PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 2758070-0 1989 [Properties of silver-containing rat ceruloplasmin]. Silver 15-21 ceruloplasmin Rattus norvegicus 37-51 2625152-1 1989 The antioxidant enzyme ceruloplasmin effect on the state of lipid and peroxide metabolism in rats with alimentary hypercholesterolemia was studied. Peroxides 70-78 ceruloplasmin Rattus norvegicus 23-36 2625152-2 1989 Ceruloplasmin was found to inhibit the development of hyperlipoproteinemia, to decrease the level of free-radical oxidation of lipids and to increase the antioxidant demands of tissues. Free Radicals 101-113 ceruloplasmin Rattus norvegicus 0-13 2719967-0 1989 Bilitranslocase is the protein responsible for the electrogenic movement of sulfobromophthalein in plasma membrane vesicles from rat liver: immunochemical evidence using mono- and poly-clonal antibodies. Sulfobromophthalein 76-95 ceruloplasmin Rattus norvegicus 0-15 2719967-1 1989 Monoclonal antibodies raised against bilitranslocase, may display either inhibitory or enhancing activity on the electrogenic transport of sulfobromophthalein, evoked in rat liver plasma-membrane vesicles by the addition of valinomycin in the presence of K+. Sulfobromophthalein 139-158 ceruloplasmin Rattus norvegicus 37-52 2719967-1 1989 Monoclonal antibodies raised against bilitranslocase, may display either inhibitory or enhancing activity on the electrogenic transport of sulfobromophthalein, evoked in rat liver plasma-membrane vesicles by the addition of valinomycin in the presence of K+. Valinomycin 224-235 ceruloplasmin Rattus norvegicus 37-52 2548436-0 1989 Changes of serum iron transferrin and copper ceruloplasmin in rats given Cu(II)2 (acetylsalicylate)4 during acute inflammation. cu(ii)2 (acetylsalicylate)4 73-100 ceruloplasmin Rattus norvegicus 45-58 2548436-1 1989 Modifications of serum levels of iron transferrin and copper ceruloplasmin after acute inflammation by carrageenan and treatment with acetyl salicylic acid [ASA] or Cu(II)2(acetylsalicylate)4 [Cu(II)2(AS)4] were studied in the rat by EPR spectroscopy. Carrageenan 103-114 ceruloplasmin Rattus norvegicus 61-74 2548436-1 1989 Modifications of serum levels of iron transferrin and copper ceruloplasmin after acute inflammation by carrageenan and treatment with acetyl salicylic acid [ASA] or Cu(II)2(acetylsalicylate)4 [Cu(II)2(AS)4] were studied in the rat by EPR spectroscopy. Aspirin 134-155 ceruloplasmin Rattus norvegicus 61-74 2548436-1 1989 Modifications of serum levels of iron transferrin and copper ceruloplasmin after acute inflammation by carrageenan and treatment with acetyl salicylic acid [ASA] or Cu(II)2(acetylsalicylate)4 [Cu(II)2(AS)4] were studied in the rat by EPR spectroscopy. Aspirin 157-160 ceruloplasmin Rattus norvegicus 61-74 2548436-1 1989 Modifications of serum levels of iron transferrin and copper ceruloplasmin after acute inflammation by carrageenan and treatment with acetyl salicylic acid [ASA] or Cu(II)2(acetylsalicylate)4 [Cu(II)2(AS)4] were studied in the rat by EPR spectroscopy. cu(ii)2(acetylsalicylate)4 165-191 ceruloplasmin Rattus norvegicus 61-74 2548436-4 1989 In these conditions the iron(III) non-heme and copper(II) ceruloplasmin concentration in serum was modified either during inflammation or after treatment with antiphlogistic agents: in carrageenan-injected rats the level of serum iron(III) non-heme was found to be very low, while the copper(II) ceruloplasmin concentration was partially reduced. Iron 24-28 ceruloplasmin Rattus norvegicus 58-71 2548436-4 1989 In these conditions the iron(III) non-heme and copper(II) ceruloplasmin concentration in serum was modified either during inflammation or after treatment with antiphlogistic agents: in carrageenan-injected rats the level of serum iron(III) non-heme was found to be very low, while the copper(II) ceruloplasmin concentration was partially reduced. Iron 24-28 ceruloplasmin Rattus norvegicus 296-309 2548436-4 1989 In these conditions the iron(III) non-heme and copper(II) ceruloplasmin concentration in serum was modified either during inflammation or after treatment with antiphlogistic agents: in carrageenan-injected rats the level of serum iron(III) non-heme was found to be very low, while the copper(II) ceruloplasmin concentration was partially reduced. Iron 230-234 ceruloplasmin Rattus norvegicus 58-71 2616386-4 1989 In rats receiving copper together with ethanol the blood levels of copper, iron and lead were higher than in the rats receiving copper alone, the total and latent iron binding capacity were depressed, the transferrin saturation with iron was increased and the ceruloplasmin content--decreased. Copper 18-24 ceruloplasmin Rattus norvegicus 260-273 2616386-4 1989 In rats receiving copper together with ethanol the blood levels of copper, iron and lead were higher than in the rats receiving copper alone, the total and latent iron binding capacity were depressed, the transferrin saturation with iron was increased and the ceruloplasmin content--decreased. Ethanol 39-46 ceruloplasmin Rattus norvegicus 260-273 2616386-5 1989 Copper protected rats against the action of lead on the following hematologic parameters: hemoglobin concentration, hematocrit, iron concentration, total and latent iron binding capacity, transferrin saturation index, copper concentration and ceruloplasmin activity. Copper 0-6 ceruloplasmin Rattus norvegicus 243-256 2616386-6 1989 Ethanol administration counteracts the protective effect of copper on iron concentration, total and latent iron binding capacity, transferrin saturation index and ceruloplasmin serum content. Ethanol 0-7 ceruloplasmin Rattus norvegicus 163-176 2758070-1 1989 Ceruloplasmin (Cp) was isolated from the sera of albino rats fed with silver nitrate (60 mg/kg of body weight). Silver Nitrate 70-84 ceruloplasmin Rattus norvegicus 0-13 2626984-4 1989 We demonstrated in female Long-Evans-Hooded rats that 4 weeks after implantation with 17 beta-estradiol their serum copper and ceruloplasmin and brain copper levels increased while hepatic copper levels decreased significantly. Estradiol 86-103 ceruloplasmin Rattus norvegicus 127-140 2560608-3 1989 Turpentine injections in rats fed 1 of 4 copper levels increased ceruloplasmin activities, but values were sensitively limited by copper intake. Turpentine 0-10 ceruloplasmin Rattus norvegicus 65-78 2560608-3 1989 Turpentine injections in rats fed 1 of 4 copper levels increased ceruloplasmin activities, but values were sensitively limited by copper intake. Copper 41-47 ceruloplasmin Rattus norvegicus 65-78 2465186-5 1989 In addition, ceruloplasmin synthesis by the uterus may be part of a system transporting copper to the fetus. Copper 88-94 ceruloplasmin Rattus norvegicus 13-26 2516709-5 1989 In irradiated rats, the elevated serum Cu concentration was accompanied by increases in plasma ceruloplasmin, lung Cu concentration, and lung Cu/Zn superoxide dismutase (SOD) activity. Copper 39-41 ceruloplasmin Rattus norvegicus 95-108 2741395-2 1989 Under the pressure of 2 ati content of ceruloplasmin was increased, while concentration of transferrin and content of lipid peroxidation products were decreased in blood serum. 4-Amino-2,2,5,5-tetramethyl-3-imidazoli-ne-1-yloxyl free radical 24-27 ceruloplasmin Rattus norvegicus 39-52 2484349-2 1988 The assay utilized polystyrene immobilized antibody which bound ceruloplasmin which then bound biotinylated antibody. Polystyrenes 19-30 ceruloplasmin Rattus norvegicus 64-77 3046720-3 1988 Streptozotocin treatment resulted in a significant decrease in plasma insulin and ceruloplasmin, and pancreatic Cu, protein, and Cu-Zn superoxide dismutase activity. Streptozocin 0-14 ceruloplasmin Rattus norvegicus 82-95 3200618-0 1988 [Formation of transferrin and ceruloplasmin in the blood of rats with acute nitrite-induced methemoglobinemia]. Nitrites 76-83 ceruloplasmin Rattus norvegicus 30-43 3655940-5 1987 Actinomycin D blocked the retinoic acid-induced stimulation of ceruloplasmin activity in copper-sufficient rats, but in copper-deficient rats only about half of the increase was blocked when the rats were given copper or copper and retinoic acid. Dactinomycin 0-13 ceruloplasmin Rattus norvegicus 63-76 3118513-4 1987 Gel filtration chromatography of plasma showed binding of gold to albumin, whereas copper was associated with albumin, ceruloplasmin and a protein eluting in the void volume of the Sephadex G-150 column. Copper 83-89 ceruloplasmin Rattus norvegicus 119-132 3655940-0 1987 Induction of ceruloplasmin synthesis by retinoic acid in rats: influence of dietary copper and vitamin A status. Tretinoin 40-53 ceruloplasmin Rattus norvegicus 13-26 3655940-1 1987 Ceruloplasmin, a copper-containing acute phase plasma protein, has been shown to be regulated by 13-cis retinoic acid in rats. Copper 17-23 ceruloplasmin Rattus norvegicus 0-13 3655940-1 1987 Ceruloplasmin, a copper-containing acute phase plasma protein, has been shown to be regulated by 13-cis retinoic acid in rats. Isotretinoin 97-117 ceruloplasmin Rattus norvegicus 0-13 3655940-2 1987 Ceruloplasmin activity was significantly increased within 24 h and remained elevated for at least 72 h after a single injection of 13-cis retinoic acid. Isotretinoin 131-151 ceruloplasmin Rattus norvegicus 0-13 3655940-3 1987 With daily injections of retinoic acid, the ceruloplasmin activity continued to increase for at least 4 d. After 4 d, the activity was four times control levels. Tretinoin 25-38 ceruloplasmin Rattus norvegicus 44-57 3258371-0 1988 Interleukin-1--stimulated induction of ceruloplasmin synthesis in normal and copper-deficient rats. Copper 77-83 ceruloplasmin Rattus norvegicus 39-52 3258371-1 1988 Regulation of ceruloplasmin synthesis by interleukin-1 (IL-1) as influenced by dietary copper status was examined in rats. Copper 87-93 ceruloplasmin Rattus norvegicus 14-27 3258371-2 1988 In copper-sufficient rats, ceruloplasmin oxidase activity did not peak in the serum until at least 24 h after IL-1 was given. Copper 3-9 ceruloplasmin Rattus norvegicus 27-40 3258371-3 1988 The rates of ceruloplasmin synthesis, as measured by pulse labeling with [3H]leucine and immunoprecipitation, peaked 12 h after IL-1 and returned to basal rates by 24 h. Copper had to be given to copper-deficient rats for the IL-1 to induce oxidase activity. Tritium 74-76 ceruloplasmin Rattus norvegicus 13-26 3258371-3 1988 The rates of ceruloplasmin synthesis, as measured by pulse labeling with [3H]leucine and immunoprecipitation, peaked 12 h after IL-1 and returned to basal rates by 24 h. Copper had to be given to copper-deficient rats for the IL-1 to induce oxidase activity. Leucine 77-84 ceruloplasmin Rattus norvegicus 13-26 3258371-3 1988 The rates of ceruloplasmin synthesis, as measured by pulse labeling with [3H]leucine and immunoprecipitation, peaked 12 h after IL-1 and returned to basal rates by 24 h. Copper had to be given to copper-deficient rats for the IL-1 to induce oxidase activity. Copper 170-176 ceruloplasmin Rattus norvegicus 13-26 3258371-3 1988 The rates of ceruloplasmin synthesis, as measured by pulse labeling with [3H]leucine and immunoprecipitation, peaked 12 h after IL-1 and returned to basal rates by 24 h. Copper had to be given to copper-deficient rats for the IL-1 to induce oxidase activity. Copper 196-202 ceruloplasmin Rattus norvegicus 13-26 3258371-7 1988 The induction pattern of ceruloplasmin synthesis by IL-1 was the same in the copper-deficient rats given copper as in copper-sufficient rats. Copper 77-83 ceruloplasmin Rattus norvegicus 25-38 3258371-7 1988 The induction pattern of ceruloplasmin synthesis by IL-1 was the same in the copper-deficient rats given copper as in copper-sufficient rats. Copper 105-111 ceruloplasmin Rattus norvegicus 25-38 3258371-7 1988 The induction pattern of ceruloplasmin synthesis by IL-1 was the same in the copper-deficient rats given copper as in copper-sufficient rats. Copper 105-111 ceruloplasmin Rattus norvegicus 25-38 3258371-8 1988 Actinomycin D blocked the stimulation of ceruloplasmin synthesis by IL-1. Dactinomycin 0-13 ceruloplasmin Rattus norvegicus 41-54 3258371-9 1988 It was concluded that ceruloplasmin is dependent on copper incorporation for oxidase activity, but its synthesis is induced by IL-1 regardless of dietary copper levels, probably by a mechanism involving transcriptional regulation. Copper 52-58 ceruloplasmin Rattus norvegicus 22-35 3655940-5 1987 Actinomycin D blocked the retinoic acid-induced stimulation of ceruloplasmin activity in copper-sufficient rats, but in copper-deficient rats only about half of the increase was blocked when the rats were given copper or copper and retinoic acid. Tretinoin 26-39 ceruloplasmin Rattus norvegicus 63-76 3655940-5 1987 Actinomycin D blocked the retinoic acid-induced stimulation of ceruloplasmin activity in copper-sufficient rats, but in copper-deficient rats only about half of the increase was blocked when the rats were given copper or copper and retinoic acid. Copper 89-95 ceruloplasmin Rattus norvegicus 63-76 3655940-6 1987 By use of pulse-labeling techniques, ceruloplasmin synthesis was shown to increase 1.5-fold after retinoic acid and this increase was blocked by actinomycin D. Tretinoin 98-111 ceruloplasmin Rattus norvegicus 37-50 3655940-6 1987 By use of pulse-labeling techniques, ceruloplasmin synthesis was shown to increase 1.5-fold after retinoic acid and this increase was blocked by actinomycin D. Dactinomycin 145-158 ceruloplasmin Rattus norvegicus 37-50 3655940-7 1987 When vitamin A-deficient rats were repleted with 13-cis retinoic acid for 3 or 5 d, both the ceruloplasmin activity and synthesis were significantly stimulated when compared to the nonrepleted, deficient rats. Vitamin A 5-14 ceruloplasmin Rattus norvegicus 93-106 3655940-7 1987 When vitamin A-deficient rats were repleted with 13-cis retinoic acid for 3 or 5 d, both the ceruloplasmin activity and synthesis were significantly stimulated when compared to the nonrepleted, deficient rats. Isotretinoin 49-69 ceruloplasmin Rattus norvegicus 93-106 3655940-8 1987 Therefore, the dietary components, copper and vitamin A, play an important role in the regulation of plasma ceruloplasmin levels. Copper 35-41 ceruloplasmin Rattus norvegicus 108-121 3655940-8 1987 Therefore, the dietary components, copper and vitamin A, play an important role in the regulation of plasma ceruloplasmin levels. Vitamin A 46-55 ceruloplasmin Rattus norvegicus 108-121 3767988-0 1986 Binding and uptake of copper from ceruloplasmin. Copper 22-28 ceruloplasmin Rattus norvegicus 34-47 3574299-5 1987 The relative amount of the ceruloplasmin gene in mononucleosomal length DNA formed during the mild digestion was 12-25-fold greater than in total rat liver DNA and 25-50-fold greater than in the mononucleosomal DNA (150-175 bp) produced in the course of extensive digestion (80-85% mononucleosomes and 15-20% acid-soluble material) by endogenous Ca2+, Mg2+-DNases. magnesium ion 352-356 ceruloplasmin Rattus norvegicus 27-40 3125311-7 1987 In general, serum copper, ceruloplasmin activity and alpha-tocopherol were correlated with serum cholesterol in these dietary manipulations. Cholesterol 97-108 ceruloplasmin Rattus norvegicus 26-39 3767988-1 1986 Specific binding of [67Cu]ceruloplasmin to plasma membrane containing preparations from rat tissues was shown in the presence of an excess of nonradioactive Cu(II) or ceruloplasmin. cu(ii) 157-163 ceruloplasmin Rattus norvegicus 26-39 4048245-2 1985 oxyphenylbutazone and hydrocortisone on serum CPN levels were investigated. Hydrocortisone 22-36 ceruloplasmin Rattus norvegicus 46-49 3701458-3 1986 Compared to controls, copper-deficient rats had lower hematocrit and ceruloplasmin levels, lower levels of copper and iron in several tissues, higher heart weights and lower spleen weights. Copper 22-28 ceruloplasmin Rattus norvegicus 69-82 3952276-0 1986 [Cyclic nucleotides and lipids in the realization of the radioprotective effect of ceruloplasmin]. Nucleotides, Cyclic 1-19 ceruloplasmin Rattus norvegicus 83-96 3952276-1 1986 Ceruloplasmin administered 60 min before irradiation diminished cAMP and cGMP levels, which were increased by irradiation at LD50 and LD100, and normalized cAMP/cGMP ratio in the rat liver during the first 24 h following irradiation with a dose of 6.24 Gy. Cyclic AMP 64-68 ceruloplasmin Rattus norvegicus 0-13 3952276-1 1986 Ceruloplasmin administered 60 min before irradiation diminished cAMP and cGMP levels, which were increased by irradiation at LD50 and LD100, and normalized cAMP/cGMP ratio in the rat liver during the first 24 h following irradiation with a dose of 6.24 Gy. Cyclic GMP 73-77 ceruloplasmin Rattus norvegicus 0-13 3952276-1 1986 Ceruloplasmin administered 60 min before irradiation diminished cAMP and cGMP levels, which were increased by irradiation at LD50 and LD100, and normalized cAMP/cGMP ratio in the rat liver during the first 24 h following irradiation with a dose of 6.24 Gy. Cyclic AMP 156-160 ceruloplasmin Rattus norvegicus 0-13 3952276-1 1986 Ceruloplasmin administered 60 min before irradiation diminished cAMP and cGMP levels, which were increased by irradiation at LD50 and LD100, and normalized cAMP/cGMP ratio in the rat liver during the first 24 h following irradiation with a dose of 6.24 Gy. Cyclic GMP 161-165 ceruloplasmin Rattus norvegicus 0-13 3952276-2 1986 The content of phospholipids increased and that of cholesterol decreased under the effect of ceruloplasmin leading to normalization of the molar cholesterol/phospholipid ratio in the rat liver on the 7th day of radiation sickness (LD50, 6.24 Gy). Phospholipids 15-28 ceruloplasmin Rattus norvegicus 93-106 3952276-2 1986 The content of phospholipids increased and that of cholesterol decreased under the effect of ceruloplasmin leading to normalization of the molar cholesterol/phospholipid ratio in the rat liver on the 7th day of radiation sickness (LD50, 6.24 Gy). Cholesterol 51-62 ceruloplasmin Rattus norvegicus 93-106 3952276-2 1986 The content of phospholipids increased and that of cholesterol decreased under the effect of ceruloplasmin leading to normalization of the molar cholesterol/phospholipid ratio in the rat liver on the 7th day of radiation sickness (LD50, 6.24 Gy). Cholesterol 145-156 ceruloplasmin Rattus norvegicus 93-106 3952276-2 1986 The content of phospholipids increased and that of cholesterol decreased under the effect of ceruloplasmin leading to normalization of the molar cholesterol/phospholipid ratio in the rat liver on the 7th day of radiation sickness (LD50, 6.24 Gy). Phospholipids 15-27 ceruloplasmin Rattus norvegicus 93-106 4048245-2 1985 oxyphenylbutazone and hydrocortisone on serum CPN levels were investigated. Oxyphenbutazone 0-17 ceruloplasmin Rattus norvegicus 46-49 3746460-3 1986 Compared with control rats, copper-deficient rats had lower hematocrits, lower ceruloplasmin levels, lower tissue levels of copper and increased hepatic iron levels. Copper 28-34 ceruloplasmin Rattus norvegicus 79-92 2987669-2 1985 These clones were identified using, i) plaque hybridization with [32P] cDNA transcribed from highly purified rat ceruloplasmin (Cp) mRNA; ii) blot hybridization of the restriction fragments of recombinant DNAs with Cp cDNA and iii) hybridization selection of Cp mRNA followed by its cell-free translation. Phosphorus-32 66-69 ceruloplasmin Rattus norvegicus 113-126 3925789-6 1985 Plots of percent dose and 67Cu specific activity against time showed that copper followed a very specific pathway after binding to albumin and transcuprein, entering mainly the liver, then reappearing in the plasma on ceruloplasmin, and then achieving peak distribution in peripheral tissues (muscles, brain, etc.). Copper 74-80 ceruloplasmin Rattus norvegicus 218-231 3925789-9 1985 Even after 7-12 days, tracer copper in plasma was still found exclusively with ceruloplasmin. Copper 29-35 ceruloplasmin Rattus norvegicus 79-92 3857634-3 1985 13-cis-Retinoic acid (160 mg/kg, orally) given daily increased serum ceruloplasmin 2.2 and 2.7 times that found in nontreated arthritic rats when given alone and with zinc (2 mg/kg, intraperitoneally), respectively. Isotretinoin 0-20 ceruloplasmin Rattus norvegicus 69-82 2485269-13 1985 Since RSV competes with BSP for binding to bilitranslocase in vitro, the data are interpreted as suggesting that reduced bilitranslocase function might underlie the delayed RSV plasma clearance and the exacerbated unconjugated hyperbilirubinaemia present in Gilbert"s syndrome. rifamycin SV 6-9 ceruloplasmin Rattus norvegicus 43-58 2485269-13 1985 Since RSV competes with BSP for binding to bilitranslocase in vitro, the data are interpreted as suggesting that reduced bilitranslocase function might underlie the delayed RSV plasma clearance and the exacerbated unconjugated hyperbilirubinaemia present in Gilbert"s syndrome. rifamycin SV 6-9 ceruloplasmin Rattus norvegicus 121-136 2485269-13 1985 Since RSV competes with BSP for binding to bilitranslocase in vitro, the data are interpreted as suggesting that reduced bilitranslocase function might underlie the delayed RSV plasma clearance and the exacerbated unconjugated hyperbilirubinaemia present in Gilbert"s syndrome. rifamycin SV 173-176 ceruloplasmin Rattus norvegicus 121-136 3994509-5 1985 Pregnant rats exposed to oral cadmium revealed decreased serum zinc and iron concentration as well as reduced ceruloplasmin activity. Cadmium 30-37 ceruloplasmin Rattus norvegicus 110-123 6332319-2 1984 Ceruloplasmin is a serum constituent which possesses scavenging activity toward oxygen radicals. Reactive Oxygen Species 80-95 ceruloplasmin Rattus norvegicus 0-13 3840503-7 1985 Purified preparations of bilitranslocase, a liver plasma-membrane protein involved