serotransferrin Oryctolagus cuniculus 32-43 2108730-1 1990 A recently developed technique combining urea gel electrophoresis with Western immunoblotting has been modified for assessing the relative ability of each iron binding site of rabbit transferrin in delivering iron to rabbit reticulocytes. Iron 155-159 serotransferrin Oryctolagus cuniculus 183-194 2108730-1 1990 A recently developed technique combining urea gel electrophoresis with Western immunoblotting has been modified for assessing the relative ability of each iron binding site of rabbit transferrin in delivering iron to rabbit reticulocytes. Iron 209-213 serotransferrin Oryctolagus cuniculus 183-194 2108730-8 1990 Thus, the transferrin-reticulocyte interaction is sensitive to environmental variables, and such sensitivity may help account for apparent discrepancies in previous studies of the relative iron-donating abilities of the two sites of transferrin. Iron 66-70 serotransferrin Oryctolagus cuniculus 10-21 2128422-5 1990 These findings indicate that the reduction of iron uptake caused by the toxin is due to inhibition of the internalization of surface-located transferrin-transferrin receptor complexes, perhaps due to a disruption of cytoskeleton integrity. Iron 46-50 serotransferrin Oryctolagus cuniculus 141-152 2128422-5 1990 These findings indicate that the reduction of iron uptake caused by the toxin is due to inhibition of the internalization of surface-located transferrin-transferrin receptor complexes, perhaps due to a disruption of cytoskeleton integrity. Iron 46-50 serotransferrin Oryctolagus cuniculus 153-164 1308796-7 1992 Furthermore, although serum iron levels are elevated onefold in the controls under chronic anemia with respect to non-bled animals, the concentration of serum transferrin is only slightly increased; hence, the iron saturation of this protein changes from a 50% to an 80% level. Iron 210-214 serotransferrin Oryctolagus cuniculus 159-170 2108730-8 1990 Thus, the transferrin-reticulocyte interaction is sensitive to environmental variables, and such sensitivity may help account for apparent discrepancies in previous studies of the relative iron-donating abilities of the two sites of transferrin. Iron 66-70 serotransferrin Oryctolagus cuniculus 233-244 2716041-3 1989 The iron binding moiety coincided with the major nontransferrin iron-containing material of endocytic vesicles labeled in vivo by incubation of cells with 59Fe, 125I-labeled transferrin. Iron 64-68 serotransferrin Oryctolagus cuniculus 52-63 3415985-0 1988 Membrane transport of non-transferrin-bound iron by reticulocytes. Iron 44-48 serotransferrin Oryctolagus cuniculus 26-37 3415985-1 1988 The transport of non-transferrin-bound iron into rabbit reticulocytes was investigated by incubating the cells in 0.27 M sucrose with iron labelled with 59Fe. Iron 39-43 serotransferrin Oryctolagus cuniculus 21-32 3415985-3 1988 The iron was taken up by cytosolic, haem and stromal fractions of the cells in greater amounts than transferrin-iron. Iron 112-116 serotransferrin Oryctolagus cuniculus 100-111 3415985-14 1988 It is concluded that the reticulocyte can transport non-transferrin-bound iron into the cytosol by a carrier-mediated process and the question is raised whether the same carrier is utilized by transferrin-iron after its release from the protein. Iron 74-78 serotransferrin Oryctolagus cuniculus 56-67 3415985-14 1988 It is concluded that the reticulocyte can transport non-transferrin-bound iron into the cytosol by a carrier-mediated process and the question is raised whether the same carrier is utilized by transferrin-iron after its release from the protein. Iron 205-209 serotransferrin Oryctolagus cuniculus 193-204 3360800-2 1988 Heme formation in reticulocytes from rabbits and rodents is subject to end product negative feedback regulation: intracellular "free" heme has been shown to control acquisition of transferrin iron for heme synthesis. Iron 192-196 serotransferrin Oryctolagus cuniculus 180-191 3355862-0 1988 Non-transferrin donors of iron for heme synthesis in immature erythroid cells. Iron 26-30 serotransferrin Oryctolagus cuniculus 4-15 3355862-1 1988 The mechanism of iron uptake from several iron-containing compounds by transferrin-depleted rabbit reticulocytes and mouse spleen erythroid cells was investigated. Iron 17-21 serotransferrin Oryctolagus cuniculus 71-82 3355862-1 1988 The mechanism of iron uptake from several iron-containing compounds by transferrin-depleted rabbit reticulocytes and mouse spleen erythroid cells was investigated. Iron 42-46 serotransferrin Oryctolagus cuniculus 71-82 3355862-2 1988 Iron complexes of DL-penicillamine, citrate and six different aroyl hydrazones may be utilized by immature erythroid cells for hemoglobin synthesis, although less efficiently than iron from transferrin. Iron 0-4 serotransferrin Oryctolagus cuniculus 190-201 3355862-2 1988 Iron complexes of DL-penicillamine, citrate and six different aroyl hydrazones may be utilized by immature erythroid cells for hemoglobin synthesis, although less efficiently than iron from transferrin. Iron 180-184 serotransferrin Oryctolagus cuniculus 190-201 3355862-5 1988 Ammonium chloride (NH4Cl) increases intracellular pH and blocks the release or utilization of iron from the internalized transferrin. Iron 94-98 serotransferrin Oryctolagus cuniculus 121-132 3355862-7 1988 Hemin inhibited transferrin iron uptake and heme synthesis, but had a much lesser effect on iron incorporation and heme synthesis from non-transferrin donors of iron. Iron 28-32 serotransferrin Oryctolagus cuniculus 16-27 3355862-8 1988 These results allow us to conclude that transferrin-depleted reticulocytes take up iron from all of the examined non-transferrin iron donors without the involvement of the transferrin/transferrin receptor pathway. Iron 83-87 serotransferrin Oryctolagus cuniculus 40-51 3355862-8 1988 These results allow us to conclude that transferrin-depleted reticulocytes take up iron from all of the examined non-transferrin iron donors without the involvement of the transferrin/transferrin receptor pathway. Iron 129-133 serotransferrin Oryctolagus cuniculus 40-51 3342069-4 1988 Examination of the single-cycle endocytosis of transferrin with pulse-chased technique suggests that DIDS retarded transferrin internalization, iron unloading and transferrin receptor recycling in the cells. Iron 144-148 serotransferrin Oryctolagus cuniculus 47-58 3257741-8 1988 The influx of the partially saturated plasma protein transferrin through disrupted blood-ocular barriers most likely accounts for the increased TIBC in the inflamed eye and could provide some protection against the potentially harmful effects of Fe arising from tissue necrosis and hemolysis subsequent to hemorrhage. Iron 246-248 serotransferrin Oryctolagus cuniculus 53-64 3335579-7 1988 The results provide strong support for the concept that transferrin endocytosis is a necessary step in iron uptake by reticulocytes. Iron 103-107 serotransferrin Oryctolagus cuniculus 56-67