in bilirubin and sulfobromophthalein (BSP) transport, specifically bound NA and the drug competitively inhibited BSP uptake in rat liver plasma membrane vesicles (Ki = 50 nM). Bilirubin 86-95 ceruloplasmin Rattus norvegicus 25-40 3840503-7 1985 Purified preparations of bilitranslocase, a liver plasma-membrane protein involved in bilirubin and sulfobromophthalein (BSP) transport, specifically bound NA and the drug competitively inhibited BSP uptake in rat liver plasma membrane vesicles (Ki = 50 nM). Sulfobromophthalein 100-119 ceruloplasmin Rattus norvegicus 25-40 6332319-3 1984 Rats exposed either to continuous 85% oxygen for 7 days or to intermittent hyperbaric oxygen for up to 19 days developed not only enhanced lung antioxidant enzymes but also increased levels of serum ceruloplasmin. Oxygen 38-44 ceruloplasmin Rattus norvegicus 199-212 6332319-3 1984 Rats exposed either to continuous 85% oxygen for 7 days or to intermittent hyperbaric oxygen for up to 19 days developed not only enhanced lung antioxidant enzymes but also increased levels of serum ceruloplasmin. Oxygen 86-92 ceruloplasmin Rattus norvegicus 199-212 6332319-5 1984 Induction of ceruloplasmin may account for some of the anti-inflammatory activities of elevated oxygen tensions. Oxygen 96-102 ceruloplasmin Rattus norvegicus 13-26 6705967-5 1984 The serum proteins, ceruloplasmin, albumin and apotransferrin, also reduced the hemolytic action of copper-ascorbate, the order of effectiveness being; ceruloplasmin greater than albumin greater than apotransferrin. copper-ascorbate 100-116 ceruloplasmin Rattus norvegicus 20-33 6464779-0 1984 Catecholamine stimulation of copper dependent haemolysis: protective action of superoxide dismutase, catalase, hydroxyl radical scavengers and serum proteins (ceruloplasmin, albumin and apotransferrin). Catecholamines 0-13 ceruloplasmin Rattus norvegicus 159-172 6464779-4 1984 The plasma proteins, ceruloplasmin, albumin and apotransferrin, also reduced the copper-catecholamine induced haemolysis. Copper 81-87 ceruloplasmin Rattus norvegicus 21-34 6464779-4 1984 The plasma proteins, ceruloplasmin, albumin and apotransferrin, also reduced the copper-catecholamine induced haemolysis. Catecholamines 88-101 ceruloplasmin Rattus norvegicus 21-34 6743361-10 1984 It is concluded that ceruloplasmin is an important protector against oxygen free radicals. oxygen free radicals 69-89 ceruloplasmin Rattus norvegicus 21-34 6330788-0 1984 [Participation of cyclic nucleotides in realizing the effect of ceruloplasmin during irradiation]. Nucleotides, Cyclic 18-36 ceruloplasmin Rattus norvegicus 64-77 6330788-1 1984 It was shown that a single intraperitoneal administration of human ceruloplasmin 60 min before irradiation (4.22, 5.28 and 7.20 Gy) increases the content of cyclic AMP and cyclic GMP in the thymus and spleen of rats 3 and 6 h following X-irradiation. Cyclic AMP 157-167 ceruloplasmin Rattus norvegicus 67-80 6330788-2 1984 Ceruloplasmin increases the cyclic AMP/cyclic GMP ratio in the above-mentioned rat organs in normal conditions and on radiation pathology. Cyclic AMP 28-38 ceruloplasmin Rattus norvegicus 0-13 6724191-1 1984 The antioxidant enzyme superoxide dismutase (SOD) found in the cytosol of eucaryotic cells and the plasma protein ceruloplasmin are copper containing proteins though to be important in providing protection from oxygen toxicity. Copper 132-138 ceruloplasmin Rattus norvegicus 114-127 6724191-1 1984 The antioxidant enzyme superoxide dismutase (SOD) found in the cytosol of eucaryotic cells and the plasma protein ceruloplasmin are copper containing proteins though to be important in providing protection from oxygen toxicity. Oxygen 211-217 ceruloplasmin Rattus norvegicus 114-127 6724191-2 1984 To investigate the hypothesis that copper deficiency in the rat could result in decreased lung SOD activity and plasma ceruloplasmin concentration resulting in increased susceptibility to O2 lung damage, we performed a series of experiments exposing copper-deficient and control rats to normobaric and hyperbaric hyperoxia. Copper 35-41 ceruloplasmin Rattus norvegicus 119-132 6700377-2 1984 All copper deficient rats, regardless of the dietary carbohydrate, exhibited decreased ceruloplasmin activity and decreased serum copper concentrations. Copper 4-10 ceruloplasmin Rattus norvegicus 87-100 6705967-5 1984 The serum proteins, ceruloplasmin, albumin and apotransferrin, also reduced the hemolytic action of copper-ascorbate, the order of effectiveness being; ceruloplasmin greater than albumin greater than apotransferrin. copper-ascorbate 100-116 ceruloplasmin Rattus norvegicus 152-165 6639990-4 1983 Leucine was found to be the N-terminal amino acid of the ceruloplasmin polypeptide chain. Leucine 0-7 ceruloplasmin Rattus norvegicus 57-70 6889313-6 1983 However, epinephrine was effective in elevating ceruloplasmin levels in the cell cytosol. Epinephrine 9-20 ceruloplasmin Rattus norvegicus 48-61 6626610-2 1983 About 100% of the gangliosides, 30-50% of ceruloplasmin and 3-5% of the glycosides were incorporated into the phospholipid vesicles under these conditions. Phospholipids 110-122 ceruloplasmin Rattus norvegicus 42-55 6889313-7 1983 Incubation with dexamethasone or copper-containing medium resulted in elevated 3H-ceruloplasmin in both cytosol and medium. Dexamethasone 16-29 ceruloplasmin Rattus norvegicus 82-95 6648508-0 1983 The effect of molybdenum upon blood serum enzymatic ceruloplasmin activity in rats. Molybdenum 14-24 ceruloplasmin Rattus norvegicus 52-65 6889313-7 1983 Incubation with dexamethasone or copper-containing medium resulted in elevated 3H-ceruloplasmin in both cytosol and medium. Copper 33-39 ceruloplasmin Rattus norvegicus 82-95 6648508-2 1983 Following 21-day intraperitoneal administration of molybdenum (Na2MoO4 X 2H2O), significant differences in the level of blood serum ceruloplasmin were noted in female rats depending upon the applied dose of molybdenum. Molybdenum 51-61 ceruloplasmin Rattus norvegicus 132-145 6859810-1 1983 The aim of the present study was to find out whether the elevation of the serum ceruloplasmin level, previously described in vitamin-A-deficient rats, is a specific phenomenon. Vitamin A 125-134 ceruloplasmin Rattus norvegicus 80-93 6648508-2 1983 Following 21-day intraperitoneal administration of molybdenum (Na2MoO4 X 2H2O), significant differences in the level of blood serum ceruloplasmin were noted in female rats depending upon the applied dose of molybdenum. na2moo4 x 2h2o 63-77 ceruloplasmin Rattus norvegicus 132-145 6648508-2 1983 Following 21-day intraperitoneal administration of molybdenum (Na2MoO4 X 2H2O), significant differences in the level of blood serum ceruloplasmin were noted in female rats depending upon the applied dose of molybdenum. Molybdenum 207-217 ceruloplasmin Rattus norvegicus 132-145 6860330-1 1983 To test the hypothesis that ferroxidase I (ceruloplasmin) activity is essential for iron mobilization, adult rats were fed a copper sufficient diet with or without the chelating drugs D-penicillamine and triethylenetetramine for 120 days. Iron 84-88 ceruloplasmin Rattus norvegicus 43-56 6859810-3 1983 Concentrations of ceruloplasmin, haptoglobin, and the value of the haptoglobin to albumin ratio are increased in the serum of vitamin-A-deficient rats compared to normal rats. Vitamin A 126-135 ceruloplasmin Rattus norvegicus 18-31 6859810-4 1983 The results suggested that the increased serum level of ceruloplasmin in vitamin-A-deficient rats was due to the presence of inflammation. Vitamin A 73-82 ceruloplasmin Rattus norvegicus 56-69 7306577-0 1981 Circulating ceruloplasmin is an important source of copper for normal and malignant animal cells. Copper 52-58 ceruloplasmin Rattus norvegicus 12-25 7106358-0 1982 The protective action of ceruloplasmin on copper ion stimulated lysis of rat erythrocytes. Copper 42-48 ceruloplasmin Rattus norvegicus 25-38 7329416-2 1981 The content of ceruloplasmin mRNA sequences in poly(A)-containing and poly(A)-free subfractions of heterogeneous nuclear RNA is respectively 1 and 27 molecules per a hepatocyte. Poly A 47-54 ceruloplasmin Rattus norvegicus 15-28 7136956-3 1982 In these experimental conditions we have shown a strong positive correlation between copper and ceruloplasmin, in the serum of both normal and inflamed rats. Copper 85-91 ceruloplasmin Rattus norvegicus 96-109 7306577-1 1981 The relative uptake of copper from ceruloplasmin and non-ceruloplasmin plasma pools, by normal and malignant cells, was investigated in vivo and in vitro, using 64Cu and 67Cu. Copper 23-29 ceruloplasmin Rattus norvegicus 35-48 7329416-2 1981 The content of ceruloplasmin mRNA sequences in poly(A)-containing and poly(A)-free subfractions of heterogeneous nuclear RNA is respectively 1 and 27 molecules per a hepatocyte. Poly A 70-77 ceruloplasmin Rattus norvegicus 15-28 7306577-8 1981 Ceruloplasmin protein was also absorbed by normal and neoplastic rat tissues, but less rapidly than ceruloplasmin copper, as determined by administration of pure [3H]leucine- or [125I]ceruloplasmin. Tritium 163-165 ceruloplasmin Rattus norvegicus 0-13 7329416-3 1981 Heterogeneous nuclear RNA carrying the sequences of ceruloplasmin mRNA sedimented in sucrose gradients containing formamide, as a broad zone around the 56S peak. Sucrose 85-92 ceruloplasmin Rattus norvegicus 52-65 7306577-8 1981 Ceruloplasmin protein was also absorbed by normal and neoplastic rat tissues, but less rapidly than ceruloplasmin copper, as determined by administration of pure [3H]leucine- or [125I]ceruloplasmin. Leucine 166-173 ceruloplasmin Rattus norvegicus 0-13 7306577-11 1981 It is concluded that, at least in rat, ceruloplasmin is the preferred plasma source of copper for normal and malignant cells, and that the copper on ceruloplasmin turns over more rapidly than the protein moiety, a finding consistent with its role as a copper transport protein. Copper 139-145 ceruloplasmin Rattus norvegicus 149-162 7329416-3 1981 Heterogeneous nuclear RNA carrying the sequences of ceruloplasmin mRNA sedimented in sucrose gradients containing formamide, as a broad zone around the 56S peak. formamide 114-123 ceruloplasmin Rattus norvegicus 52-65 7306577-11 1981 It is concluded that, at least in rat, ceruloplasmin is the preferred plasma source of copper for normal and malignant cells, and that the copper on ceruloplasmin turns over more rapidly than the protein moiety, a finding consistent with its role as a copper transport protein. Copper 139-145 ceruloplasmin Rattus norvegicus 149-162 7222096-0 1981 Serum ceruloplasmin in manganese-treated rats. Manganese 23-32 ceruloplasmin Rattus norvegicus 6-19 24271757-0 1981 The response of serum ceruloplasmin to injections of walker 256 tumor cells or turpentine into rats. Turpentine 79-89 ceruloplasmin Rattus norvegicus 22-35 24271757-3 1981 Based upon studies with(67)Cu, the increase in plasma ceruloplasmin seemed to reflect increased production of the enzyme by the livers of rats bearing the tumors. Copper 27-29 ceruloplasmin Rattus norvegicus 54-67 24271757-4 1981 Injections of turpentine also raised plasma ceruloplasmin, but to a significantly lesser extent and normal values were reached within 2 weeks. Turpentine 14-24 ceruloplasmin Rattus norvegicus 44-57 6168902-2 1981 The content of CP-coding sequences in poly(A)-containing and poly(A)-free subfractions of hnRNA was shown to be respectively 1 and 27 equivalents of CP mRNA molecule per one hepatocyte. Poly A 38-45 ceruloplasmin Rattus norvegicus 15-17 6168902-2 1981 The content of CP-coding sequences in poly(A)-containing and poly(A)-free subfractions of hnRNA was shown to be respectively 1 and 27 equivalents of CP mRNA molecule per one hepatocyte. Poly A 38-45 ceruloplasmin Rattus norvegicus 149-151 6168902-2 1981 The content of CP-coding sequences in poly(A)-containing and poly(A)-free subfractions of hnRNA was shown to be respectively 1 and 27 equivalents of CP mRNA molecule per one hepatocyte. Poly A 61-68 ceruloplasmin Rattus norvegicus 15-17 6168902-3 1981 The gel electrophoresis of hnRNA under strongly denaturing conditions with the subsequent transfer of RNA to diazobenzyloxymethyl paper and hybridization with [32P]-cDNA probe showed that CP mRNA sequences were of multiple molecular weight distribution. Phosphorus-32 160-163 ceruloplasmin Rattus norvegicus 188-190 7242525-2 1981 Optimal potassium concentration for the total protein-synthesizing activity and for the synthesis of immunoreactive ceruloplasmin was 96 and 186 mM respectively. Potassium 8-17 ceruloplasmin Rattus norvegicus 116-129 7242525-3 1981 7-methylguanosine 5"-monophosphate caused two-fold inhibition of the cell-free synthesis of ceruloplasmin. 7-methylguanosine-5'-monophosphate 0-34 ceruloplasmin Rattus norvegicus 92-105 7242525-4 1981 Immunoprecipitated ceruloplasmin that was synthesized at optimal potassium concentration was a homogeneous polypeptide of a molecular weight about 84 kD. Potassium 65-74 ceruloplasmin Rattus norvegicus 19-32 7242526-4 1981 10(6) daltons which is large enough to code for a putative precursor of ceruloplasmin (approximately 700 amino acid acids). amino acid acids 105-121 ceruloplasmin Rattus norvegicus 72-85 7202807-0 1981 The protective action of ceruloplasmin on Fe2+ stimulated lysis of rat erythrocytes. ammonium ferrous sulfate 42-46 ceruloplasmin Rattus norvegicus 25-38 7335075-0 1981 [Molecular mechanisms of the control of ceruloplasmin synthesis by estradiol]. Estradiol 67-76 ceruloplasmin Rattus norvegicus 40-53 7335075-4 1981 Cell-free translation of free and membrane-bound polysomes revealed that there is a two-fold increase in the relative rate of CP synthesis by membrane-bound polysomes from estradiol-treated rats, while free polysomes did not contribute to CP synthesis. Estradiol 172-181 ceruloplasmin Rattus norvegicus 126-128 7335075-4 1981 Cell-free translation of free and membrane-bound polysomes revealed that there is a two-fold increase in the relative rate of CP synthesis by membrane-bound polysomes from estradiol-treated rats, while free polysomes did not contribute to CP synthesis. Estradiol 172-181 ceruloplasmin Rattus norvegicus 239-241 7211579-3 1980 Ceruloplasmin oxidase activity appeared to be inhibited in certain cases but rose in all cases except for orally treated rats after 24 h. The initial rise in serum copper was due mainly to copper present on albumin. Copper 164-170 ceruloplasmin Rattus norvegicus 0-13 7449747-0 1980 Modulation oestradiol effects by silver nitrate: inhibition of the adenohypophyseal reaction, block of the ceruloplasmin increase and block of hypothalamic ascorbic acid depletion. Silver Nitrate 33-47 ceruloplasmin Rattus norvegicus 107-120 7449747-5 1980 The possibility of the interaction of polyphenol oxidase(ceruloplasmin), silver nitrate and hypothalamic ascorbic acid in the dopaminergic modulation of the adenohypophyseal reaction to oestradiol is discussed. Estradiol 186-196 ceruloplasmin Rattus norvegicus 57-70 7211579-3 1980 Ceruloplasmin oxidase activity appeared to be inhibited in certain cases but rose in all cases except for orally treated rats after 24 h. The initial rise in serum copper was due mainly to copper present on albumin. Copper 189-195 ceruloplasmin Rattus norvegicus 0-13 7364132-1 1980 The administration of silver nitrate (6.47 mg, i.e. 60 mumol Ag+/rat/day) in food was followed in only two days by a pronounced decrease in polyphenoloxidase activity (ceruloplasmin) in rat serum. Silver Nitrate 22-36 ceruloplasmin Rattus norvegicus 168-181 6783127-0 1980 [Estradiol-induced formation of the polyribosomal complex synthesizing ceruloplasmin in rats]. Estradiol 1-10 ceruloplasmin Rattus norvegicus 71-84 6783127-2 1980 Using radioimmunological methods, it was shown that a 2--3-fold increase of the oxidase activity of CP in the blood induced by estradiol is accompanied by an increase in the amount of nascent CP chains in the polyribosomes. Estradiol 127-136 ceruloplasmin Rattus norvegicus 100-102 6783127-2 1980 Using radioimmunological methods, it was shown that a 2--3-fold increase of the oxidase activity of CP in the blood induced by estradiol is accompanied by an increase in the amount of nascent CP chains in the polyribosomes. Estradiol 127-136 ceruloplasmin Rattus norvegicus 192-194 6783127-4 1980 The values of sedimentation coefficients for the CP-synthesizing polyribosomes in the control and under estradiol induction are identical and make up to 425--430S. Estradiol 104-113 ceruloplasmin Rattus norvegicus 49-51 7364132-2 1980 The administration of copper in the form of copper sulphate (12.7 mg, i.e. 200 mumol Cu2+/rat/day) raised polyphenoloxidase activity (the ceruloplasmin level), the increase being particularly marked on the first four days. Copper 22-28 ceruloplasmin Rattus norvegicus 138-151 7364132-2 1980 The administration of copper in the form of copper sulphate (12.7 mg, i.e. 200 mumol Cu2+/rat/day) raised polyphenoloxidase activity (the ceruloplasmin level), the increase being particularly marked on the first four days. Copper Sulfate 44-59 ceruloplasmin Rattus norvegicus 138-151 7383973-2 1980 Rat ceruloplasmin was purified by a three-step column chromatography procedure, utilizing DEAE-Sepharose, Sepharose CL-6B, and CM-Sephadex A50 columns. deae-sepharose 90-104 ceruloplasmin Rattus norvegicus 4-17 6444734-3 1980 The simultaneous administration of L-thyroxine (0.1 mg/rat/per day) or dried thyroid (but not D-thyroxine) significantly inhibits these changes (adenohypophysis, ceruloplasmin) or completely suppresses them (hypothalamic ascorbic acid). Thyroxine 35-46 ceruloplasmin Rattus norvegicus 162-175 6446099-1 1980 In male and female rats, oestradiol raises adenohypophyseal weight, the thyroxine-binding capacity of the adenohypophyseal proteins and the blood ceruloplasmin (polyphenol oxidase) level and reduces the ascorbic acid concentration in the hypothalamus. Estradiol 25-35 ceruloplasmin Rattus norvegicus 146-159 6446099-3 1980 The simultaneous administration of perphenazine (a dopaminergic neurone inhibitor) potentiates the adenohypophyseal and ceruloplasmin reaction, but does not modify the hypothalamic ascorbic acid reaction. Perphenazine 35-47 ceruloplasmin Rattus norvegicus 120-133 6446099-4 1980 Perphenazine combined with the thyroid hormones blocks the latters" inhibitory effect on the adenohypophyseal, ceruloplasmin and hypothalamic ascorbic acid reaction to oestradiol. Perphenazine 0-12 ceruloplasmin Rattus norvegicus 111-124 7383973-2 1980 Rat ceruloplasmin was purified by a three-step column chromatography procedure, utilizing DEAE-Sepharose, Sepharose CL-6B, and CM-Sephadex A50 columns. sepharose CL 6B 106-121 ceruloplasmin Rattus norvegicus 4-17 7383973-5 1980 A decrease in lysine in rat ceruloplasmin compared with human ceruloplasmin could account for its reduced anodal mobility. Lysine 14-20 ceruloplasmin Rattus norvegicus 28-41 7383973-6 1980 Other differences in the amino acid sequence of the rat ceruloplasmin included an increase in methionine and cystine/cysteine, and a decrease in histidine, tyrosine and tryptophan. Methionine 94-104 ceruloplasmin Rattus norvegicus 56-69 7383973-6 1980 Other differences in the amino acid sequence of the rat ceruloplasmin included an increase in methionine and cystine/cysteine, and a decrease in histidine, tyrosine and tryptophan. Cystine 109-116 ceruloplasmin Rattus norvegicus 56-69 7383973-6 1980 Other differences in the amino acid sequence of the rat ceruloplasmin included an increase in methionine and cystine/cysteine, and a decrease in histidine, tyrosine and tryptophan. Cysteine 117-125 ceruloplasmin Rattus norvegicus 56-69 7383973-6 1980 Other differences in the amino acid sequence of the rat ceruloplasmin included an increase in methionine and cystine/cysteine, and a decrease in histidine, tyrosine and tryptophan. Histidine 145-154 ceruloplasmin Rattus norvegicus 56-69 7383973-6 1980 Other differences in the amino acid sequence of the rat ceruloplasmin included an increase in methionine and cystine/cysteine, and a decrease in histidine, tyrosine and tryptophan. Tyrosine 156-164 ceruloplasmin Rattus norvegicus 56-69 7383973-6 1980 Other differences in the amino acid sequence of the rat ceruloplasmin included an increase in methionine and cystine/cysteine, and a decrease in histidine, tyrosine and tryptophan. Tryptophan 169-179 ceruloplasmin Rattus norvegicus 56-69 91944-1 1979 Poly(A) containing rat liver 21S RNA homogeneous in polyacrylamide gel electrophoresis under denaturing conditions and stimulating the synthesis of ceruloplasmin in a cell-free proteinsynthesizing system, was used as a template for reverse transcription in the presence of T10 primer and highly purified reverse transcriptase from avian myeloblastosis virus. Poly A 0-7 ceruloplasmin Rattus norvegicus 148-161 436807-0 1979 Copper regulation of ceruloplasmin in copper-deficient rats. Copper 0-6 ceruloplasmin Rattus norvegicus 21-34 503063-1 1979 Highly purified preparations of mRNA coding for ceruloplasmin (CP) ere isolated from rat liver polyribosomes using indirect immunoprecipitation of CP polysomes and poly(U)-sepharose chromatography of polysomal RNA. Sepharose 172-181 ceruloplasmin Rattus norvegicus 48-61 503063-1 1979 Highly purified preparations of mRNA coding for ceruloplasmin (CP) ere isolated from rat liver polyribosomes using indirect immunoprecipitation of CP polysomes and poly(U)-sepharose chromatography of polysomal RNA. Sepharose 172-181 ceruloplasmin Rattus norvegicus 63-65 503063-6 1979 The experiments on end-labeling with [3H]borohydride after periodate oxidation whowed that CP mRNA contains 3"-terminal poly(A). [3h]borohydride 37-52 ceruloplasmin Rattus norvegicus 91-93 503063-7 1979 Poly(U)-sepharose chromatography with stepwise temperature elution revealed length heterogeneity of poly(A) consisting of particular, different thermal subfractions of CP mRNA contain poly(A) consisting of 38, 90 and 165 adenylate residue. Poly U 0-8 ceruloplasmin Rattus norvegicus 168-170 503063-7 1979 Poly(U)-sepharose chromatography with stepwise temperature elution revealed length heterogeneity of poly(A) consisting of particular, different thermal subfractions of CP mRNA contain poly(A) consisting of 38, 90 and 165 adenylate residue. Sepharose 8-17 ceruloplasmin Rattus norvegicus 168-170 503063-8 1979 5"-end of CP mRNA is block with inverted 7-methylguanosine (m7G) which is reducible with [3H]borohydride after periodate oxidation. 7-methylguanosine 41-58 ceruloplasmin Rattus norvegicus 10-12 503063-8 1979 5"-end of CP mRNA is block with inverted 7-methylguanosine (m7G) which is reducible with [3H]borohydride after periodate oxidation. [3h]borohydride 89-104 ceruloplasmin Rattus norvegicus 10-12 436807-0 1979 Copper regulation of ceruloplasmin in copper-deficient rats. Copper 38-44 ceruloplasmin Rattus norvegicus 21-34 436807-1 1979 In copper-deficient rats, oral intubation of copper increases the rate of ceruloplasmin synthesis without affecting general synthesis of plasma or liver proteins. Copper 45-51 ceruloplasmin Rattus norvegicus 74-87 436807-5 1979 Thus, at least in deficiency, copper availability controls the rate of synthesis, acitvation, and plasma concentration of ceruloplasmin. Copper 30-36 ceruloplasmin Rattus norvegicus 122-135 456340-3 1979 Incorporation of [3H]-leucine indicated a specific enhancement of ceruloplasmin synthesis in the tumor-bearing rats, and a greater state of activation of the enzyme was also observed. 3h]-leucine 18-29 ceruloplasmin Rattus norvegicus 66-79 208663-8 1978 After injection of histamine to rats the enzyme activity is increased without a simultaneous increase in Cu concentration in the blood serum, i.e. without de novo synthesis of ceruloplasmin. Histamine 19-28 ceruloplasmin Rattus norvegicus 176-189 218778-4 1978 The level of ceruloplasmin was markedly increased after formalin arthritis, after ACTH treatment in controls and in adrenalectomized animals. Formaldehyde 56-64 ceruloplasmin Rattus norvegicus 13-26 26613-3 1978 Ceruloplasmin polyphenol oxidase activity was inhibited by 0.1M phosphate buffer in the mouse, rat and multimammate mouse, but not in the other species. Phosphates 64-73 ceruloplasmin Rattus norvegicus 0-13 658834-3 1978 After this period approximately 20% of total alpha amino nitrogen was released from ceruloplasmin and over 40% from haptoglobin. alpha amino nitrogen 45-65 ceruloplasmin Rattus norvegicus 84-97 151286-4 1978 By themselves, both inhibitors raised the blood ceruloplasmin level and their effect summated with that of oestradiol. Estradiol 107-117 ceruloplasmin Rattus norvegicus 48-61 415444-3 1977 Then lycanol or daonil were used for treatment, serum GOT, GPT, and ceruloplasmin were changes towards normalization, while ceruloplasmin returned to normal values. GLYMIDINE SODIUM 5-12 ceruloplasmin Rattus norvegicus 68-81 415444-3 1977 Then lycanol or daonil were used for treatment, serum GOT, GPT, and ceruloplasmin were changes towards normalization, while ceruloplasmin returned to normal values. GLYMIDINE SODIUM 5-12 ceruloplasmin Rattus norvegicus 124-137 415444-3 1977 Then lycanol or daonil were used for treatment, serum GOT, GPT, and ceruloplasmin were changes towards normalization, while ceruloplasmin returned to normal values. Glyburide 16-22 ceruloplasmin Rattus norvegicus 68-81 415444-3 1977 Then lycanol or daonil were used for treatment, serum GOT, GPT, and ceruloplasmin were changes towards normalization, while ceruloplasmin returned to normal values. Glyburide 16-22 ceruloplasmin Rattus norvegicus 124-137 911889-3 1977 With p-phenylenediamine, ceruloplasmin-like oxidase activity was detected in heart post-mitochondrial and 100 000 X g supernatants in amounts far exceeding those that could be accounted for by residual blood. 4-phenylenediamine 5-23 ceruloplasmin Rattus norvegicus 25-38 911889-7 1977 When pure [3H]leucine-labeled ceruloplasmin was infused intravenously into a copper-deficient rat, radioactivity was concentrated in the heart and brain within 2 h; radioactive counts per g attained 11 and 3 times those of plasma in the two organs, respectively. Tritium 11-13 ceruloplasmin Rattus norvegicus 30-43 911889-7 1977 When pure [3H]leucine-labeled ceruloplasmin was infused intravenously into a copper-deficient rat, radioactivity was concentrated in the heart and brain within 2 h; radioactive counts per g attained 11 and 3 times those of plasma in the two organs, respectively. Leucine 14-21 ceruloplasmin Rattus norvegicus 30-43 911889-7 1977 When pure [3H]leucine-labeled ceruloplasmin was infused intravenously into a copper-deficient rat, radioactivity was concentrated in the heart and brain within 2 h; radioactive counts per g attained 11 and 3 times those of plasma in the two organs, respectively. Copper 77-83 ceruloplasmin Rattus norvegicus 30-43 911889-9 1977 the results suggest that circulating ceruloplasmin (made by the liver) finds its way into the cells of some organs, especially the heart, a phenomenon which may be related to the function of ceruloplasmin to provide copper to the cytochrome oxidase of various tissues. Copper 216-222 ceruloplasmin Rattus norvegicus 37-50 911889-9 1977 the results suggest that circulating ceruloplasmin (made by the liver) finds its way into the cells of some organs, especially the heart, a phenomenon which may be related to the function of ceruloplasmin to provide copper to the cytochrome oxidase of various tissues. Copper 216-222 ceruloplasmin Rattus norvegicus 191-204 144282-0 1977 Effect of oestrogen and ascorbic acid on the serum ceruloplasmin level in rats. Ascorbic Acid 24-37 ceruloplasmin Rattus norvegicus 51-64 144282-2 1977 The simultaneous administration of ascorbic acid in a dose of 10, 20 or 50 mg/rat/day in food raises the ceruloplasmin concentration to 180-200% of the control value (no significant difference was observed in the effect of the various doses of ascorbic acid). Ascorbic Acid 35-48 ceruloplasmin Rattus norvegicus 105-118 144282-4 1977 The mechanism by which ascorbic acid potentiates the effect of oestrogens on the ceruloplasmin level is not known. Ascorbic Acid 23-36 ceruloplasmin Rattus norvegicus 81-94 205111-0 1977 Iron and copper metabolism in cancer, as exemplified by changes in ferritin and ceruloplasmin in rats with transplantable tumors. Iron 0-4 ceruloplasmin Rattus norvegicus 80-93 205111-0 1977 Iron and copper metabolism in cancer, as exemplified by changes in ferritin and ceruloplasmin in rats with transplantable tumors. Copper 9-15 ceruloplasmin Rattus norvegicus 80-93 870819-1 1977 Partially purified ceruloplasmin mRNA was isolated using indirect immunoprecipitation of rat liver polysomes and poly(U)-Sepharose chromatography of polysomal RNA. Poly U 113-120 ceruloplasmin Rattus norvegicus 19-32 870819-1 1977 Partially purified ceruloplasmin mRNA was isolated using indirect immunoprecipitation of rat liver polysomes and poly(U)-Sepharose chromatography of polysomal RNA. Sepharose 121-130 ceruloplasmin Rattus norvegicus 19-32 870819-4 1977 The purified ceruloplasmin mRNA migrated as a major homogeneous component with an apparent molecular weight about 1 X 10(6) daltons in polyacrylamide gels containing sodium dodecyl sulfate. polyacrylamide 135-149 ceruloplasmin Rattus norvegicus 13-26 870819-4 1977 The purified ceruloplasmin mRNA migrated as a major homogeneous component with an apparent molecular weight about 1 X 10(6) daltons in polyacrylamide gels containing sodium dodecyl sulfate. Sodium Dodecyl Sulfate 166-188 ceruloplasmin Rattus norvegicus 13-26 910112-4 1977 An increase of serum copper was also found during the process of wound healing, but increase in serum copper was probably due to an elevation of ceruloplasmin in serum. Copper 102-108 ceruloplasmin Rattus norvegicus 145-158 533078-0 1979 [Relation between ceruloplasmin and vitamin A in Sprague-Dawley rats]. Vitamin A 36-45 ceruloplasmin Rattus norvegicus 18-31 533078-1 1979 The Moore"s hypothesis concerning a relationship between the metabolism of copper and that of vitamin A led us to consider a possible relationship between this vitamin and ceruloplasmin, the carrier protein for copper. Copper 75-81 ceruloplasmin Rattus norvegicus 172-185 533078-1 1979 The Moore"s hypothesis concerning a relationship between the metabolism of copper and that of vitamin A led us to consider a possible relationship between this vitamin and ceruloplasmin, the carrier protein for copper. Vitamin A 94-103 ceruloplasmin Rattus norvegicus 172-185 533078-1 1979 The Moore"s hypothesis concerning a relationship between the metabolism of copper and that of vitamin A led us to consider a possible relationship between this vitamin and ceruloplasmin, the carrier protein for copper. Copper 211-217 ceruloplasmin Rattus norvegicus 172-185 533078-3 1979 The ceruloplasmin level of control animals and vitamin A - deficient rats was determined An average increase between 22 and 33% was observed in the animals with vitamin A deficiency, the highest levels being observed in the females. Vitamin A 47-56 ceruloplasmin Rattus norvegicus 4-17 533078-9 1979 Could the relationship between ceruloplasmin and vitamin A be possibly due to an inflammatory state in vitamin A deficient rats. Vitamin A 49-58 ceruloplasmin Rattus norvegicus 31-44 533078-9 1979 Could the relationship between ceruloplasmin and vitamin A be possibly due to an inflammatory state in vitamin A deficient rats. Vitamin A 103-112 ceruloplasmin Rattus norvegicus 31-44 140385-0 1977 Effect of interaction of oestrogen, testosterone and thyroid hormones on the serum ceruloplasmin level in rats. Testosterone 36-48 ceruloplasmin Rattus norvegicus 83-96 140385-4 1977 Oestradiol raised adenohypophyseal weight, the binding capacity of the adenohypophyseal proteins for thyroxine and the serum ceruloplasmin level. Estradiol 0-10 ceruloplasmin Rattus norvegicus 125-138 144921-0 1977 Antioestrogenic action of the aldosterone antagonist canrenoate K in the rat (adenohypophysis, ceruloplasmin). canrenoate k 53-65 ceruloplasmin Rattus norvegicus 95-108 144921-1 1977 In a dose of 7,k mg/rat/day in food, the aldosterone antagonist canrenoate K inhibited the adenohypophyseal reaction (growth, raised thyroxine-binding capacity of the adenohypophyseal proteins in vitro) and the ceruloplasmin reaction (elevation of the serum ceruloplasmin level) to three weeks" intramuscular administration of long-acting oestradiol benzoate in doses of 1 mg twice a week. Canrenoic Acid 64-74 ceruloplasmin Rattus norvegicus 211-224 144921-1 1977 In a dose of 7,k mg/rat/day in food, the aldosterone antagonist canrenoate K inhibited the adenohypophyseal reaction (growth, raised thyroxine-binding capacity of the adenohypophyseal proteins in vitro) and the ceruloplasmin reaction (elevation of the serum ceruloplasmin level) to three weeks" intramuscular administration of long-acting oestradiol benzoate in doses of 1 mg twice a week. Canrenoic Acid 64-74 ceruloplasmin Rattus norvegicus 258-271 420513-0 1979 Serum ceruloplasmin concentrations in rats with primary and transplanted sarcomas induced by nickel subsulfide. nickel subsulfide 93-110 ceruloplasmin Rattus norvegicus 6-19 1004686-3 1976 The estrogen-induced increase in the serum ceruloplasmin level, however, was potentiated significantly by all 3 Pimozide doses. Pimozide 112-120 ceruloplasmin Rattus norvegicus 43-56 935620-9 1976 This phenomenon could be explained by the presence of two copper-dependent ferroxidases (ferroxidase I or ceruloplasmin and ferroxidase II) in rat plasma, as recently published. Copper 58-64 ceruloplasmin Rattus norvegicus 106-119 1210102-3 1975 In dificiency of thiamin, caused by a single administration of hydroxythiamin, content of hexosamines and sialic acids were decreased in liver, pancreas and heart; in blood serum content of ceruloplasmin was decreased but that of glycoproteins was increased. Thiamine 17-24 ceruloplasmin Rattus norvegicus 190-203 139624-0 1976 Effect of colchicine and demecolcine on the serum ceruloplasmin level in rats. Colchicine 10-20 ceruloplasmin Rattus norvegicus 50-63 139624-0 1976 Effect of colchicine and demecolcine on the serum ceruloplasmin level in rats. Demecolcine 25-36 ceruloplasmin Rattus norvegicus 50-63 139624-3 1976 The time course of the decrease in the rat serum ceruloplasmin concentration after the same dose of colchicine was then studied. Colchicine 100-110 ceruloplasmin Rattus norvegicus 49-62 139624-5 1976 Eight hours after the administration of colchicine, the serum ceruloplasmin level began to rise again in female rats, but not in male rats. Colchicine 40-50 ceruloplasmin Rattus norvegicus 62-75 1224810-0 1975 [Changes of Cu status and ceruloplasmin activity in mother and suckling rats during a gradual increase of copper supply]. Copper 106-112 ceruloplasmin Rattus norvegicus 26-39 1210102-3 1975 In dificiency of thiamin, caused by a single administration of hydroxythiamin, content of hexosamines and sialic acids were decreased in liver, pancreas and heart; in blood serum content of ceruloplasmin was decreased but that of glycoproteins was increased. Oxythiamine 63-77 ceruloplasmin Rattus norvegicus 190-203 5589074-0 1967 [Effect of administration of griseofulvin on copper and ceruloplasmin in the blood of rats]. Griseofulvin 29-41 ceruloplasmin Rattus norvegicus 56-69 5480864-8 1970 Rat ceruloplasmin, which has little ferroxidase activity, was much less effective than porcine or human ceruloplasmin in inducing increases in plasma iron. Iron 150-154 ceruloplasmin Rattus norvegicus 4-17 4684353-0 1973 Anemia, iron storage and ceruloplasmin in copper nutrition in the growing rat. Copper 42-48 ceruloplasmin Rattus norvegicus 25-38 5060209-0 1972 Distribution of ceruloplasmin- ceruloplasmin-bound 67 Cu in the rat. Copper 55-57 ceruloplasmin Rattus norvegicus 16-29 5060209-0 1972 Distribution of ceruloplasmin- ceruloplasmin-bound 67 Cu in the rat. Copper 55-57 ceruloplasmin Rattus norvegicus 31-44 5436224-0 1970 Effect of some copper antagonists on induction of ceruloplasmin in the rat. Copper 15-21 ceruloplasmin Rattus norvegicus 50-63 5780000-0 1969 Iron and copper effects on serum ceruloplasmin activity of rats with zinc-induced copper deficiency. Iron 0-4 ceruloplasmin Rattus norvegicus 33-46 5780000-0 1969 Iron and copper effects on serum ceruloplasmin activity of rats with zinc-induced copper deficiency. Copper 9-15 ceruloplasmin Rattus norvegicus 33-46 5254228-0 1967 [Experience in studying the synthesis of ceruloplasmin with the use of Cu64 in experimental streptococcal myocarditis in the rat]. cu64 71-75 ceruloplasmin Rattus norvegicus 41-54 33127410-3 2021 Among the mechanisms of defense against oxidative stress, several copper-dependent proteins have been implicated: Cu/Zn-SOD, ceruloplasmin, and metallothionein. Copper 66-72 ceruloplasmin Rattus norvegicus 125-138 33249375-1 2021 BACKGROUND: Ceruloplasmin (Cp) is a major copper-binding protein produced in the liver and delivers copper to extrahepatic organs. Copper 42-48 ceruloplasmin Rattus norvegicus 12-25 33249375-1 2021 BACKGROUND: Ceruloplasmin (Cp) is a major copper-binding protein produced in the liver and delivers copper to extrahepatic organs. Copper 100-106 ceruloplasmin Rattus norvegicus 12-25 32832891-8 2020 Results: At 4 and at 24 hours, curcumin and quercetin have shown protective systemic effects, decreasing significantly the oxidative stress (malondialdehyde level) and stimulating significantly the antioxidant protection (ceruloplasmin and glutathione levels) compared to the group that received only carrageenan. Curcumin 31-39 ceruloplasmin Rattus norvegicus 222-235 32832891-8 2020 Results: At 4 and at 24 hours, curcumin and quercetin have shown protective systemic effects, decreasing significantly the oxidative stress (malondialdehyde level) and stimulating significantly the antioxidant protection (ceruloplasmin and glutathione levels) compared to the group that received only carrageenan. Quercetin 44-53 ceruloplasmin Rattus norvegicus 222-235 31560858-1 2019 Hereditary aceruloplasminemia (HA), related to mutations in the ceruloplasmin (Cp) gene, leads to iron accumulation. Iron 98-102 ceruloplasmin Rattus norvegicus 12-25 31417989-5 2019 Contrary to the hepatic Cu accumulation, the serum Cu concentrations in the neonatal rats were low due to the decreased amount of Cu bound to ceruloplasmin. Copper 51-53 ceruloplasmin Rattus norvegicus 142-155 31417989-5 2019 Contrary to the hepatic Cu accumulation, the serum Cu concentrations in the neonatal rats were low due to the decreased amount of Cu bound to ceruloplasmin. Copper 51-53 ceruloplasmin Rattus norvegicus 142-155 30932415-1 2019 AIM: To investigate the content of essential elements (EE): copper, zinc, magnesium, iron and calcium and the evaluation of the activity of metal-containing enzymes - ceruloplasmin (CP), myeloperoxidase (MPO) and the content of transferrin (TF) in blood plasma (BP) and tumor tissue (TT) of animals with Walker-256 carcinosarcoma treated with lactoferrin (LF). Metals 140-145 ceruloplasmin Rattus norvegicus 167-180 31009842-6 2019 RESULTS: Diet with Cu as nanoparticles resulted in an elevated catalase activity and ferric reducing ability of plasma, however decreased Cu (plasma), and ceruloplasmin (Cp) compared to carbonate. Copper 19-21 ceruloplasmin Rattus norvegicus 155-168 30579253-8 2019 Fangchinoline treatment decreased NO, uric acid, ceruloplasmin, and copper levels, whereas the zinc content was increased. fangchinoline 0-13 ceruloplasmin Rattus norvegicus 49-62 30315404-0 2019 Brain Ceruloplasmin Expression After Experimental Intracerebral Hemorrhage and Protection Against Iron-Induced Brain Injury. Iron 98-102 ceruloplasmin Rattus norvegicus 6-19 30618103-3 2019 Addition of Cu nanoparticles resulted in higher Cp (ceruloplasmin) activity and LOOH (lipid peroxides) and MDA (malondialdehyde) content, as well as decrease the CAT (catalase) activity and level of PC (protein carbonyl), 3-NT (3-nitrotyrosine), 8-OHdG (8-hydroxydeoxyguanosine), GSH + GSSG (total glutathione) and DNA methylation. Copper 12-14 ceruloplasmin Rattus norvegicus 52-65 32148904-4 2019 The usage of flavonoid for 7 days resulted in stabilization of radical oxidation due to reduction of superoxide dismutase activity, maintenance at the high-level catalase activity, and ceruloplasmin concentration in the rat"s blood plasma with experimental bacterial-immune periodontitis. Flavonoids 13-22 ceruloplasmin Rattus norvegicus 186-199 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). Iron 79-83 ceruloplasmin Rattus norvegicus 0-13 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). Iron 79-83 ceruloplasmin Rattus norvegicus 15-17 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ammonium ferrous sulfate 115-122 ceruloplasmin Rattus norvegicus 0-13 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ammonium ferrous sulfate 115-122 ceruloplasmin Rattus norvegicus 15-17 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). Iron 123-127 ceruloplasmin Rattus norvegicus 0-13 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). Iron 123-127 ceruloplasmin Rattus norvegicus 15-17 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ammonium ferrous sulfate 129-133 ceruloplasmin Rattus norvegicus 0-13 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ammonium ferrous sulfate 129-133 ceruloplasmin Rattus norvegicus 15-17 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ferric sulfate 149-160 ceruloplasmin Rattus norvegicus 0-13 30782290-5 2019 Copper-administered animals showed significant increase in brain copper concentration and a depleted Ceruloplasmin level. Copper 0-6 ceruloplasmin Rattus norvegicus 101-114 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ferric sulfate 149-160 ceruloplasmin Rattus norvegicus 15-17 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ferric sulfate 162-166 ceruloplasmin Rattus norvegicus 0-13 30315404-1 2019 Ceruloplasmin (CP) is an essential ferroxidase that is involved in maintaining iron homeostasis by oxidizing toxic ferrous iron (Fe2+) to less-toxic ferric iron (Fe3+). ferric sulfate 162-166 ceruloplasmin Rattus norvegicus 15-17 30315404-3 2019 This research investigated brain CP expression in rats after ICH and the effect of CP on Fe2+-induced brain injury. ammonium ferrous sulfate 89-93 ceruloplasmin Rattus norvegicus 83-85 30315404-10 2019 Exogenous CP reduced Fe2+-induced T2 lesions, blood-brain barrier disruption, brain cell death, and neurological deficits. ammonium ferrous sulfate 21-25 ceruloplasmin Rattus norvegicus 10-12 30002993-7 2018 The levels of lipid peroxidation, uric acid, ceruloplasmin, NO, and PGE2 were significantly reduced following methionine supplementation. Methionine 110-120 ceruloplasmin Rattus norvegicus 45-58 27377930-1 2016 Strongly pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin (CP) ferroxidase activity. silver chloride 47-51 ceruloplasmin Rattus norvegicus 135-137 29177316-0 2017 Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic. Copper 32-38 ceruloplasmin Rattus norvegicus 4-17 29177316-0 2017 Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic. Copper 61-67 ceruloplasmin Rattus norvegicus 4-17 29177316-1 2017 Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. Copper 24-30 ceruloplasmin Rattus norvegicus 0-13 28089327-3 2017 Four primary copper homeostasis genes in mammals: (1) ceruloplasmin (Cp) encoding multifunction multicopper blue (ferr)oxidase; (2) CTR1 encoding high affinity copper importer 1; and (3 and 4) two similar genes encoding Cu(I)/Cu(II)-ATPases P1 type (ATP7A and ATP7B) responsible for copper efflux from the cells and metallation of cuproenzymes formed in the Golgi complex are expressed in MG. Copper 13-19 ceruloplasmin Rattus norvegicus 54-67 28089327-3 2017 Four primary copper homeostasis genes in mammals: (1) ceruloplasmin (Cp) encoding multifunction multicopper blue (ferr)oxidase; (2) CTR1 encoding high affinity copper importer 1; and (3 and 4) two similar genes encoding Cu(I)/Cu(II)-ATPases P1 type (ATP7A and ATP7B) responsible for copper efflux from the cells and metallation of cuproenzymes formed in the Golgi complex are expressed in MG. Copper 101-107 ceruloplasmin Rattus norvegicus 54-67 28089327-3 2017 Four primary copper homeostasis genes in mammals: (1) ceruloplasmin (Cp) encoding multifunction multicopper blue (ferr)oxidase; (2) CTR1 encoding high affinity copper importer 1; and (3 and 4) two similar genes encoding Cu(I)/Cu(II)-ATPases P1 type (ATP7A and ATP7B) responsible for copper efflux from the cells and metallation of cuproenzymes formed in the Golgi complex are expressed in MG. Copper 101-107 ceruloplasmin Rattus norvegicus 54-67 27377930-9 2016 It is concluded that saturation of apo-LF with iron, provided by active CP, can strongly affect its protective capacity. Iron 47-51 ceruloplasmin Rattus norvegicus 72-74 29377294-1 2018 Ceruloplasmin (Cp), an enzyme containing six copper atoms, has important roles in iron homeostasis and antioxidant defense. Copper 45-51 ceruloplasmin Rattus norvegicus 0-13 29377294-1 2018 Ceruloplasmin (Cp), an enzyme containing six copper atoms, has important roles in iron homeostasis and antioxidant defense. Iron 82-86 ceruloplasmin Rattus norvegicus 0-13 29546308-13 2018 Whether these iron intakes perturb copper metabolism is worth considering, especially since copper defi-ciency can impair iron utilization (e.g., by decreasing the ferroxidase activity of ceruloplasmin). Iron 14-18 ceruloplasmin Rattus norvegicus 188-201 29546308-13 2018 Whether these iron intakes perturb copper metabolism is worth considering, especially since copper defi-ciency can impair iron utilization (e.g., by decreasing the ferroxidase activity of ceruloplasmin). Copper 92-98 ceruloplasmin Rattus norvegicus 188-201 29078076-0 2018 Involvement of bilitranslocase and beta-glucuronidase in the vascular protection by hydroxytyrosol and its glucuronide metabolites in oxidative stress conditions. 3,4-dihydroxyphenylethanol 84-98 ceruloplasmin Rattus norvegicus 15-30 29078076-0 2018 Involvement of bilitranslocase and beta-glucuronidase in the vascular protection by hydroxytyrosol and its glucuronide metabolites in oxidative stress conditions. Glucuronides 107-118 ceruloplasmin Rattus norvegicus 15-30 29078076-7 2018 In agreement, bilitranslocase inhibition with 100 muM phenylmethanesulfonyl fluoride for 20 min reduced significantly HT, but not GC, effect on the vascular function upon stress induction. Phenylmethylsulfonyl Fluoride 54-84 ceruloplasmin Rattus norvegicus 14-29 27565173-3 2017 Having ruled out changes in bilirubin metabolism, we demonstrated a 2- to 3-fold increase in serum ceruloplasmin levels, likely accounting for the observed green color. Bilirubin 28-37 ceruloplasmin Rattus norvegicus 99-112 27377930-4 2016 In CP purified from sera of Ag-rats two copper ions were substituted with two silver ions. Copper 40-46 ceruloplasmin Rattus norvegicus 3-5 27377930-4 2016 In CP purified from sera of Ag-rats two copper ions were substituted with two silver ions. Silver 78-84 ceruloplasmin Rattus norvegicus 3-5 28721756-10 2016 Treatments with lycopene in the colitis decreased MDA, total sialic acid and DNA fragmentation levels, while SOD activity (p < 0.05), TAS (in colon p < 0.05; in serum p < 0.01), CPN (p < 0.05) and Fe levels (p < 0.05) were significantly increased. Lycopene 16-24 ceruloplasmin Rattus norvegicus 187-190 27250827-11 2016 In conclusion, downregulation of ferroportin-1 and ceruloplasmin caused by hepcidin enhanced iron-dependent oxidative damage and may be the potential mechanism of SAH. Iron 93-97 ceruloplasmin Rattus norvegicus 51-64 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 ceruloplasmin Rattus norvegicus 53-66 26463975-12 2016 Iron-handling protein levels in the brain, including ceruloplasmin and transferrin, were reduced in the minocycline co-injected animals. Minocycline 104-115 ceruloplasmin Rattus norvegicus 53-66 27116885-5 2015 Decreasing of ceruloplasmin concentration can be used as additional biochemical test in estimation of the state of liver affection at prolonged Simvastatin intake. Simvastatin 144-155 ceruloplasmin Rattus norvegicus 14-27 29782743-5 2016 Analysis of the effect of cytoflavin on activity of the antioxidant system components showed that the level of ceruloplasmin and vitamin E in the blood of animals was reliably (p < 0.05) higher by 10 - 33% than analogous indicator in rats of the control group. cytoflavin 26-36 ceruloplasmin Rattus norvegicus 111-124 26474410-3 2015 In embryonic type copper metabolism (ETCM), newborns accumulate copper to high level in the liver because its excretion via bile is blocked; and serum copper concentration is low because ceruloplasmin (the main copper-containing protein of plasma) gene expression is repressed. Copper 18-24 ceruloplasmin Rattus norvegicus 187-200 26474410-4 2015 In the late weaning, the ETCM switches to the adult type copper metabolism (ATCM), which is manifested by the unlocking of copper excretion and the induction of ceruloplasmin gene activity. Copper 57-63 ceruloplasmin Rattus norvegicus 161-174 25656940-0 2015 Ceruloplasmin is Involved in the Nigral Iron Accumulation of 6-OHDA-Lesioned Rats. Iron 40-44 ceruloplasmin Rattus norvegicus 0-13 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. ammonium ferrous sulfate 57-64 ceruloplasmin Rattus norvegicus 0-13 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. ammonium ferrous sulfate 57-64 ceruloplasmin Rattus norvegicus 15-17 25656940-0 2015 Ceruloplasmin is Involved in the Nigral Iron Accumulation of 6-OHDA-Lesioned Rats. Oxidopamine 61-67 ceruloplasmin Rattus norvegicus 0-13 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. Iron 65-69 ceruloplasmin Rattus norvegicus 0-13 26681075-9 2015 BIL administration significantly decreased plasma levels of C-reactive protein and ceruloplasmin in the AIA-BIL group in comparison to the AIA group. Bilirubin 0-3 ceruloplasmin Rattus norvegicus 83-96 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. Iron 65-69 ceruloplasmin Rattus norvegicus 15-17 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. Ferric enterobactin ion 87-93 ceruloplasmin Rattus norvegicus 0-13 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. Ferric enterobactin ion 87-93 ceruloplasmin Rattus norvegicus 15-17 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. Iron 168-172 ceruloplasmin Rattus norvegicus 0-13 25656940-2 2015 Ceruloplasmin (CP), a ferroxidase, converts highly toxic ferrous iron to its non-toxic ferric form, which cooperated with ferroportin1 (FP1) facilitating the export of iron from cells. Iron 168-172 ceruloplasmin Rattus norvegicus 15-17 25656940-3 2015 To elucidate if the abnormal expression of CP is involved in the nigral iron accumulation, here, we investigated CP expression in the SN of rats lesioned by 6-hydroxydopamine (6-OHDA). Iron 72-76 ceruloplasmin Rattus norvegicus 43-45 25656940-3 2015 To elucidate if the abnormal expression of CP is involved in the nigral iron accumulation, here, we investigated CP expression in the SN of rats lesioned by 6-hydroxydopamine (6-OHDA). Oxidopamine 176-182 ceruloplasmin Rattus norvegicus 43-45 25656940-5 2015 One day after 6-OHDA lesion, when there was a half reduction in the number of dopaminergic neurons, the iron level was increased compared with the normal rats; both the mRNA and protein expressions of CP decreased compared with the control. Oxidopamine 14-20 ceruloplasmin Rattus norvegicus 201-203 25656940-9 2015 These results show that FP1 and CP colocalize in the rat brain, indicating the coordinated actions of the two proteins in the cellular iron export, and suggest that decreased expression of CP in the SN is involved in the nigral iron accumulation of 6-OHDA-lesioned rats. Iron 228-232 ceruloplasmin Rattus norvegicus 32-34 25656940-9 2015 These results show that FP1 and CP colocalize in the rat brain, indicating the coordinated actions of the two proteins in the cellular iron export, and suggest that decreased expression of CP in the SN is involved in the nigral iron accumulation of 6-OHDA-lesioned rats. Iron 228-232 ceruloplasmin Rattus norvegicus 189-191 25656940-9 2015 These results show that FP1 and CP colocalize in the rat brain, indicating the coordinated actions of the two proteins in the cellular iron export, and suggest that decreased expression of CP in the SN is involved in the nigral iron accumulation of 6-OHDA-lesioned rats. Oxidopamine 249-255 ceruloplasmin Rattus norvegicus 32-34 25656940-9 2015 These results show that FP1 and CP colocalize in the rat brain, indicating the coordinated actions of the two proteins in the cellular iron export, and suggest that decreased expression of CP in the SN is involved in the nigral iron accumulation of 6-OHDA-lesioned rats. Oxidopamine 249-255 ceruloplasmin Rattus norvegicus 189-191 26146528-2 2015 With substantia nigral stereotaxic technique and NSCs transplantation, we found that tyrosine hydroxylase and CP expression decreased and iron deposition increased in the lesioned SN after 6-OHDA administration compared with control, while tyrosine hydroxylase and CP expression increased and iron deposition decreased after NSCs transplantation compared to 6-OHDA administration alone. Oxidopamine 189-195 ceruloplasmin Rattus norvegicus 110-112 26146528-2 2015 With substantia nigral stereotaxic technique and NSCs transplantation, we found that tyrosine hydroxylase and CP expression decreased and iron deposition increased in the lesioned SN after 6-OHDA administration compared with control, while tyrosine hydroxylase and CP expression increased and iron deposition decreased after NSCs transplantation compared to 6-OHDA administration alone. Oxidopamine 189-195 ceruloplasmin Rattus norvegicus 265-267 26146528-4 2015 These results suggest that grafted NSCs have an influence on improving the content of CP expression, which may play a neuroprotective role by decreasing iron deposition and ameliorating damage of dopaminergic neurons and possibly underline the iron-related common mechanism of Parkinson"s disease and Wilson"s disease. Iron 153-157 ceruloplasmin Rattus norvegicus 86-88 26146528-4 2015 These results suggest that grafted NSCs have an influence on improving the content of CP expression, which may play a neuroprotective role by decreasing iron deposition and ameliorating damage of dopaminergic neurons and possibly underline the iron-related common mechanism of Parkinson"s disease and Wilson"s disease. Iron 244-248 ceruloplasmin Rattus norvegicus 86-88 26681075-9 2015 BIL administration significantly decreased plasma levels of C-reactive protein and ceruloplasmin in the AIA-BIL group in comparison to the AIA group. aia 104-107 ceruloplasmin Rattus norvegicus 83-96 26681075-9 2015 BIL administration significantly decreased plasma levels of C-reactive protein and ceruloplasmin in the AIA-BIL group in comparison to the AIA group. Bilirubin 108-111 ceruloplasmin Rattus norvegicus 83-96 24363953-3 2013 Increased amounts of nonceruloplasmin-bound Cu were observed in plasma and brain hippocampus together with a higher concentration of ceruloplasmin in plasma, cortex, and hippocampus. Copper 44-46 ceruloplasmin Rattus norvegicus 24-37 25540010-4 2014 Colorimetric and immunoturbidimetric methods were used to determine the concentrations of plasma iron and the proteins involved in its metabolism - ceruloplasmin, transferrin, and ferritin. Iron 97-101 ceruloplasmin Rattus norvegicus 148-161 25008154-3 2014 In Ag-A1 rats, the Ag-diet caused a dramatic decrease of copper status indexes that was manifested as ceruloplasmin-associated copper deficiency. Copper 57-63 ceruloplasmin Rattus norvegicus 102-115 25008154-6 2014 Silver was incorporated into ceruloplasmin (Cp), but not SOD1. Silver 0-6 ceruloplasmin Rattus norvegicus 29-42 25224679-1 2014 BACKGROUND: Ceruloplasmin is a ferroxidase expressed in the central nervous system both as soluble form in the cerebrospinal fluid (CSF) and as membrane-bound GPI-anchored isoform on astrocytes, where it plays a role in iron homeostasis and antioxidant defense. Iron 220-224 ceruloplasmin Rattus norvegicus 12-25 25224679-2 2014 It has been proposed that ceruloplasmin is also able to activate microglial cells with ensuing nitric oxide (NO) production, thereby contributing to neuroinflammatory conditions. Nitric Oxide 95-107 ceruloplasmin Rattus norvegicus 26-39 24374050-0 2014 Protein expression of kidney and liver bilitranslocase in rats exposed to mercuric chloride--a potential tissular biomarker of toxicity. Mercuric Chloride 74-91 ceruloplasmin Rattus norvegicus 39-54 24374050-6 2014 This study was designed to evaluate the renal and hepatic expression of BTL in rats exposed to a nephrotoxic and hepatotoxic dose of HgCl2. Mercuric Chloride 133-138 ceruloplasmin Rattus norvegicus 72-75 24374050-12 2014 In rats treated with HgCl2, immunoblotting showed a significant decrease in the abundance of BTL in homogenates and plasma membranes from kidney and liver. Mercuric Chloride 21-26 ceruloplasmin Rattus norvegicus 93-96 24374050-14 2014 Thus, BTL might be postulated as a new biomarker of tissue toxicity induced by mercury. Mercury 79-86 ceruloplasmin Rattus norvegicus 6-9 24148954-10 2013 Compared with the control group, the lead acetate group had a lower content of CP in the hippocampus (1.23+-0.40 U/mg provs0.78+-0.08 U/mg pro) and 31.81%and 19.49%decreases in CP content and Cu/Zn SOD activity. Acetates 42-49 ceruloplasmin Rattus norvegicus 79-81 24148954-10 2013 Compared with the control group, the lead acetate group had a lower content of CP in the hippocampus (1.23+-0.40 U/mg provs0.78+-0.08 U/mg pro) and 31.81%and 19.49%decreases in CP content and Cu/Zn SOD activity. Acetates 42-49 ceruloplasmin Rattus norvegicus 177-179 24148954-14 2013 The lead acetate + quercetin group had higher Cu/Zn SOD activity and CP content in the hippocampus than the lead acetate group (P < 0.05). Acetates 9-16 ceruloplasmin Rattus norvegicus 69-71 24148954-14 2013 The lead acetate + quercetin group had higher Cu/Zn SOD activity and CP content in the hippocampus than the lead acetate group (P < 0.05). Quercetin 19-28 ceruloplasmin Rattus norvegicus 69-71 23179138-6 2013 Reduction in the level of C-reactive protein, ceruloplasmin and rheumatoid factor were also observed in arthritic rats treated with alginic acid along with reduced lipid peroxidation and enhanced activities of antioxidant enzymes, which suggest the antioxidant potential of the compound. Alginic Acid 132-144 ceruloplasmin Rattus norvegicus 46-59 23801909-1 2013 BACKGROUND: Bilitranslocase (TC 2.A.65.1.1) is a bilirubin-specific membrane transporter, found on absorptive (stomach and intestine) and excretory (kidney and liver) epithelia and in vascular endothelium. Bilirubin 49-58 ceruloplasmin Rattus norvegicus 12-27 26527957-13 2013 2) Sildenafil and Donepezil administration stimulates extracellular AO defense on account of CP. Sildenafil Citrate 3-13 ceruloplasmin Rattus norvegicus 93-95 26527957-13 2013 2) Sildenafil and Donepezil administration stimulates extracellular AO defense on account of CP. Donepezil 18-27 ceruloplasmin Rattus norvegicus 93-95 28911460-7 2014 Also levels of the acute phase protein, ceruloplasmin, were brought to their normal range in DME-treated rats. dimethylethylsilylimidazole 93-96 ceruloplasmin Rattus norvegicus 40-53 23887896-5 2014 The activities of inflammatory marker enzymes like cyclooxygenase, 15-lipoxygenase in monocytes and myeloperoxidase, C-reactive protein and ceruloplasmin levels in serum were found to be decreased on treatment with AL. Aluminum 215-217 ceruloplasmin Rattus norvegicus 140-153 23298529-4 2013 Copper (Cu) plays an important role as prosthetic group of several proteins involved in iron metabolism and antioxidant responses, such as ceruloplasmin (Cp). Copper 0-6 ceruloplasmin Rattus norvegicus 139-152 23298529-4 2013 Copper (Cu) plays an important role as prosthetic group of several proteins involved in iron metabolism and antioxidant responses, such as ceruloplasmin (Cp). Copper 8-10 ceruloplasmin Rattus norvegicus 139-152 23298529-4 2013 Copper (Cu) plays an important role as prosthetic group of several proteins involved in iron metabolism and antioxidant responses, such as ceruloplasmin (Cp). Iron 88-92 ceruloplasmin Rattus norvegicus 139-152 21768302-0 2011 Serum ceruloplasmin protein expression and activity increases in iron-deficient rats and is further enhanced by higher dietary copper intake. Iron 65-69 ceruloplasmin Rattus norvegicus 6-19 22866317-2 2012 The effect of silver ions on copper metabolism was assessed by body weight, relative weight of organs (body weight/organ weight), oxidase activity, content of immunoreactive ceruloplasmin and copper concentration in blood serum, by the expression of copper-transporting protein genes in the liver, and copper and silver distribution in liver and brain cells. Silver 14-20 ceruloplasmin Rattus norvegicus 174-187 21546228-0 2013 The endothelial plasma membrane transporter bilitranslocase mediates rat aortic vasodilation induced by anthocyanins. Anthocyanins 104-116 ceruloplasmin Rattus norvegicus 44-59 21546228-3 2013 We therefore investigated the possible role of bilitranslocase (TC 2.A.65.1.1), an endothelial plasma membrane carrier that transports flavonoids, in the vasodilation activity induced by anthocyanins. Flavonoids 135-145 ceruloplasmin Rattus norvegicus 47-62 21546228-3 2013 We therefore investigated the possible role of bilitranslocase (TC 2.A.65.1.1), an endothelial plasma membrane carrier that transports flavonoids, in the vasodilation activity induced by anthocyanins. Anthocyanins 187-199 ceruloplasmin Rattus norvegicus 47-62 21546228-5 2013 Pre-treatment of aortic rings with anti-sequence bilitranslocase antibodies targeting the carrier, decreased vasodilation induced by cyanidin 3-glucoside and bilberry anthocyanins. cyanidin-3-o-glucoside 133-153 ceruloplasmin Rattus norvegicus 49-64 21546228-5 2013 Pre-treatment of aortic rings with anti-sequence bilitranslocase antibodies targeting the carrier, decreased vasodilation induced by cyanidin 3-glucoside and bilberry anthocyanins. Anthocyanins 167-179 ceruloplasmin Rattus norvegicus 49-64 21546228-6 2013 CONCLUSION: Here we show for the first time that bilitranslocase mediates a critical step in vasodilation induced by anthocyanins. Anthocyanins 117-129 ceruloplasmin Rattus norvegicus 49-64 23470127-0 2012 Bilitranslocase is involved in the uptake of bromosulfophthalein in rat and human liver. Sulfobromophthalein 45-64 ceruloplasmin Rattus norvegicus 0-15 21274654-8 2011 Since alterations in iron levels in the brain are causally linked to degenerative conditions such as Alzheimer"s disease, an improved understanding of the regulation of iron transport protein expression such as FPN1, DMT1, and CP could lead to novel strategies for treatments. Iron 21-25 ceruloplasmin Rattus norvegicus 227-229 21274654-8 2011 Since alterations in iron levels in the brain are causally linked to degenerative conditions such as Alzheimer"s disease, an improved understanding of the regulation of iron transport protein expression such as FPN1, DMT1, and CP could lead to novel strategies for treatments. Iron 169-173 ceruloplasmin Rattus norvegicus 227-229 21768302-0 2011 Serum ceruloplasmin protein expression and activity increases in iron-deficient rats and is further enhanced by higher dietary copper intake. Copper 127-133 ceruloplasmin Rattus norvegicus 6-19 21768302-2 2011 One point of intersection between the 2 metals is the liver-derived, multicopper ferroxidase ceruloplasmin (Cp) that is important for iron release from certain tissues. Iron 134-138 ceruloplasmin Rattus norvegicus 93-106 21355016-1 2011 Ceruloplasmin (Cp), a multicopper ferroxidase, is expressed as both a secreted (sCp) plasma enzyme from the liver and a membrane-bound glycosylphosphatidylinositol-anchored (GPI-Cp) splice variant protein. Glycosylphosphatidylinositols 135-163 ceruloplasmin Rattus norvegicus 0-13 22024494-7 2011 Superoxide dismutase (Sod1) and ceruloplasmin protein were found to be altered by both iron and CuD, whereas CCS and CCS/Sod1 ratio were found to only be altered only in CuD rats and, importantly, after only 1 week of treatment. Iron 87-91 ceruloplasmin Rattus norvegicus 32-45 21332026-3 2011 Here, expression of ceruloplasmin (CP), the major copper-containing protein in blood released by the liver, was investigated. Copper 50-56 ceruloplasmin Rattus norvegicus 20-33 21332026-3 2011 Here, expression of ceruloplasmin (CP), the major copper-containing protein in blood released by the liver, was investigated. Copper 50-56 ceruloplasmin Rattus norvegicus 35-37 21332026-5 2011 The PI3K inhibitor wortmannin counteracted this insulin effect on CP mRNA levels, indicating that the PI3K/Akt cascade is involved in the regulation of CP expression. Wortmannin 19-29 ceruloplasmin Rattus norvegicus 66-68 21332026-5 2011 The PI3K inhibitor wortmannin counteracted this insulin effect on CP mRNA levels, indicating that the PI3K/Akt cascade is involved in the regulation of CP expression. Wortmannin 19-29 ceruloplasmin Rattus norvegicus 152-154 21355016-1 2011 Ceruloplasmin (Cp), a multicopper ferroxidase, is expressed as both a secreted (sCp) plasma enzyme from the liver and a membrane-bound glycosylphosphatidylinositol-anchored (GPI-Cp) splice variant protein. gpi-cp 174-180 ceruloplasmin Rattus norvegicus 0-13 19490425-6 2009 Zn treatment dramatically increased the expression of the metallothionein (Mt), and modestly increased the expression of acute-phase protein genes (ceruloplasmin, Stat3, egr1, Cxc chemokines and heat-shock proteins). Zinc 0-2 ceruloplasmin Rattus norvegicus 148-161 20302851-4 2010 By Cu-overloading, GST-P(+) foci that co-expressed transferrin receptors or downregulated ceruloplasmin increased, suggesting preneoplastic lesion-specific enhancement of oxidative cellular stress. Copper 3-5 ceruloplasmin Rattus norvegicus 90-103 21268857-0 2010 [Characteristics of rat ceruloplasmin from the serum of animals, which received salts of silver with food]. Silver 89-95 ceruloplasmin Rattus norvegicus 24-37 21268857-2 2010 Rodents receiving Ag-salts with food develop extracellular deficiency of copper associated with ceruloplasmin (Cp, the major copper-transporting protein in blood serum of vertebrates). ag-salts 18-26 ceruloplasmin Rattus norvegicus 96-109 20143528-3 2009 The enterosorbents polysorb, litovit, and sapropel have been found to have a corrective effect on the level of the major plasma antioxidant ceruloplasmin in acute ethanol intoxication. Ethanol 163-170 ceruloplasmin Rattus norvegicus 140-153 20110735-4 2010 Bilitranslocase function was studied by measuring the kinetic parameters of electrogenic bromosulfophthalein (BSP) uptake in KBLM and LPM by a spectrophotometric technique. Sulfobromophthalein 89-108 ceruloplasmin Rattus norvegicus 0-15 20110735-4 2010 Bilitranslocase function was studied by measuring the kinetic parameters of electrogenic bromosulfophthalein (BSP) uptake in KBLM and LPM by a spectrophotometric technique. Sulfobromophthalein 110-113 ceruloplasmin Rattus norvegicus 0-15 17235666-1 2007 We demonstrated previously that loading iron into ferritin via its own ferroxidase activity resulted in damage to the ferritin while ferritin loaded by ceruloplasmin, a copper-containing ferroxidase, was not damaged and had similar characteristics to native ferritin (Welch et al. Copper 169-175 ceruloplasmin Rattus norvegicus 152-165 19138444-8 2009 The high-calcium diet increased hepatic copper concentration but decreased plasma copper concentration and ceruloplasmin activity, which was restored by the iron supplementation. Calcium 9-16 ceruloplasmin Rattus norvegicus 107-120 19138444-8 2009 The high-calcium diet increased hepatic copper concentration but decreased plasma copper concentration and ceruloplasmin activity, which was restored by the iron supplementation. Iron 157-161 ceruloplasmin Rattus norvegicus 107-120 18286237-1 2008 A noticeable effect of sulfite treatment was observed on the plasma ceruloplasmin ferroxidase activity of rats with normal sulfite oxidase activity when compared to normal controls. Sulfites 23-30 ceruloplasmin Rattus norvegicus 68-81 17768667-9 2008 Serum ceruloplasmin level was increased due to fenthion administration, but prophylactic and therapeutic melatonin administration inhibited the increase in ceruloplasmin level of serum. Fenthion 47-55 ceruloplasmin Rattus norvegicus 6-19 17768667-9 2008 Serum ceruloplasmin level was increased due to fenthion administration, but prophylactic and therapeutic melatonin administration inhibited the increase in ceruloplasmin level of serum. Melatonin 105-114 ceruloplasmin Rattus norvegicus 156-169 21475473-8 2008 RESULTS: In CII treated group, the levels of LPO, NO, PGE2, UA, CP and Cu were significantly higher, but the levels of SOD, GSH and Zn were significantly lower than controls. N-[(1S)-2-methyl-1-(pyridin-4-ylcarbamoyl)propyl]cyclohexanecarboxamide 12-15 ceruloplasmin Rattus norvegicus 64-66 21475473-9 2008 In CII + Allo treated group, the levels of SOD and GSH were significantly increased, but the levels of PGE2, LPO, NO, UA, Cu and CP were significantly decreased in comparison with CII-treated group. N-[(1S)-2-methyl-1-(pyridin-4-ylcarbamoyl)propyl]cyclohexanecarboxamide 3-6 ceruloplasmin Rattus norvegicus 129-131 21475473-10 2008 The levels of SOD, GSH and Zn were significantly increased, but the levels of PGE2, NO and CP were significantly decreased in the vitamin E treated group in comparison with CII-treated group. Vitamin E 130-139 ceruloplasmin Rattus norvegicus 91-93 23105850-6 2009 In CII group, levels of LPO, NO, PGE(2), UA, CP, Cu were higher while SOD, GSH, Zn were lower than controls. N-[(1S)-2-methyl-1-(pyridin-4-ylcarbamoyl)propyl]cyclohexanecarboxamide 3-6 ceruloplasmin Rattus norvegicus 45-47 23105850-7 2009 In groups treated with vitamin C and GTE, levels of SOD, GSH were increased while levels of LPO, NO, PGE(2), Cu, CP were decreased compared with CII group. Ascorbic Acid 23-32 ceruloplasmin Rattus norvegicus 113-115 23105850-7 2009 In groups treated with vitamin C and GTE, levels of SOD, GSH were increased while levels of LPO, NO, PGE(2), Cu, CP were decreased compared with CII group. gte 37-40 ceruloplasmin Rattus norvegicus 113-115 19154773-12 2009 Finally, DU exposure increased significantly the transporters (Divalent-Metal-Transporter1; DMT1), the storage molecule (ferritin) and the ferroxidase enzyme (ceruloplasmin), but not EU. du 9-11 ceruloplasmin Rattus norvegicus 159-172 19076073-1 2009 In the blood plasma of humans and rats, ceruloplasmin is the major copper-binding protein and ferroxidase, accounting for 70% of the copper present in the plasma, with the rest binding primarily to albumin and a macroglobulin. Copper 67-73 ceruloplasmin Rattus norvegicus 40-53 19076073-1 2009 In the blood plasma of humans and rats, ceruloplasmin is the major copper-binding protein and ferroxidase, accounting for 70% of the copper present in the plasma, with the rest binding primarily to albumin and a macroglobulin. Copper 133-139 ceruloplasmin Rattus norvegicus 40-53 18655007-7 2008 Since the transport activity of the bilitranslocase in kidney basolateral membrane vesicles was competitively inhibited by malvidin 3-glucoside (K(i) = 4.8 +/- 0.2 microM), the anthocyanin uptake from blood into kidney tubular cells is likely to be mediated by the kidney isoform of this organic anion membrane transporter. 3-glucoside 132-143 ceruloplasmin Rattus norvegicus 36-51 18655007-7 2008 Since the transport activity of the bilitranslocase in kidney basolateral membrane vesicles was competitively inhibited by malvidin 3-glucoside (K(i) = 4.8 +/- 0.2 microM), the anthocyanin uptake from blood into kidney tubular cells is likely to be mediated by the kidney isoform of this organic anion membrane transporter. Anthocyanins 177-188 ceruloplasmin Rattus norvegicus 36-51 18375546-9 2008 In addition, chronic exposure to DU induced increased gene expression of ceruloplasmin (x12), of DMT1 (x2.5), and decreased mRNA levels of erythropoietin receptor (x0.2). du 33-35 ceruloplasmin Rattus norvegicus 73-86 17383861-5 2007 Here, we investigated expression of iron exporters including ferroportin 1 (Fpn1), ceruloplasmin (CP) and hephaestin (Heph) and provided evidence for their existence in the heart. Iron 36-40 ceruloplasmin Rattus norvegicus 83-96 17383861-5 2007 Here, we investigated expression of iron exporters including ferroportin 1 (Fpn1), ceruloplasmin (CP) and hephaestin (Heph) and provided evidence for their existence in the heart. Iron 36-40 ceruloplasmin Rattus norvegicus 98-100 17383861-6 2007 We demonstrated that iron has a significant effect on expression of Fpn1 and CP, but not Heph. Iron 21-25 ceruloplasmin Rattus norvegicus 77-79 17383861-7 2007 Treatment of a high-iron diet induced a significant increase in Fpn1, a decrease in CP but no change in Heph mRNA and protein. Iron 20-24 ceruloplasmin Rattus norvegicus 84-86 17383861-8 2007 The control of Fpn1 and CP protein expression by iron was parallel to that of their mRNA expression, suggesting a transcriptional regulation of Fpn1 and CP by iron. Iron 49-53 ceruloplasmin Rattus norvegicus 24-26 17383861-8 2007 The control of Fpn1 and CP protein expression by iron was parallel to that of their mRNA expression, suggesting a transcriptional regulation of Fpn1 and CP by iron. Iron 49-53 ceruloplasmin Rattus norvegicus 153-155 17383861-8 2007 The control of Fpn1 and CP protein expression by iron was parallel to that of their mRNA expression, suggesting a transcriptional regulation of Fpn1 and CP by iron. Iron 159-163 ceruloplasmin Rattus norvegicus 24-26 17383861-8 2007 The control of Fpn1 and CP protein expression by iron was parallel to that of their mRNA expression, suggesting a transcriptional regulation of Fpn1 and CP by iron. Iron 159-163 ceruloplasmin Rattus norvegicus 153-155 17316903-7 2007 These findings suggest a translational regulation of CP expression by iron in the cells. Iron 70-74 ceruloplasmin Rattus norvegicus 53-55 17316903-8 2007 We also examined the effects of CP on iron transport in the cells. Iron 38-42 ceruloplasmin Rattus norvegicus 32-34 17316903-10 2007 However, low concentrations of soluble CP (2-8 microg/ml) increased iron uptake by iron-deficient C6 glioma cells, while the same concentrations of CP had no effect on iron uptake by normal iron cells and iron release from normal iron and iron-sufficient cells. Iron 68-72 ceruloplasmin Rattus norvegicus 39-41 17316903-10 2007 However, low concentrations of soluble CP (2-8 microg/ml) increased iron uptake by iron-deficient C6 glioma cells, while the same concentrations of CP had no effect on iron uptake by normal iron cells and iron release from normal iron and iron-sufficient cells. Iron 83-87 ceruloplasmin Rattus norvegicus 39-41 17316903-0 2007 Ceruloplasmin expression and its role in iron transport in C6 cells. Iron 41-45 ceruloplasmin Rattus norvegicus 0-13 17316903-10 2007 However, low concentrations of soluble CP (2-8 microg/ml) increased iron uptake by iron-deficient C6 glioma cells, while the same concentrations of CP had no effect on iron uptake by normal iron cells and iron release from normal iron and iron-sufficient cells. Iron 83-87 ceruloplasmin Rattus norvegicus 39-41 17316903-1 2007 Ceruloplasmin (CP) is essential for brain iron homeostasis. Iron 42-46 ceruloplasmin Rattus norvegicus 0-13 17316903-10 2007 However, low concentrations of soluble CP (2-8 microg/ml) increased iron uptake by iron-deficient C6 glioma cells, while the same concentrations of CP had no effect on iron uptake by normal iron cells and iron release from normal iron and iron-sufficient cells. Iron 83-87 ceruloplasmin Rattus norvegicus 39-41 17316903-1 2007 Ceruloplasmin (CP) is essential for brain iron homeostasis. Iron 42-46 ceruloplasmin Rattus norvegicus 15-17 17316903-2 2007 However, little is known about the effect of iron on CP expression in the brain. Iron 45-49 ceruloplasmin Rattus norvegicus 53-55 17316903-3 2007 Also, the role of CP in brain iron transport has not been well determined. Iron 30-34 ceruloplasmin Rattus norvegicus 18-20 17316903-6 2007 However, western blotting analysis demonstrated that cell iron overload induced a significant decrease in CP protein content in the cells and that treatment with iron chelators led to a significant increase in CP protein level in the cells. Iron 58-62 ceruloplasmin Rattus norvegicus 106-108 17316903-6 2007 However, western blotting analysis demonstrated that cell iron overload induced a significant decrease in CP protein content in the cells and that treatment with iron chelators led to a significant increase in CP protein level in the cells. Iron 162-166 ceruloplasmin Rattus norvegicus 210-212 17316903-10 2007 However, low concentrations of soluble CP (2-8 microg/ml) increased iron uptake by iron-deficient C6 glioma cells, while the same concentrations of CP had no effect on iron uptake by normal iron cells and iron release from normal iron and iron-sufficient cells. Iron 83-87 ceruloplasmin Rattus norvegicus 39-41 17316903-10 2007 However, low concentrations of soluble CP (2-8 microg/ml) increased iron uptake by iron-deficient C6 glioma cells, while the same concentrations of CP had no effect on iron uptake by normal iron cells and iron release from normal iron and iron-sufficient cells. Iron 83-87 ceruloplasmin Rattus norvegicus 39-41 17317455-5 2007 Epithalamin can be more beneficial than melatonin because the former not only produces direct antioxidant effects, but also is able to stimulate the expression of SOD, ceruloplasmin and other antioxidant enzymes. epithalamin 0-11 ceruloplasmin Rattus norvegicus 168-181 17317455-5 2007 Epithalamin can be more beneficial than melatonin because the former not only produces direct antioxidant effects, but also is able to stimulate the expression of SOD, ceruloplasmin and other antioxidant enzymes. Melatonin 40-49 ceruloplasmin Rattus norvegicus 168-181 16597684-4 2006 Ceruloplasmin (Cp) is a copper-containing ferroxidase that functions as an antioxidant in part by oxidizing toxic ferrous iron to nontoxic ferric iron. Copper 24-30 ceruloplasmin Rattus norvegicus 0-13 17526207-1 2007 Sapropel was tested for its effect on the permeability of erythrocytic membranes and on the erythrocytic and serum levels of ceruloplasmin, malonic dialdehyde, and dienic conjugates in rats after acute poisoning by carbofos, a malathion insecticide. sapropel 0-8 ceruloplasmin Rattus norvegicus 125-138 17697957-1 2007 This research focuses on the role of milk ceruloplasmin (Cp), the main extracellular copper-containing protein of vertebrates, as a source of copper for newborns. Copper 85-91 ceruloplasmin Rattus norvegicus 42-55 17697957-1 2007 This research focuses on the role of milk ceruloplasmin (Cp), the main extracellular copper-containing protein of vertebrates, as a source of copper for newborns. Copper 142-148 ceruloplasmin Rattus norvegicus 42-55 16597684-4 2006 Ceruloplasmin (Cp) is a copper-containing ferroxidase that functions as an antioxidant in part by oxidizing toxic ferrous iron to nontoxic ferric iron. Iron 122-126 ceruloplasmin Rattus norvegicus 0-13 16597684-4 2006 Ceruloplasmin (Cp) is a copper-containing ferroxidase that functions as an antioxidant in part by oxidizing toxic ferrous iron to nontoxic ferric iron. ferric sulfate 139-150 ceruloplasmin Rattus norvegicus 0-13 16671455-12 2006 Our results demonstrate that thrombin increases brain ceruloplasmin levels and exogenous ceruloplasmin reduces ferrous iron-induced brain edema, suggesting that ceruloplasmin up-regulation may contribute to thrombin-induced brain tolerance to ICH by limiting the injury caused by ferrous iron released from the hematoma. Iron 119-123 ceruloplasmin Rattus norvegicus 89-102 16448835-0 2006 Plasma peptidylglycine alpha-amidating monooxygenase (PAM) and ceruloplasmin are affected by age and copper status in rats and mice. Copper 101-107 ceruloplasmin Rattus norvegicus 63-76 16671455-2 2006 Ceruloplasmin is involved in iron metabolism by oxidizing ferrous iron to ferric iron. Iron 29-33 ceruloplasmin Rattus norvegicus 0-13 16671455-12 2006 Our results demonstrate that thrombin increases brain ceruloplasmin levels and exogenous ceruloplasmin reduces ferrous iron-induced brain edema, suggesting that ceruloplasmin up-regulation may contribute to thrombin-induced brain tolerance to ICH by limiting the injury caused by ferrous iron released from the hematoma. Iron 119-123 ceruloplasmin Rattus norvegicus 89-102 16671455-2 2006 Ceruloplasmin is involved in iron metabolism by oxidizing ferrous iron to ferric iron. Iron 58-70 ceruloplasmin Rattus norvegicus 0-13 16671455-2 2006 Ceruloplasmin is involved in iron metabolism by oxidizing ferrous iron to ferric iron. ferric sulfate 74-85 ceruloplasmin Rattus norvegicus 0-13 15978035-0 2005 Characterization of electrogenic bromosulfophthalein transport in carnation petal microsomes and its inhibition by antibodies against bilitranslocase. Sulfobromophthalein 33-52 ceruloplasmin Rattus norvegicus 134-149 16671455-3 2006 The present study examines whether thrombin modulates brain ceruloplasmin levels and whether exogenous ceruloplasmin reduces brain edema induced by ferrous iron in vivo. Iron 156-160 ceruloplasmin Rattus norvegicus 103-116 16671455-8 2006 Brain ceruloplasmin levels were higher after thrombin infusion than after saline injection. Sodium Chloride 74-80 ceruloplasmin Rattus norvegicus 6-19 16671455-11 2006 Co-injection of ferrous iron with ceruloplasmin reduced ferrous iron-induced brain edema (p < 0.05). Iron 16-28 ceruloplasmin Rattus norvegicus 34-47 16671455-11 2006 Co-injection of ferrous iron with ceruloplasmin reduced ferrous iron-induced brain edema (p < 0.05). Iron 56-68 ceruloplasmin Rattus norvegicus 34-47 16671455-12 2006 Our results demonstrate that thrombin increases brain ceruloplasmin levels and exogenous ceruloplasmin reduces ferrous iron-induced brain edema, suggesting that ceruloplasmin up-regulation may contribute to thrombin-induced brain tolerance to ICH by limiting the injury caused by ferrous iron released from the hematoma. Iron 111-123 ceruloplasmin Rattus norvegicus 89-102 16671455-12 2006 Our results demonstrate that thrombin increases brain ceruloplasmin levels and exogenous ceruloplasmin reduces ferrous iron-induced brain edema, suggesting that ceruloplasmin up-regulation may contribute to thrombin-induced brain tolerance to ICH by limiting the injury caused by ferrous iron released from the hematoma. Iron 111-123 ceruloplasmin Rattus norvegicus 89-102 17338279-3 2006 A single dose of streptozotocin (65 mg kg(-1) bwt) resulted in decreased insulin, hyperglycemia, increased lipid peroxidation (thiobarbituric reactive substances, lipid hydroperoxides), and decreased antioxidant levels (vitamin C, vitamin E, reduced glutathione and ceruloplasmin). Streptozocin 17-31 ceruloplasmin Rattus norvegicus 266-279 16088091-6 2005 There was a positive correlation between Cu supplementation and ceruloplasmin levels. Copper Sulfate 41-43 ceruloplasmin Rattus norvegicus 64-77 15744747-0 2005 Effects of development and iron status on ceruloplasmin expression in rat brain. Iron 27-31 ceruloplasmin Rattus norvegicus 42-55 15744747-1 2005 The increased iron content in the brain of subjects with aceruloplasminemia has implicated ceruloplasmin (CP) as a major factor in the regulation of regional brain iron content. Iron 14-18 ceruloplasmin Rattus norvegicus 58-71 15744747-1 2005 The increased iron content in the brain of subjects with aceruloplasminemia has implicated ceruloplasmin (CP) as a major factor in the regulation of regional brain iron content. Iron 164-168 ceruloplasmin Rattus norvegicus 106-108 15744747-2 2005 In this study, we investigated the effects of age and iron on CP expression in rat brain. Iron 54-58 ceruloplasmin Rattus norvegicus 62-64 15744747-9 2005 These findings suggested that the effects of iron on CP expression in the brain may be region-specific, and that regulation of CP expression by iron in the substantia nigra was at the post-transcriptional level. Iron 144-148 ceruloplasmin Rattus norvegicus 127-129 15978035-1 2005 Bilitranslocase is a rat liver plasma membrane carrier, displaying a high-affinity binding site for bilirubin. Bilirubin 100-109 ceruloplasmin Rattus norvegicus 0-15 15978035-4 2005 The aim of this work was to determine whether a homologue of rat liver bilitranslocase is expressed in carnation petals, where it might play a role in the membrane transport of anthocyanins. Anthocyanins 177-189 ceruloplasmin Rattus norvegicus 71-86 15978035-5 2005 The bromosulfophthalein-based assay of rat liver bilitranslocase transport activity was implemented in subcellular membrane fractions, leading to the identification of a bromosulfophthalein carrier (K(M) = 5.3 microm), which is competitively inhibited by cyanidine 3-glucoside (Ki = 51.6 microm) and mainly noncompetitively by cyanidin (Ki = 88.3 microm). Sulfobromophthalein 4-23 ceruloplasmin Rattus norvegicus 49-64 15978035-5 2005 The bromosulfophthalein-based assay of rat liver bilitranslocase transport activity was implemented in subcellular membrane fractions, leading to the identification of a bromosulfophthalein carrier (K(M) = 5.3 microm), which is competitively inhibited by cyanidine 3-glucoside (Ki = 51.6 microm) and mainly noncompetitively by cyanidin (Ki = 88.3 microm). Sulfobromophthalein 170-189 ceruloplasmin Rattus norvegicus 49-64 15978035-5 2005 The bromosulfophthalein-based assay of rat liver bilitranslocase transport activity was implemented in subcellular membrane fractions, leading to the identification of a bromosulfophthalein carrier (K(M) = 5.3 microm), which is competitively inhibited by cyanidine 3-glucoside (Ki = 51.6 microm) and mainly noncompetitively by cyanidin (Ki = 88.3 microm). asterin 255-276 ceruloplasmin Rattus norvegicus 49-64 15978035-5 2005 The bromosulfophthalein-based assay of rat liver bilitranslocase transport activity was implemented in subcellular membrane fractions, leading to the identification of a bromosulfophthalein carrier (K(M) = 5.3 microm), which is competitively inhibited by cyanidine 3-glucoside (Ki = 51.6 microm) and mainly noncompetitively by cyanidin (Ki = 88.3 microm). cyanidin 255-263 ceruloplasmin Rattus norvegicus 49-64 15978035-7 2005 In analogy to liver bilitranslocase, one antibody identified a bilirubin-binding site (Kd = 1.7 nm) in the carnation carrier. Bilirubin 63-72 ceruloplasmin Rattus norvegicus 20-35 15334819-1 2004 Biosynthesis of ceruloplasmin, a copper-containing glycoprotein, which plays an important role in copper transfer and bidirectional iron transport in vertebrates, was studied in 7-day old rats characterized by the embryonic type of copper metabolism. Copper 33-39 ceruloplasmin Rattus norvegicus 16-29 15703998-4 2005 These data point to a possible role of bilitranslocase and of its food-borne substrates (anthocyanins and nicotinic acid) in regulating the function and the permeability of the gastric mucosa. Anthocyanins 89-101 ceruloplasmin Rattus norvegicus 39-54 15703998-4 2005 These data point to a possible role of bilitranslocase and of its food-borne substrates (anthocyanins and nicotinic acid) in regulating the function and the permeability of the gastric mucosa. Niacin 106-120 ceruloplasmin Rattus norvegicus 39-54 16119446-0 2005 [Milk ceruloplasmin as a physiological source of nutritional copper in early ontogenesis in mammals]. Copper 61-67 ceruloplasmin Rattus norvegicus 6-19 15334819-1 2004 Biosynthesis of ceruloplasmin, a copper-containing glycoprotein, which plays an important role in copper transfer and bidirectional iron transport in vertebrates, was studied in 7-day old rats characterized by the embryonic type of copper metabolism. Iron 132-136 ceruloplasmin Rattus norvegicus 16-29 15334819-1 2004 Biosynthesis of ceruloplasmin, a copper-containing glycoprotein, which plays an important role in copper transfer and bidirectional iron transport in vertebrates, was studied in 7-day old rats characterized by the embryonic type of copper metabolism. Copper 98-104 ceruloplasmin Rattus norvegicus 16-29 15334819-4 2004 [14C]-Ceruloplasmin is absorbed from the blood flow by cells of the heart, lung, and kidneys and binds to erythrocytes. Carbon-14 1-4 ceruloplasmin Rattus norvegicus 6-19 15334819-7 2004 It was shown by reverse transcription coupled with PCR using selective primers these cells contain molecular forms of ceruloplasmin mRNAs programming the synthesis of both secretory ceruloplasmin and ceruloplasmin connected with the plasma membrane via the glycosyl phosphatidylinositol anchor. Phosphatidylinositols 266-286 ceruloplasmin Rattus norvegicus 118-131 15334819-8 2004 After transition to the adult type of copper metabolism, the blood serum contents of copper and ceruloplasmin sharply increase, while the content of CP in the cerebrospinal fluid, as measured according to the oxidase and antigen activities, and copper concentration, as determined by atom-absorption spectrometry, remain low. Copper 38-44 ceruloplasmin Rattus norvegicus 96-109 12899943-6 2003 In addition, copper reduced the QUIN-induced decreased striatal activity of Cu,Zn-dependent superoxide dismutase, and increased the ferroxidase activity of ceruloplasmin in cerebrospinal fluid from QUIN-treated rats. Copper 13-19 ceruloplasmin Rattus norvegicus 156-169 15282960-3 2004 The activity of ceruloplasmin and levels of glutathione, vitamins E and C were also found to be substantially decreased in serum with a concomitant rise in lipid peroxide levels after isoproterenol exposure to rats. Lipid Peroxides 156-170 ceruloplasmin Rattus norvegicus 16-29 15282960-3 2004 The activity of ceruloplasmin and levels of glutathione, vitamins E and C were also found to be substantially decreased in serum with a concomitant rise in lipid peroxide levels after isoproterenol exposure to rats. Isoproterenol 184-197 ceruloplasmin Rattus norvegicus 16-29 12760904-1 2003 Release of iron from enterocytes and hepatocytes is thought to require the copper-dependent ferroxidase activity of hephaestin (Hp) and ceruloplasmin (Cp), respectively. Iron 11-15 ceruloplasmin Rattus norvegicus 136-149 12760904-1 2003 Release of iron from enterocytes and hepatocytes is thought to require the copper-dependent ferroxidase activity of hephaestin (Hp) and ceruloplasmin (Cp), respectively. Copper 75-81 ceruloplasmin Rattus norvegicus 136-149 15172111-0 2004 Interleukin-1beta up-regulates iron efflux in rat C6 glioma cells through modulation of ceruloplasmin and ferroportin-1 synthesis. Iron 31-35 ceruloplasmin Rattus norvegicus 88-101 15172111-3 2004 The iron exporter ferroportin-1 (FP) and the multicopper oxidase ceruloplasmin (CP) are essential for iron efflux from cells. Iron 4-8 ceruloplasmin Rattus norvegicus 80-82 15172111-3 2004 The iron exporter ferroportin-1 (FP) and the multicopper oxidase ceruloplasmin (CP) are essential for iron efflux from cells. Iron 102-106 ceruloplasmin Rattus norvegicus 80-82 15122050-1 2004 BACKGROUND: Plasma ceruloplasmin, a copper containing protein, belongs to a class called acute phase proteins. Copper 36-42 ceruloplasmin Rattus norvegicus 19-32 15122050-12 2004 The plasma ceruloplasmin was estimated immediately after stress during each stage--that is preoperative control, stressed control, after overiectomy and then following treatment with Estradiol Valerate. Estradiol 183-201 ceruloplasmin Rattus norvegicus 11-24 14707133-0 2004 Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells. Glycosylphosphatidylinositols 15-43 ceruloplasmin Rattus norvegicus 51-64 14707133-0 2004 Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells. Copper 72-78 ceruloplasmin Rattus norvegicus 51-64 14707133-0 2004 Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells. Nitric Oxide 84-96 ceruloplasmin Rattus norvegicus 51-64 14707133-0 2004 Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells. Heparitin Sulfate 133-148 ceruloplasmin Rattus norvegicus 51-64 14707133-5 2004 Here, we have investigated processing of glypican-1 in rat C6 glioma cells and the possible participation of the copper-containing glycosylphosphatidylinositol-linked splice variant of ceruloplasmin in nitrosothiol formation. Glycosylphosphatidylinositols 131-159 ceruloplasmin Rattus norvegicus 185-198 14707133-5 2004 Here, we have investigated processing of glypican-1 in rat C6 glioma cells and the possible participation of the copper-containing glycosylphosphatidylinositol-linked splice variant of ceruloplasmin in nitrosothiol formation. S-Nitrosothiols 202-214 ceruloplasmin Rattus norvegicus 185-198 14707133-8 2004 RNA interference silencing of ceruloplasmin expression reduced the extent of Zn(II)-supported degradation. Zinc 77-83 ceruloplasmin Rattus norvegicus 30-43 14707133-10 2004 However, in the presence of Cu(II)-loaded ceruloplasmin, heparan sulfate in Zn(II)-loaded glypican-1 underwent extensive, ascorbate-induced degradation. cu(ii) 28-34 ceruloplasmin Rattus norvegicus 42-55 14707133-10 2004 However, in the presence of Cu(II)-loaded ceruloplasmin, heparan sulfate in Zn(II)-loaded glypican-1 underwent extensive, ascorbate-induced degradation. Heparitin Sulfate 57-72 ceruloplasmin Rattus norvegicus 42-55 14707133-10 2004 However, in the presence of Cu(II)-loaded ceruloplasmin, heparan sulfate in Zn(II)-loaded glypican-1 underwent extensive, ascorbate-induced degradation. Zinc 76-82 ceruloplasmin Rattus norvegicus 42-55 14707133-11 2004 We propose that the Cu(II)-to-Cu(I)-reduction that is required for S-nitrosylation of glypican-1 can take place on ceruloplasmin and thereby ensure extensive glypican-1 processing in the presence of free Zn(II) ions. Zinc 204-206 ceruloplasmin Rattus norvegicus 115-128 12899943-6 2003 In addition, copper reduced the QUIN-induced decreased striatal activity of Cu,Zn-dependent superoxide dismutase, and increased the ferroxidase activity of ceruloplasmin in cerebrospinal fluid from QUIN-treated rats. Quinolinic Acid 32-36 ceruloplasmin Rattus norvegicus 156-169 12899943-6 2003 In addition, copper reduced the QUIN-induced decreased striatal activity of Cu,Zn-dependent superoxide dismutase, and increased the ferroxidase activity of ceruloplasmin in cerebrospinal fluid from QUIN-treated rats. Quinolinic Acid 198-202 ceruloplasmin Rattus norvegicus 156-169 12860309-4 2003 Oral administration of the water extract (125 and 250mgkg(-1)) twice a day for 4 weeks resulted in significant reductions in blood glucose, plasma thiobarbituric acid reactive substances, hydroperoxides, ceruloplasmin and alpha-tocopherol and a significant elevation in plasma reduced glutathione and Vitamin C in diabetic rats. Water 27-32 ceruloplasmin Rattus norvegicus 204-217 11693190-7 2001 Arjunolic acid treatment is also shown to prevent the decrease in the levels of superoxide dismutase, catalase, glutathione peroxidase, ceruloplasmin, alpha-tocopherol, reduced glutathione (GSH), ascorbic acid, lipid peroxide, MPO and the cardioprotection is confirmed by the histopathological studies. arjunolic acid 0-14 ceruloplasmin Rattus norvegicus 136-149 12724641-8 2003 Expression of the secreted and expression of the membrane-anchored glycosyl phosphatidyl inositol (GPI) linked forms of ceruloplasmin were assesed in rat retina using primers specific for each form. Glycosylphosphatidylinositols 67-97 ceruloplasmin Rattus norvegicus 120-133 12724641-8 2003 Expression of the secreted and expression of the membrane-anchored glycosyl phosphatidyl inositol (GPI) linked forms of ceruloplasmin were assesed in rat retina using primers specific for each form. Glycosylphosphatidylinositols 99-102 ceruloplasmin Rattus norvegicus 120-133 12099680-0 2002 Ceruloplasmin carries the anionic glycan oligo/poly alpha2,8 deaminoneuraminic acid. Polysaccharides 34-40 ceruloplasmin Rattus norvegicus 0-13 12099680-0 2002 Ceruloplasmin carries the anionic glycan oligo/poly alpha2,8 deaminoneuraminic acid. oligo/ 41-47 ceruloplasmin Rattus norvegicus 0-13 12099680-0 2002 Ceruloplasmin carries the anionic glycan oligo/poly alpha2,8 deaminoneuraminic acid. poly(2,8-deaminoneuraminic acid) 47-83 ceruloplasmin Rattus norvegicus 0-13 12099680-4 2002 The immunoreactivity for oligo/poly alpha2,8 KDN on purified serum ceruloplasmin was abolished by N-glycosidase F treatment but not by beta-elimination, indicating that it is present on N-glycosidically linked oligosaccharides. n-glycosidically linked oligosaccharides 186-226 ceruloplasmin Rattus norvegicus 67-80 12099680-5 2002 However, the copper binding activity of ceruloplasmin was independent of the presence of the anionic glycan. Copper 13-19 ceruloplasmin Rattus norvegicus 40-53 12099680-5 2002 However, the copper binding activity of ceruloplasmin was independent of the presence of the anionic glycan. Polysaccharides 101-107 ceruloplasmin Rattus norvegicus 40-53 14534613-1 2003 Experiments on rats showed that pulse therapy with prednisolone (100 mg/kg intraperitoneally for 3 days) stimulated urinary excretion of hydroxyproline, increased the content of inorganic phosphorus, promoted the increase in the content of dienic conjugates and catalase activity, and decreased serum levels of MDA and ceruloplasmin. Prednisolone 51-63 ceruloplasmin Rattus norvegicus 319-332 12555201-1 2003 Ceruloplasmin is a key enzyme involved in detoxifying ferrous iron, which can generate free radicals. Iron 54-66 ceruloplasmin Rattus norvegicus 0-13 12555201-1 2003 Ceruloplasmin is a key enzyme involved in detoxifying ferrous iron, which can generate free radicals. Free Radicals 87-100 ceruloplasmin Rattus norvegicus 0-13 12555201-3 2003 We have previously identified a membrane-bound glycosylphosphatidylinositol (GPI)-anchored form of ceruloplasmin (GPI-Cp) that is expressed by astrocytes in the central nervous system (CNS) (Patel and David. Glycosylphosphatidylinositols 47-75 ceruloplasmin Rattus norvegicus 99-112 12555201-3 2003 We have previously identified a membrane-bound glycosylphosphatidylinositol (GPI)-anchored form of ceruloplasmin (GPI-Cp) that is expressed by astrocytes in the central nervous system (CNS) (Patel and David. Glycosylphosphatidylinositols 77-80 ceruloplasmin Rattus norvegicus 99-112 12683081-3 2003 The treatment with glucocorticosteroid enhanced the excretion of hydroxyproline and inorganic phosphates with urine, increased the LPO rate and antioxidant activity of the blood serum, and decreases the level of ceruloplasmin and the catalase activity in the blood. glucocorticosteroid 19-38 ceruloplasmin Rattus norvegicus 212-225 12204581-0 2002 The effect of Au injection on the ceruloplasmin, metallothionein and 8-hydroxydeoxyguanosine of rat serum, kidney and liver. Gold 14-16 ceruloplasmin Rattus norvegicus 34-47 11880554-3 2002 We therefore examined in rats how nutritional iron status would affect expression of ceruloplasmin. Iron 46-50 ceruloplasmin Rattus norvegicus 85-98 11673641-5 2001 Rats fed low dietary copper had significantly lower (p<0.0001) hematocrits, hemoglobin, ceruloplasmin activity and plasma and liver copper concentrations than rats fed adequate dietary copper. Copper 21-27 ceruloplasmin Rattus norvegicus 91-104 11446991-8 2001 Ceruloplasmin activity of the rats fed the marginal Cu and fructose-containing diets declined to undetectable levels and plasma cholesterol levels increased. Fructose 59-67 ceruloplasmin Rattus norvegicus 0-13 11846014-13 2001 We conclude that silver resembles copper in aspects of its tissue distribution, response to lactation, and incorporation into ceruloplasmin. Silver 17-23 ceruloplasmin Rattus norvegicus 126-139 11846014-13 2001 We conclude that silver resembles copper in aspects of its tissue distribution, response to lactation, and incorporation into ceruloplasmin. Copper 34-40 ceruloplasmin Rattus norvegicus 126-139 12557918-2 2000 In myocardial necrosis induced by isoproterenol, a significant increase in serum iron content with a significant decrease in plasma iron binding capacity, ceruloplasmin activity and glutathione level were observed. Isoproterenol 34-47 ceruloplasmin Rattus norvegicus 155-168 11082702-1 2000 Copper (Cu) is an essential trace element and constitutes the active center of the redox Cu enzymes such as Cu, Zn-superoxide dismutase (Cu, Zn-SOD), ceruloplasmin and cytochrome c oxidase. Copper 0-6 ceruloplasmin Rattus norvegicus 150-163 11082702-1 2000 Copper (Cu) is an essential trace element and constitutes the active center of the redox Cu enzymes such as Cu, Zn-superoxide dismutase (Cu, Zn-SOD), ceruloplasmin and cytochrome c oxidase. Copper 8-10 ceruloplasmin Rattus norvegicus 150-163 11019827-1 2000 We have previously reported several studies on the loading of iron into ferritin by ceruloplasmin using proteins from rats. Iron 62-66 ceruloplasmin Rattus norvegicus 84-97 10613762-6 2000 Liver and heart superoxide dismutase and cytochrome c oxidase activities, and plasma ceruloplasmin and erythrocyte superoxide dismutase activities were significantly lower in the copper-deficient rats than in the other two groups. Copper 179-185 ceruloplasmin Rattus norvegicus 85-98 10959791-15 2000 Ag may compete with Cu in the uptake into CP (conversion of apo-CP to holo-CP). Copper 20-22 ceruloplasmin Rattus norvegicus 42-44 10943080-7 2000 The level of vitamin C and ceruloplasmin in plasma were decreased in young, middle-aged and old groups in response to SO2. Sulfur Dioxide 118-121 ceruloplasmin Rattus norvegicus 27-40 10491642-0 1999 Glycosyl phosphatidylinositol-anchored ceruloplasmin is expressed by rat Sertoli cells and is concentrated in detergent-insoluble membrane fractions. Glycosylphosphatidylinositols 0-29 ceruloplasmin Rattus norvegicus 39-52 10491642-2 1999 Studies on serum ceruloplasmin have demonstrated it to be a ferroxidase that is essential for iron transport throughout the body. Iron 94-98 ceruloplasmin Rattus norvegicus 17-30 10491642-8 1999 This is the first report of GPI-anchored ceruloplasmin in Sertoli cells and the first study of GPI-anchored ceruloplasmin in DIGs. Glycosylphosphatidylinositols 95-98 ceruloplasmin Rattus norvegicus 108-121 10491642-3 1999 We report here that a glycosyl phosphatidylinositol (GPI)-anchored form of ceruloplasmin is expressed by Sertoli cells. Glycosylphosphatidylinositols 22-51 ceruloplasmin Rattus norvegicus 75-88 10491642-3 1999 We report here that a glycosyl phosphatidylinositol (GPI)-anchored form of ceruloplasmin is expressed by Sertoli cells. Glycosylphosphatidylinositols 53-56 ceruloplasmin Rattus norvegicus 75-88 10491642-8 1999 This is the first report of GPI-anchored ceruloplasmin in Sertoli cells and the first study of GPI-anchored ceruloplasmin in DIGs. digs 125-129 ceruloplasmin Rattus norvegicus 108-121 10491642-6 1999 The presence of the GPI anchor on ceruloplasmin was confirmed by Triton X-114 phase partitioning experiments and by recognition with an antibody to the GPI anchor. Glycosylphosphatidylinositols 20-23 ceruloplasmin Rattus norvegicus 34-47 10491642-9 1999 We suggest that GPI-anchored ceruloplasmin may be the dominant form expressed by Sertoli cells and that Sertoli cell DIGs may play a role in iron metabolism within the seminiferous tubule. Glycosylphosphatidylinositols 16-19 ceruloplasmin Rattus norvegicus 29-42 10491642-6 1999 The presence of the GPI anchor on ceruloplasmin was confirmed by Triton X-114 phase partitioning experiments and by recognition with an antibody to the GPI anchor. Nonidet P-40 65-77 ceruloplasmin Rattus norvegicus 34-47 10491642-6 1999 The presence of the GPI anchor on ceruloplasmin was confirmed by Triton X-114 phase partitioning experiments and by recognition with an antibody to the GPI anchor. Glycosylphosphatidylinositols 152-155 ceruloplasmin Rattus norvegicus 34-47 10491642-7 1999 GPI-anchored ceruloplasmin was enriched in detergent-insoluble glycolipid-enriched membrane microdomains (DIGs) of Sertoli cells. Glycolipids 63-73 ceruloplasmin Rattus norvegicus 13-26 10405174-0 1999 Specific sequence-directed anti-bilitranslocase antibodies as a tool to detect potentially bilirubin-binding proteins in different tissues of the rat. Bilirubin 91-100 ceruloplasmin Rattus norvegicus 32-47 10498756-5 1999 Compared with copper-adequate rats, copper-deficient rats had lower hematocrits, liver copper concentrations and plasma ceruloplasmin activities, and higher heart weights and liver iron concentrations. Copper 36-42 ceruloplasmin Rattus norvegicus 120-133 10498756-5 1999 Compared with copper-adequate rats, copper-deficient rats had lower hematocrits, liver copper concentrations and plasma ceruloplasmin activities, and higher heart weights and liver iron concentrations. Copper 36-42 ceruloplasmin Rattus norvegicus 120-133 10474204-6 1999 Cu in Cu-containing enzymes such as Cu,Zn-superoxide dismutase (SOD) in liver and ceruloplasmin (Cp) in plasma was decreased by excessive thiomolybdates, the Cu being found in the plasma in the form of a Cu/thiomolybdate/albumin complex. tetrathiomolybdate 138-152 ceruloplasmin Rattus norvegicus 82-95 10474204-6 1999 Cu in Cu-containing enzymes such as Cu,Zn-superoxide dismutase (SOD) in liver and ceruloplasmin (Cp) in plasma was decreased by excessive thiomolybdates, the Cu being found in the plasma in the form of a Cu/thiomolybdate/albumin complex. tetrathiomolybdate 138-151 ceruloplasmin Rattus norvegicus 82-95 9882459-0 1999 Mutational analysis of loading of iron into rat liver ferritin by ceruloplasmin. Iron 34-38 ceruloplasmin Rattus norvegicus 66-79 9882459-1 1999 Site-directed mutagenesis was used to investigate the loading of iron into rat liver ferritin by ceruloplasmin. Iron 65-69 ceruloplasmin Rattus norvegicus 97-110 9882459-3 1999 Mutation Y34F affected the rate of iron loading by ceruloplasmin and incorporation of the oxidized iron into the core. Iron 35-39 ceruloplasmin Rattus norvegicus 51-64 9882459-6 1999 Additional changes in the L chain involving the BC loop suggest that the entire BC loop is involved in the association of ferritin with ceruloplasmin, increasing its ferroxidase activity and the rate of iron loading into ferritin. Iron 203-207 ceruloplasmin Rattus norvegicus 136-149 9578464-0 1998 Bilitranslocase can exist in two metastable forms with different affinities for the substrates--evidence from cysteine and arginine modification. Arginine 123-131 ceruloplasmin Rattus norvegicus 0-15 9587137-13 1998 Copper in milk ceruloplasmin appears to be particularly available for absorption, at least in rats. Copper 0-6 ceruloplasmin Rattus norvegicus 15-28 9521817-1 1998 We previously reported that the heavy chain of ferritin was required for loading it with iron using ceruloplasmin as a ferroxidase [J.-H. Guo, M. Abedi, and S. D. Aust (1996) Arch. Iron 89-93 ceruloplasmin Rattus norvegicus 100-113 9521817-8 1998 The rH-Ft mutant homopolymer could not be loaded, whereas the rL-Ft mutant homopolymer could be loaded with iron by ceruloplasmin. Iron 108-112 ceruloplasmin Rattus norvegicus 116-129 9521817-9 1998 However, we found that the initial rate of iron loading into the rL-Ft mutant homopolymer by ceruloplasmin was less than that into the rH-Ft homopolymer. Iron 43-47 ceruloplasmin Rattus norvegicus 93-106 9521817-10 1998 When 500 atoms of iron per ferritin were used for loading, 98% was loaded into the rH-Ft homopolymer by ceruloplasmin in 15 min, but only 30% was loaded into the rL-Ft mutant homopolymer in the same time. Iron 18-22 ceruloplasmin Rattus norvegicus 104-117 9521817-12 1998 These observations suggested that the four alpha-helix bundle channel of ferritin is required for iron loading, but an additional factor, i.e. , a site which stimulate the ferroxidase activity of ceruloplasmin, is also essential. Iron 98-102 ceruloplasmin Rattus norvegicus 196-209 10461685-2 1999 However, it increases toward and at the onset of acute hepatitis in LEC rats, the increased Cu in the plasma being bound to ceruloplasmin, metallothionein and albumin. Copper 92-94 ceruloplasmin Rattus norvegicus 124-137 10205787-0 1999 [A comparative study of the transport dynamics of the peptide moiety of the milk ceruloplasmin molecule in the body of rats with embryonic and adult types of copper metabolism]. Copper 158-164 ceruloplasmin Rattus norvegicus 81-94 10205787-4 1999 The dynamic aspects of the distribution of labeled milk ceruloplasmin in the body of six-day old rats over a period of 4 h point out that, under the conditions of embryonic copper metabolism, it can serve as a transporter of copper ions to extrahepatic organs. Copper 173-179 ceruloplasmin Rattus norvegicus 56-69 10205787-5 1999 We discuss the role of milk ceruloplasmin in copper metabolism in mammals during the neonatal period. Copper 45-51 ceruloplasmin Rattus norvegicus 28-41 9788274-0 1998 Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin. Glycosylphosphatidylinositols 36-39 ceruloplasmin Rattus norvegicus 57-70 9788274-9 1998 Protein sequencing of the Ran-2 antigen immunopurified from rat brain membranes showed complete identity over two extended segments with the copper binding protein ceruloplasmin. Copper 141-147 ceruloplasmin Rattus norvegicus 164-177 9788274-10 1998 These findings indicate that astrocytes and Schwann cells express a novel GPI-anchored form of ceruloplasmin and suggest that this GPI form plays a role in axonal-glial interactions. Glycosylphosphatidylinositols 74-77 ceruloplasmin Rattus norvegicus 95-108 9801065-10 1998 Iron supplementation has resulted in decreased mobilization of stored iron as reflected by increased mucosal ferritin level and decreased serum ceruloplasmin ferroxidase activity contributing to greater peroxidative stress in the intestine. Iron 0-4 ceruloplasmin Rattus norvegicus 144-169 9647667-1 1998 We showed previously that ceruloplasmin associates with the H chain of rat liver ferritin during iron loading into ferritin such that the iron oxidized by ceruloplasmin was deposited into ferritin [S.-H. Juan et al. Iron 97-101 ceruloplasmin Rattus norvegicus 26-39 9647667-1 1998 We showed previously that ceruloplasmin associates with the H chain of rat liver ferritin during iron loading into ferritin such that the iron oxidized by ceruloplasmin was deposited into ferritin [S.-H. Juan et al. Iron 138-142 ceruloplasmin Rattus norvegicus 26-39 9647667-1 1998 We showed previously that ceruloplasmin associates with the H chain of rat liver ferritin during iron loading into ferritin such that the iron oxidized by ceruloplasmin was deposited into ferritin [S.-H. Juan et al. Iron 138-142 ceruloplasmin Rattus norvegicus 155-168 9647667-6 1998 Three synthetic decapeptides derived from domains 2, 4, and 6 of ceruloplasmin, referred to CP-2, CP-4, and CP-6, were utilized to identify a possible binding site on ceruloplasmin for ferritin. cp-6 108-112 ceruloplasmin Rattus norvegicus 65-78 9647667-6 1998 Three synthetic decapeptides derived from domains 2, 4, and 6 of ceruloplasmin, referred to CP-2, CP-4, and CP-6, were utilized to identify a possible binding site on ceruloplasmin for ferritin. cp-6 108-112 ceruloplasmin Rattus norvegicus 167-180 9647667-7 1998 Two of the peptides, CP-4 and CP-6, were found to inhibit iron loading into the recombinant ferritin H chain homopolymer (rH-Ft) by ceruloplasmin. Iron 58-62 ceruloplasmin Rattus norvegicus 132-145 9647667-8 1998 The extent of inhibition of iron loading into ferritin by ceruloplasmin by CP-6, but not CP-4, varied with pH, whereas the inhibitory effect remained constant in increasing concentrations of NaCl. Iron 28-32 ceruloplasmin Rattus norvegicus 58-71 9647667-8 1998 The extent of inhibition of iron loading into ferritin by ceruloplasmin by CP-6, but not CP-4, varied with pH, whereas the inhibitory effect remained constant in increasing concentrations of NaCl. cp-6 75-79 ceruloplasmin Rattus norvegicus 58-71 9647667-14 1998 Only the BC loop of ferritin H chain decreased the amount of iron loading into ferritin by ceruloplasmin. Iron 61-65 ceruloplasmin Rattus norvegicus 91-104 9578464-0 1998 Bilitranslocase can exist in two metastable forms with different affinities for the substrates--evidence from cysteine and arginine modification. Cysteine 110-118 ceruloplasmin Rattus norvegicus 0-15 9578464-1 1998 Bilitranslocase is an organic anion carrier involved in bilirubin and phthalein uptake by the liver. Bilirubin 56-65 ceruloplasmin Rattus norvegicus 0-15 9578464-1 1998 Bilitranslocase is an organic anion carrier involved in bilirubin and phthalein uptake by the liver. phthalein 70-79 ceruloplasmin Rattus norvegicus 0-15 9578464-7 1998 It is concluded that bilitranslocase occurs in two possible states, featured by high and low affinity for the substrates (for sulfobromophthalein, Km = 5 microM and 37 microM, respectively). Sulfobromophthalein 126-145 ceruloplasmin Rattus norvegicus 21-36 9305790-0 1997 The effect of silver administration on the biosynthesis and the molecular properties of rat ceruloplasmin. Silver 14-20 ceruloplasmin Rattus norvegicus 92-105 9430557-10 1998 The possible role of ceruloplasmin in inhibiting reaction oxygen species in the retina after injury is discussed. oxygen species 58-72 ceruloplasmin Rattus norvegicus 21-34 9795975-4 1998 Low copper intake produced low activities of two serum copper enzymes: ceruloplasmin and extracellular SOD. Copper 4-10 ceruloplasmin Rattus norvegicus 71-84 9795975-4 1998 Low copper intake produced low activities of two serum copper enzymes: ceruloplasmin and extracellular SOD. Copper 55-61 ceruloplasmin Rattus norvegicus 71-84 9485527-1 1997 The possible relation of the increase in the concentration of copper (Cu) in the bloodstream with the increased supply of Cu to ceruloplasmin in the liver was examined in relation to the onset of jaundice in Long-Evans rats with a cinnamon-like coat color (LEC rats), an animal model of Wilson disease. Copper 62-68 ceruloplasmin Rattus norvegicus 128-141 9485527-1 1997 The possible relation of the increase in the concentration of copper (Cu) in the bloodstream with the increased supply of Cu to ceruloplasmin in the liver was examined in relation to the onset of jaundice in Long-Evans rats with a cinnamon-like coat color (LEC rats), an animal model of Wilson disease. Copper 70-72 ceruloplasmin Rattus norvegicus 128-141 9485527-1 1997 The possible relation of the increase in the concentration of copper (Cu) in the bloodstream with the increased supply of Cu to ceruloplasmin in the liver was examined in relation to the onset of jaundice in Long-Evans rats with a cinnamon-like coat color (LEC rats), an animal model of Wilson disease. Copper 122-124 ceruloplasmin Rattus norvegicus 128-141 9305790-1 1997 To examine the cause of the altered ceruloplasmin (Cp) metabolism by silver administration, we analysed the properties of serum Cp by gel filtration chromatography, affinity chromatography and polyacrylamide gel electrophoresis. Silver 69-75 ceruloplasmin Rattus norvegicus 36-49 9030219-1 1997 The serine protease inhibitor phenylmethylsulfonyl fluoride is shown to cause partial inhibition of bilitranslocase transport activity in rat liver plasma membrane vesicles. Phenylmethylsulfonyl Fluoride 30-59 ceruloplasmin Rattus norvegicus 100-115 9169016-0 1997 Loading of iron into recombinant rat liver ferritin heteropolymers by ceruloplasmin. Iron 11-15 ceruloplasmin Rattus norvegicus 70-83 9169016-1 1997 We have reported previously that the heavy chain of ferritin is required for iron incorporation by ceruloplasmin (J.-H. Guo, M. Abedi, and S. D. Aust (1996) Arch. Iron 77-81 ceruloplasmin Rattus norvegicus 99-112 9169016-5 1997 The purpose of this study was to determine how many heavy chains were required for ceruloplasmin to interact with ferritin such that iron loading occurred. Iron 133-137 ceruloplasmin Rattus norvegicus 83-96 9169016-9 1997 The maximal extent of iron loading was observed using 1 mol of rat ceruloplasmin per mole of H chain in the two heteropolymers. Iron 22-26 ceruloplasmin Rattus norvegicus 67-80 9169016-10 1997 The extent of iron incorporation decreased with additional ceruloplasmin. Iron 14-18 ceruloplasmin Rattus norvegicus 59-72 9169016-11 1997 Iron incorporation into rat liver ferritin, found to contain 10 H chains, increased as the molar ratio of ceruloplasmin to ferritin increased to 4:1 and remained the same up to 8:1. Iron 0-4 ceruloplasmin Rattus norvegicus 106-119 9169016-13 1997 Therefore, we propose that the optimal molar ratio of ceruloplasmin to ferritin depends upon the numbers of H chain making up the ferritin molecule for the maximal incorporation of iron into ferritin. Iron 181-185 ceruloplasmin Rattus norvegicus 54-67 9030219-4 1997 From these protection experiments, the Ka for the complex of bilitranslocase with either bilirubin or nicotinic acid has been estimated to be 2.1 and 10.8 nM. Bilirubin 89-98 ceruloplasmin Rattus norvegicus 61-76 9030219-4 1997 From these protection experiments, the Ka for the complex of bilitranslocase with either bilirubin or nicotinic acid has been estimated to be 2.1 and 10.8 nM. Niacin 102-116 ceruloplasmin Rattus norvegicus 61-76 9030219-6 1997 Tentatively, the target for phenylmethylsulfonyl fluoride on bilitranslocase is identified as a recognition site for the physiological substrates. Phenylmethylsulfonyl Fluoride 28-57 ceruloplasmin Rattus norvegicus 61-76 8988625-4 1996 The responses of serum cholesterol, liver nonprotein SH, and serum ceruloplasmin to cystine were greater than of those to cysteine. Cystine 84-91 ceruloplasmin Rattus norvegicus 67-80 9202972-0 1997 Regulation of ceruloplasmin by retinoic acid in the developing rat. Tretinoin 31-44 ceruloplasmin Rattus norvegicus 14-27 9202972-1 1997 Ceruloplasmin (Cp), the major copper-binding protein in the plasma, is an acute phase protein with ferrioxidase activity. Copper 30-36 ceruloplasmin Rattus norvegicus 0-13 9007005-0 1996 Cadmium interaction with essential metals (Zn, Cu, Fe), metabolism metallothionein, and ceruloplasmin in pregnant rats and fetuses. Cadmium 0-7 ceruloplasmin Rattus norvegicus 88-101 8988625-8 1996 This study demonstrates that dietary cystine and cysteine had the same influence on growth, but had a differential influence on such metabolic parameters as liver nonprotein SH, serum ceruloplasmin, serum cholesterol, and tissue ascorbic acid. Cystine 37-44 ceruloplasmin Rattus norvegicus 184-197 8988625-8 1996 This study demonstrates that dietary cystine and cysteine had the same influence on growth, but had a differential influence on such metabolic parameters as liver nonprotein SH, serum ceruloplasmin, serum cholesterol, and tissue ascorbic acid. Cysteine 49-57 ceruloplasmin Rattus norvegicus 184-197 8748229-3 1995 In the animals fed a cholesterol-supplemented diet, the mean values of serum lipid peroxide, ceruloplasmin, serum copper, and unesterified fatty acids were increased significantly (p < 0.01) as compared to the control group. Cholesterol 21-32 ceruloplasmin Rattus norvegicus 93-106 8876933-1 1996 The antioxidant effects of ceruloplasmin (CAS 9031-37-2) against oxygen free radicals (.O2-, .OH, 1O2) and their by-products (H2O2, HOCl), generated by electrolysis of Krebs-Henseleit buffer, were determined in vitro by the DPD (N,N-diethyl-p-phenylenediamine) colorimetric method and ex vivo by quantifying cardiodynamic variables of the isolated perfused rat heart. oxygen free radicals 65-85 ceruloplasmin Rattus norvegicus 27-40 8876933-1 1996 The antioxidant effects of ceruloplasmin (CAS 9031-37-2) against oxygen free radicals (.O2-, .OH, 1O2) and their by-products (H2O2, HOCl), generated by electrolysis of Krebs-Henseleit buffer, were determined in vitro by the DPD (N,N-diethyl-p-phenylenediamine) colorimetric method and ex vivo by quantifying cardiodynamic variables of the isolated perfused rat heart. Oxygen 88-90 ceruloplasmin Rattus norvegicus 27-40 8876933-1 1996 The antioxidant effects of ceruloplasmin (CAS 9031-37-2) against oxygen free radicals (.O2-, .OH, 1O2) and their by-products (H2O2, HOCl), generated by electrolysis of Krebs-Henseleit buffer, were determined in vitro by the DPD (N,N-diethyl-p-phenylenediamine) colorimetric method and ex vivo by quantifying cardiodynamic variables of the isolated perfused rat heart. Hydrogen Peroxide 126-130 ceruloplasmin Rattus norvegicus 27-40 8876933-1 1996 The antioxidant effects of ceruloplasmin (CAS 9031-37-2) against oxygen free radicals (.O2-, .OH, 1O2) and their by-products (H2O2, HOCl), generated by electrolysis of Krebs-Henseleit buffer, were determined in vitro by the DPD (N,N-diethyl-p-phenylenediamine) colorimetric method and ex vivo by quantifying cardiodynamic variables of the isolated perfused rat heart. Hypochlorous Acid 132-136 ceruloplasmin Rattus norvegicus 27-40 8876933-1 1996 The antioxidant effects of ceruloplasmin (CAS 9031-37-2) against oxygen free radicals (.O2-, .OH, 1O2) and their by-products (H2O2, HOCl), generated by electrolysis of Krebs-Henseleit buffer, were determined in vitro by the DPD (N,N-diethyl-p-phenylenediamine) colorimetric method and ex vivo by quantifying cardiodynamic variables of the isolated perfused rat heart. Krebs-Henseleit solution 168-190 ceruloplasmin Rattus norvegicus 27-40 8876933-1 1996 The antioxidant effects of ceruloplasmin (CAS 9031-37-2) against oxygen free radicals (.O2-, .OH, 1O2) and their by-products (H2O2, HOCl), generated by electrolysis of Krebs-Henseleit buffer, were determined in vitro by the DPD (N,N-diethyl-p-phenylenediamine) colorimetric method and ex vivo by quantifying cardiodynamic variables of the isolated perfused rat heart. N,N-diethyl 4-phenylenediamine 224-227 ceruloplasmin Rattus norvegicus 27-40 8876933-1 1996 The antioxidant effects of ceruloplasmin (CAS 9031-37-2) against oxygen free radicals (.O2-, .OH, 1O2) and their by-products (H2O2, HOCl), generated by electrolysis of Krebs-Henseleit buffer, were determined in vitro by the DPD (N,N-diethyl-p-phenylenediamine) colorimetric method and ex vivo by quantifying cardiodynamic variables of the isolated perfused rat heart. N,N-diethyl 4-phenylenediamine 229-259 ceruloplasmin Rattus norvegicus 27-40 8754148-1 1996 Four subcutaneous administrations of 2 g/kg of tetrachloromethane to albino rats inhibited the hepatic activity of superoxide dismutase, catalase, glutathione peroxidase, reduced the concentrations of tocopherol, retinol, ascorbic acid, glutathiones, decreased the plasma level of ceruloplasmin and the total antioxidative activity of liver tissue. Carbon Tetrachloride 47-65 ceruloplasmin Rattus norvegicus 281-294 8748229-6 1995 Correlations between ceruloplasmin and lipid peroxides as well as copper were statistically significant in these animals. Lipid Peroxides 39-54 ceruloplasmin Rattus norvegicus 21-34 7779145-4 1995 Ceruloplasmin exhibited a cardioprotective effect and prevented the oxygen free radical-induced release of noradrenaline, indicating that it can also protect the sympathetic nerve endings from oxygen free-radical injury. oxygen free radical 68-87 ceruloplasmin Rattus norvegicus 0-13 7674840-0 1995 Defective copper binding to apo-ceruloplasmin in a rat model and patients with Wilson"s disease. Copper 10-16 ceruloplasmin Rattus norvegicus 32-45 7726856-1 1995 Copper incorporation into ceruloplasmin during ceruloplasmin synthesis was studied by comparing LEC and control rats. Copper 0-6 ceruloplasmin Rattus norvegicus 26-39 7726856-1 1995 Copper incorporation into ceruloplasmin during ceruloplasmin synthesis was studied by comparing LEC and control rats. Copper 0-6 ceruloplasmin Rattus norvegicus 47-60 7726856-4 1995 Copper was present in ceruloplasmin in the Golgi apparatus and serum of controls, while it was not detected in ceruloplasmin in the Golgi apparatus and serum of the LEC rat. Copper 0-6 ceruloplasmin Rattus norvegicus 22-35 7726856-5 1995 These results indicate that copper is incorporated into ceruloplasmin in the Golgi apparatus of normal hepatocytes. Copper 28-34 ceruloplasmin Rattus norvegicus 56-69 7779145-0 1995 Protection of myocardial tissue against deleterious effects of oxygen free radicals by ceruloplasmin. oxygen free radicals 63-83 ceruloplasmin Rattus norvegicus 87-100 7779145-1 1995 This study describes the carioprotective effect of ceruloplasmin (CAS 9031-37-2) against oxygen free radical injury, as indicated by several biochemical indicators and some cardiodynamic variables. Oxygen 89-95 ceruloplasmin Rattus norvegicus 51-64 7779145-4 1995 Ceruloplasmin exhibited a cardioprotective effect and prevented the oxygen free radical-induced release of noradrenaline, indicating that it can also protect the sympathetic nerve endings from oxygen free-radical injury. Norepinephrine 107-120 ceruloplasmin Rattus norvegicus 0-13 7779145-4 1995 Ceruloplasmin exhibited a cardioprotective effect and prevented the oxygen free radical-induced release of noradrenaline, indicating that it can also protect the sympathetic nerve endings from oxygen free-radical injury. Oxygen 68-74 ceruloplasmin Rattus norvegicus 0-13 7779145-5 1995 Purified ceruloplasmin, a circulating extracellular antioxidant and oxygen free radical scavenger, seems to be an effective heart protective agent against myocardial and neuronal injuries generated by oxygen free radicals. oxygen free radical 68-87 ceruloplasmin Rattus norvegicus 9-22 7779145-5 1995 Purified ceruloplasmin, a circulating extracellular antioxidant and oxygen free radical scavenger, seems to be an effective heart protective agent against myocardial and neuronal injuries generated by oxygen free radicals. oxygen free radicals 201-221 ceruloplasmin Rattus norvegicus 9-22 7734924-0 1995 Embryotoxicity of silver ions is diminished by ceruloplasmin--further evidence for its role in the transport of copper. Silver 18-24 ceruloplasmin Rattus norvegicus 47-60 7734924-0 1995 Embryotoxicity of silver ions is diminished by ceruloplasmin--further evidence for its role in the transport of copper. Copper 112-118 ceruloplasmin Rattus norvegicus 47-60 7734924-2 1995 Feeding of female rats throughout the term on a regular diet supplemented with AgCl did not cause alterations of their physiological functions, despite the fact that enzymatically active copper-containing ceruloplasmin (CP) was eliminated from the blood plasma. silver chloride 79-83 ceruloplasmin Rattus norvegicus 205-218 7734924-2 1995 Feeding of female rats throughout the term on a regular diet supplemented with AgCl did not cause alterations of their physiological functions, despite the fact that enzymatically active copper-containing ceruloplasmin (CP) was eliminated from the blood plasma. silver chloride 79-83 ceruloplasmin Rattus norvegicus 220-222 7734924-2 1995 Feeding of female rats throughout the term on a regular diet supplemented with AgCl did not cause alterations of their physiological functions, despite the fact that enzymatically active copper-containing ceruloplasmin (CP) was eliminated from the blood plasma. Copper 187-193 ceruloplasmin Rattus norvegicus 205-218 7734924-2 1995 Feeding of female rats throughout the term on a regular diet supplemented with AgCl did not cause alterations of their physiological functions, despite the fact that enzymatically active copper-containing ceruloplasmin (CP) was eliminated from the blood plasma. Copper 187-193 ceruloplasmin Rattus norvegicus 220-222 8002499-3 1994 These spectra consisted of at least three distinct species: one with a broad feature having an effective g factor for the unpaired electron (g) of 2.06 assigned to the copper-binding acute phase protein ceruloplasmin, and two with narrower features that evolved at core temperatures > 39 degrees C representing a semiquinone radical and .NO-heme. Copper 168-174 ceruloplasmin Rattus norvegicus 203-216 7734924-6 1995 Embryotoxicity of AgCl was seriously diminished by repetitive injections of native CP to the pregnant rats. silver chloride 18-22 ceruloplasmin Rattus norvegicus 83-85 7734924-9 1995 It is suggested that the embryotoxic effect of AgCl is caused by its ability to interfere with copper metabolism, in particular by altering the copper-transporting function of CP. Copper 144-150 ceruloplasmin Rattus norvegicus 176-178 7746837-0 1995 The comparative abilities of inorganic cobalt and cobalt-protoporphyrin to affect copper metabolism and elevate plasma ceruloplasmin. Cobalt 39-45 ceruloplasmin Rattus norvegicus 119-132 7746837-0 1995 The comparative abilities of inorganic cobalt and cobalt-protoporphyrin to affect copper metabolism and elevate plasma ceruloplasmin. cobaltiprotoporphyrin 50-71 ceruloplasmin Rattus norvegicus 119-132 7746837-2 1995 Following subcutaneous treatment (250 mumol/kg body weight), inorganic cobalt elicited only a moderate (25-30%) and transient (48 h) increase in plasma copper levels and a concomitant elevation (up to 2-fold) in ceruloplasmin (ferroxidase) activity. inorganic cobalt 61-77 ceruloplasmin Rattus norvegicus 212-225 7746837-3 1995 Treatment with cobalt-protoporphyrin (25 mumol/kg), however, produced substantial (2- to 3-fold) and prolonged (up to 4 weeks) increases in plasma copper levels and ceruloplasmin. cobaltiprotoporphyrin 15-36 ceruloplasmin Rattus norvegicus 165-178 7746837-4 1995 This effect on ceruloplasmin was specific to cobalt-protoporphyrin, since equimolar doses (25 mumol/kg body weight) of both tin-protoporphyrin and iron-protoporphyrin did not produce changes in the levels of circulating ceruloplasmin. cobaltiprotoporphyrin 45-66 ceruloplasmin Rattus norvegicus 15-28 7746837-4 1995 This effect on ceruloplasmin was specific to cobalt-protoporphyrin, since equimolar doses (25 mumol/kg body weight) of both tin-protoporphyrin and iron-protoporphyrin did not produce changes in the levels of circulating ceruloplasmin. tin protoporphyrin IX 124-142 ceruloplasmin Rattus norvegicus 15-28 7746837-4 1995 This effect on ceruloplasmin was specific to cobalt-protoporphyrin, since equimolar doses (25 mumol/kg body weight) of both tin-protoporphyrin and iron-protoporphyrin did not produce changes in the levels of circulating ceruloplasmin. iron-protoporphyrin 147-166 ceruloplasmin Rattus norvegicus 15-28 7779549-6 1995 Serum zinc correlated negatively with plasma fibrinogen (r = -0.69, p < 0.0005) and serum copper correlated positively with serum ceruloplasmin (r = 0.92, p < 0.0005) both in indomethacin-treated and untreated arthritic rats. Copper 93-99 ceruloplasmin Rattus norvegicus 133-146 7779549-6 1995 Serum zinc correlated negatively with plasma fibrinogen (r = -0.69, p < 0.0005) and serum copper correlated positively with serum ceruloplasmin (r = 0.92, p < 0.0005) both in indomethacin-treated and untreated arthritic rats. Indomethacin 181-193 ceruloplasmin Rattus norvegicus 133-146 7827136-0 1995 Copper incorporation into ceruloplasmin in rat livers. Copper 0-6 ceruloplasmin Rattus norvegicus 26-39 7827136-6 1995 The data indicate that copper is incorporated into ceruloplasmin late in the course of its transport through the secretory compartments. Copper 23-29 ceruloplasmin Rattus norvegicus 51-64 7825519-3 1995 Copper deficiency, as demonstrated by low plasma copper and ceruloplasmin, caused a decrease of liver, heart, and testes copper; a decline of liver and heart zinc; and an increase of hepatic iron. Copper 121-127 ceruloplasmin Rattus norvegicus 60-73 7825519-3 1995 Copper deficiency, as demonstrated by low plasma copper and ceruloplasmin, caused a decrease of liver, heart, and testes copper; a decline of liver and heart zinc; and an increase of hepatic iron. Iron 191-195 ceruloplasmin Rattus norvegicus 60-73 7926469-3 1994 Wilson"s disease is an autosomal recessive disorder of copper metabolism characterized by abnormal copper accumulation in the liver and low serum ceruloplasmin activity. Copper 55-61 ceruloplasmin Rattus norvegicus 146-159 7850252-0 1994 Direct transfer of copper from metallothionein to superoxide dismutase: a possible mechanism for differential supply of Cu to SOD and ceruloplasmin in LEC rats. Copper 19-25 ceruloplasmin Rattus norvegicus 134-147 7850252-0 1994 Direct transfer of copper from metallothionein to superoxide dismutase: a possible mechanism for differential supply of Cu to SOD and ceruloplasmin in LEC rats. Copper 120-122 ceruloplasmin Rattus norvegicus 134-147 7819403-0 1994 [Influence of ceruloplasmin on the embryotoxic effect of silver ions]. Silver 57-63 ceruloplasmin Rattus norvegicus 14-27 7819403-2 1994 Feeding of AgCl to pregnant female rats throughout gestation did not result in any alterations in their physiological functions, although the active copper-containing ceruloplasmin (Cp) was eliminated from the blood stream. Copper 149-155 ceruloplasmin Rattus norvegicus 167-180 8031737-8 1994 Because the concentrations of Cu in plasma and bile, and also plasma ceruloplasmin (EC 1.16.3.1) activities, showed much greater percentage reductions with increasing Fe intake than did the concentrations of Cu in organs, it is possible that increased Fe status interferes with the mobilization of Cu stores. Iron 167-169 ceruloplasmin Rattus norvegicus 69-82 8280128-0 1993 Lack of copper binding sites in ceruloplasmin of LEC rats with abnormal copper metabolism. Copper 8-14 ceruloplasmin Rattus norvegicus 32-45 8179585-2 1994 The hepatic uptake of tetrabromosulfophthalein (BSP) is also a carrier-mediated function accomplished at least by two different transport mechanisms, bilitranslocase (BTL) and BSP/Bilirubin Binding Protein (BBBP). Sulfobromophthalein 22-46 ceruloplasmin Rattus norvegicus 150-165 8179585-2 1994 The hepatic uptake of tetrabromosulfophthalein (BSP) is also a carrier-mediated function accomplished at least by two different transport mechanisms, bilitranslocase (BTL) and BSP/Bilirubin Binding Protein (BBBP). Sulfobromophthalein 22-46 ceruloplasmin Rattus norvegicus 167-170 8296323-7 1994 However, immunoblot analysis of serum CP in silver-treated groups showed only a slight decrease in protein levels, suggesting that most of the CP existed as an oxidase inactive apo-form. Silver 44-50 ceruloplasmin Rattus norvegicus 38-40 8296323-7 1994 However, immunoblot analysis of serum CP in silver-treated groups showed only a slight decrease in protein levels, suggesting that most of the CP existed as an oxidase inactive apo-form. Silver 44-50 ceruloplasmin Rattus norvegicus 143-145 7841167-0 1994 Methylene blue inhibition of oestradiol-induced increase of ceruloplasmin serum levels in rats. Methylene Blue 0-14 ceruloplasmin Rattus norvegicus 60-73 7841167-0 1994 Methylene blue inhibition of oestradiol-induced increase of ceruloplasmin serum levels in rats. Estradiol 29-39 ceruloplasmin Rattus norvegicus 60-73 7841167-3 1994 We describe the inhibitory effect of methylene blue on the increase of ceruloplasmin plasma level in rats during oestradiol treatment. Methylene Blue 37-51 ceruloplasmin Rattus norvegicus 71-84 7841167-3 1994 We describe the inhibitory effect of methylene blue on the increase of ceruloplasmin plasma level in rats during oestradiol treatment. Estradiol 113-123 ceruloplasmin Rattus norvegicus 71-84 8179585-0 1994 Role of BSP/bilirubin binding protein and bilitranslocase in glutathione uptake in rat basolateral liver plasma membrane vesicles. Glutathione 61-72 ceruloplasmin Rattus norvegicus 42-57 7504610-2 1993 The data indicate that sodium molybdate significantly protected the uptake of lead in blood, liver, and kidneys and restored the lead-induced inhibited activity of blood delta-aminolevulinic acid dehydratase, elevation of blood zinc protoporphyrin, hepatic lipid peroxidation, and serum ceruloplasmin. sodium molybdate(VI) 23-39 ceruloplasmin Rattus norvegicus 287-300 8303090-4 1993 Cu plasma distribution on a gel filtration column by HPLC-ICP revealed that the holo-form of ceruloplasmin (Cp) was present before hepatitis and increased with its development, indicating the availability of Cu for Cp by hepatitis. Copper 0-2 ceruloplasmin Rattus norvegicus 93-106 8292651-1 1993 Biosynthesis and secretion of ceruloplasmin (CP) in rat liver has been studied in order to elucidate its role in the distribution, transport and excretion of copper in the body. Copper 158-164 ceruloplasmin Rattus norvegicus 30-43 8292651-1 1993 Biosynthesis and secretion of ceruloplasmin (CP) in rat liver has been studied in order to elucidate its role in the distribution, transport and excretion of copper in the body. Copper 158-164 ceruloplasmin Rattus norvegicus 45-47 8292651-4 1993 Liver slices incubated in vitro with [35S]methionine were characterized by a two-stage release of [35S]CP into the medium. Sulfur-35 38-41 ceruloplasmin Rattus norvegicus 103-105 8292651-4 1993 Liver slices incubated in vitro with [35S]methionine were characterized by a two-stage release of [35S]CP into the medium. Methionine 42-52 ceruloplasmin Rattus norvegicus 103-105 8292651-4 1993 Liver slices incubated in vitro with [35S]methionine were characterized by a two-stage release of [35S]CP into the medium. Sulfur-35 99-102 ceruloplasmin Rattus norvegicus 103-105 8292651-6 1993 The pulse-labelling experiments with [35S]methionine in rats with catheters inserted into the carotid artery and the common bile duct revealed the polar secretion of two distinct CP species differing in molecular structure and secretion rate. Sulfur-35 38-41 ceruloplasmin Rattus norvegicus 179-181 8292651-6 1993 The pulse-labelling experiments with [35S]methionine in rats with catheters inserted into the carotid artery and the common bile duct revealed the polar secretion of two distinct CP species differing in molecular structure and secretion rate. Methionine 42-52 ceruloplasmin Rattus norvegicus 179-181 8118109-6 1993 Dams fed the low copper diet had low tissue copper concentrations, and low plasma ceruloplasmin and erythrocyte superoxide dismutase activities compared to copper-adequate dams. Copper 17-23 ceruloplasmin Rattus norvegicus 82-95 8120673-0 1993 Responses of tissue ascorbic acid and of serum cholesterol, alpha-tocopherol, and ceruloplasmin in rats to dietary level of cystine. Cystine 124-131 ceruloplasmin Rattus norvegicus 82-95 8120673-4 1993 Addition of 0.3-5% cystine to 10% casein diet and addition of 5% cystine to 25% casein diet caused a decreased activity of serum ceruloplasmin. Cystine 19-26 ceruloplasmin Rattus norvegicus 129-142 8120673-4 1993 Addition of 0.3-5% cystine to 10% casein diet and addition of 5% cystine to 25% casein diet caused a decreased activity of serum ceruloplasmin. Cystine 65-72 ceruloplasmin Rattus norvegicus 129-142 8120673-5 1993 The changes in liver ascorbic acid, serum cholesterol, and serum alpha-tocopherol and in ceruloplasmin activity by dietary cystine correlated with the changes in liver levels of non-protein sulfhydryl. Cystine 123-130 ceruloplasmin Rattus norvegicus 89-102 8373444-8 1993 The Kd value for binding of the organic anions to purified bilitranslocase, a plasma membrane protein involved in the electrogenic transport of pthaleins, was also significantly lower for BSP than DBSP (1.10 +/- 0.12 vs 3.02 +/- 0.27 microM, N = 3, P < 0.001), indicating a higher affinity of the former ligand for the carrier protein. pthaleins 144-153 ceruloplasmin Rattus norvegicus 59-74 8373444-8 1993 The Kd value for binding of the organic anions to purified bilitranslocase, a plasma membrane protein involved in the electrogenic transport of pthaleins, was also significantly lower for BSP than DBSP (1.10 +/- 0.12 vs 3.02 +/- 0.27 microM, N = 3, P < 0.001), indicating a higher affinity of the former ligand for the carrier protein. dbsp 197-201 ceruloplasmin Rattus norvegicus 59-74 1524435-0 1992 Stoichiometry of Fe(II) oxidation during ceruloplasmin-catalyzed loading of ferritin. ammonium ferrous sulfate 17-23 ceruloplasmin Rattus norvegicus 41-54 8394586-1 1993 We have examined the tissue uptake of 67Cu from ceruloplasmin versus albumin and transcuprein, after its intravenous administration to pregnant rats, in the last 4 days of gestation. Copper-67 38-42 ceruloplasmin Rattus norvegicus 48-61 8394586-2 1993 67Cu infused as in vivo-labeled ceruloplasmin remained on ceruloplasmin in the maternal circulation over the 4- to 6-hr time period examined, as determined by gel chromatography and immunoreactivity. Copper-67 0-4 ceruloplasmin Rattus norvegicus 32-45 8394586-2 1993 67Cu infused as in vivo-labeled ceruloplasmin remained on ceruloplasmin in the maternal circulation over the 4- to 6-hr time period examined, as determined by gel chromatography and immunoreactivity. Copper-67 0-4 ceruloplasmin Rattus norvegicus 58-71 8394586-5 1993 Total uptake of Cu from ceruloplasmin was seven times greater than that from albumin and transcuprein for the placenta, whole fetus, and fetal liver. Copper 16-18 ceruloplasmin Rattus norvegicus 24-37 8394586-7 1993 When synthesis of maternal 67Cu-ceruloplasmin (from 67Cu administered on albumin and transcuprein) was inhibited with cycloheximide, uptake by nonhepatic tissues was reduced markedly. Cycloheximide 118-131 ceruloplasmin Rattus norvegicus 32-45 8394586-10 1993 We conclude that Cu destined for the fetus is delivered mainly or exclusively by ceruloplasmin. Copper 17-19 ceruloplasmin Rattus norvegicus 81-94 8473340-0 1993 Inhibition of the copper incorporation into ceruloplasmin leads to the deficiency in serum ceruloplasmin activity in Long-Evans cinnamon mutant rat. Copper 18-24 ceruloplasmin Rattus norvegicus 44-57 8473340-0 1993 Inhibition of the copper incorporation into ceruloplasmin leads to the deficiency in serum ceruloplasmin activity in Long-Evans cinnamon mutant rat. Copper 18-24 ceruloplasmin Rattus norvegicus 91-104 8473340-1 1993 Although ceruloplasmin is known to be a copper-transporting protein, little is known about the biochemical mechanisms of copper incorporation into ceruloplasmin during the biosynthesis. Copper 40-46 ceruloplasmin Rattus norvegicus 9-22 8473340-7 1993 These results suggest that an abnormality of the copper delivery mechanism causes an inhibition of copper incorporation into the ceruloplasmin molecule in the liver, leading to the deficiency in serum ceruloplasmin activity in the LEC rat. Copper 49-55 ceruloplasmin Rattus norvegicus 129-142 8473340-7 1993 These results suggest that an abnormality of the copper delivery mechanism causes an inhibition of copper incorporation into the ceruloplasmin molecule in the liver, leading to the deficiency in serum ceruloplasmin activity in the LEC rat. Copper 49-55 ceruloplasmin Rattus norvegicus 201-214 8473340-7 1993 These results suggest that an abnormality of the copper delivery mechanism causes an inhibition of copper incorporation into the ceruloplasmin molecule in the liver, leading to the deficiency in serum ceruloplasmin activity in the LEC rat. Copper 99-105 ceruloplasmin Rattus norvegicus 129-142 8473340-7 1993 These results suggest that an abnormality of the copper delivery mechanism causes an inhibition of copper incorporation into the ceruloplasmin molecule in the liver, leading to the deficiency in serum ceruloplasmin activity in the LEC rat. Copper 99-105 ceruloplasmin Rattus norvegicus 201-214 8231629-3 1993 Results from pulse labeling of ceruloplasmin for 3 hours with [35S]methionine in primary hepatocyte culture, followed by immunoprecipitation, SDS-PAGE and fluorography, showed only minor changes in ceruloplasmin protein synthesis and secretion. Sulfur-35 63-66 ceruloplasmin Rattus norvegicus 31-44 8231629-3 1993 Results from pulse labeling of ceruloplasmin for 3 hours with [35S]methionine in primary hepatocyte culture, followed by immunoprecipitation, SDS-PAGE and fluorography, showed only minor changes in ceruloplasmin protein synthesis and secretion. Methionine 67-77 ceruloplasmin Rattus norvegicus 31-44 8231629-3 1993 Results from pulse labeling of ceruloplasmin for 3 hours with [35S]methionine in primary hepatocyte culture, followed by immunoprecipitation, SDS-PAGE and fluorography, showed only minor changes in ceruloplasmin protein synthesis and secretion. Sodium Dodecyl Sulfate 142-145 ceruloplasmin Rattus norvegicus 31-44 1524435-8 1992 These results provide evidence for ceruloplasmin as an effective catalyst for the incorporation of iron into both apo- and holoferritin. Iron 99-103 ceruloplasmin Rattus norvegicus 35-48 8396362-1 1993 Ceruloplasmin (Cp), the main copper transport glycoprotein found in the blood, delivers its copper to intracellular proteins via a plasma membrane receptor protein. Copper 29-35 ceruloplasmin Rattus norvegicus 0-13 8489241-0 1993 Synthesis and turnover of ceruloplasmin in rats treated with 17 beta-estradiol. Estradiol 61-78 ceruloplasmin Rattus norvegicus 26-39 8489241-2 1993 Daily treatment with 140 microgram 17 beta-estradiol resulted in a slow rise of ceruloplasmin concentrations, as measured by p-phenylenediamine oxidase activity, leading to a 70% increase by 7 days and a tripling by Day 14. Estradiol 35-52 ceruloplasmin Rattus norvegicus 80-93 1524435-1 1992 Ceruloplasmin catalyzed the incorporation of iron into apoferritin with a stoichiometry of 3.8 Fe(II)/O2. Iron 45-49 ceruloplasmin Rattus norvegicus 0-13 1524435-1 1992 Ceruloplasmin catalyzed the incorporation of iron into apoferritin with a stoichiometry of 3.8 Fe(II)/O2. ammonium ferrous sulfate 95-101 ceruloplasmin Rattus norvegicus 0-13 1524435-1 1992 Ceruloplasmin catalyzed the incorporation of iron into apoferritin with a stoichiometry of 3.8 Fe(II)/O2. Oxygen 102-104 ceruloplasmin Rattus norvegicus 0-13 1447833-7 1992 In addition, TE-5 prevented the reductions of growth rate, iron metabolism functions, plasma alkaline phosphatase activity, serum ceruloplasmin concentration and liver pyruvate carboxylase activity. TE 5 13-17 ceruloplasmin Rattus norvegicus 130-143 1415546-7 1992 Addition of polyclonal monospecific anti-bilitranslocase antibody to liver vesicles specifically inhibited TBS uptake rate (3.27 +/- 0.17 vs. 5.82 +/- 0.61 nmol.s-1.mg protein-1, n = 3, P less than 0.001). 3,4,5,6-tetrabromophenolsulfonephthalein 107-110 ceruloplasmin Rattus norvegicus 41-56 1415546-8 1992 These data indicate that TBS is electrogenically transported across the liver cell plasma membrane by bilitranslocase. 3,4,5,6-tetrabromophenolsulfonephthalein 25-28 ceruloplasmin Rattus norvegicus 102-117 1377744-8 1992 The absolute increase in ceruloplasmin in response to TNF was enhanced in rats fed the alanine-supplemented diet relative to those fed the 20% casein diet. Alanine 87-94 ceruloplasmin Rattus norvegicus 25-38 1354437-5 1992 We utilized this CP gene polymorphism for the investigation of the pathogenesis of the aberrant hepatic copper metabolism in LEC mutant rat, since CP has a pivotal role in copper metabolism in the liver. Copper 104-110 ceruloplasmin Rattus norvegicus 17-19 1354437-5 1992 We utilized this CP gene polymorphism for the investigation of the pathogenesis of the aberrant hepatic copper metabolism in LEC mutant rat, since CP has a pivotal role in copper metabolism in the liver. Copper 104-110 ceruloplasmin Rattus norvegicus 147-149 1354437-5 1992 We utilized this CP gene polymorphism for the investigation of the pathogenesis of the aberrant hepatic copper metabolism in LEC mutant rat, since CP has a pivotal role in copper metabolism in the liver. Copper 172-178 ceruloplasmin Rattus norvegicus 17-19 1354437-5 1992 We utilized this CP gene polymorphism for the investigation of the pathogenesis of the aberrant hepatic copper metabolism in LEC mutant rat, since CP has a pivotal role in copper metabolism in the liver. Copper 172-178 ceruloplasmin Rattus norvegicus 147-149 1377744-10 1992 This observation--the effects of taurine and serine on lung GSH and a significant negative correlation between ceruloplasmin and liver and lung GSH concentration in rats fed TNF--suggests that supplemental serine and taurine may improve antioxidant defenses when dietary supplies of cysteine are low but do not influence cysteine availability for a normal response to TNF. Serine 206-212 ceruloplasmin Rattus norvegicus 111-124 1377744-10 1992 This observation--the effects of taurine and serine on lung GSH and a significant negative correlation between ceruloplasmin and liver and lung GSH concentration in rats fed TNF--suggests that supplemental serine and taurine may improve antioxidant defenses when dietary supplies of cysteine are low but do not influence cysteine availability for a normal response to TNF. Taurine 217-224 ceruloplasmin Rattus norvegicus 111-124 1996664-7 1991 Exposure of adult rats to 95% O2 resulted in a five- to sixfold induction of ceruloplasmin mRNA in lung tissue within 46 h, and this response was time dependent, reaching maximum values at 86 h. Hyperoxic induction of ceruloplasmin mRNA was specific to the lung and not the result of systemic inflammation because hepatic ceruloplasmin mRNA content remained constant. Oxygen 30-32 ceruloplasmin Rattus norvegicus 218-231 1777845-0 1991 Protective effects of ceruloplasmin against electrolysis-induced oxygen free radicals in rat heart. oxygen free radicals 65-85 ceruloplasmin Rattus norvegicus 22-35 1777845-7 1991 Moreover, CP significantly reduced the increase of norepinephrine washout in the effluent perfusate after electrolysis suggesting a protection against free radical-induced injury to sympathetic nerve endings. Norepinephrine 51-65 ceruloplasmin Rattus norvegicus 10-12 1777845-7 1991 Moreover, CP significantly reduced the increase of norepinephrine washout in the effluent perfusate after electrolysis suggesting a protection against free radical-induced injury to sympathetic nerve endings. Free Radicals 151-163 ceruloplasmin Rattus norvegicus 10-12 1858867-6 1991 In comparison, ceruloplasmin (Cp) transferred relatively little copper to tissues (less than 1 microgram/h). Copper 64-70 ceruloplasmin Rattus norvegicus 15-28 1531003-5 1992 Kinetic analysis of rat ceruloplasmin produced a biphasic v vs v/s plot with apparent Km"s of 40 and 1.5 microM for iron. Iron 116-120 ceruloplasmin Rattus norvegicus 24-37 1531003-7 1992 Rates of p-phenylenediamine oxidation by rat ceruloplasmin were about one-half those obtained with human ceruloplasmin, with maximal p-phenylenediamine oxidase activity at pH 5.0 for both enzymes. 4-phenylenediamine 9-27 ceruloplasmin Rattus norvegicus 45-58 1936203-5 1991 It seems likely that excretion of Cu from the liver into the bile and blood (as ceruloplasmin) is inherently lacking in the LEC rat. Copper 34-36 ceruloplasmin Rattus norvegicus 80-93 1788866-1 1991 Carbon tetrachloride injected to white rats during four days in the dose of 2 g/kg drastically activates intensity of free radical lipid oxidation and induces impairment of the antioxidant system inhibition of the activity of superoxide dismutase, catalase, glutathione peroxidase, glutathione reductase, a decrease of SH-groups and general plasma ceruloplasmin level and total phospholipids in the liver. Carbon Tetrachloride 0-20 ceruloplasmin Rattus norvegicus 348-361 2045141-4 1991 Rats fed the high sodium diets were characterized by high plasma copper concentrations and ceruloplasmin activities compared with their respective control sodium rats. Sodium 18-24 ceruloplasmin Rattus norvegicus 91-104 2045141-5 1991 The magnitude of the sodium-induced rise in plasma copper and ceruloplasmin was affected by dietary copper intake; however, dietary copper intake had no effect on the development of hypertension in the high sodium groups. Sodium 21-27 ceruloplasmin Rattus norvegicus 62-75 2045141-5 1991 The magnitude of the sodium-induced rise in plasma copper and ceruloplasmin was affected by dietary copper intake; however, dietary copper intake had no effect on the development of hypertension in the high sodium groups. Copper 100-106 ceruloplasmin Rattus norvegicus 62-75 2045141-5 1991 The magnitude of the sodium-induced rise in plasma copper and ceruloplasmin was affected by dietary copper intake; however, dietary copper intake had no effect on the development of hypertension in the high sodium groups. Copper 100-106 ceruloplasmin Rattus norvegicus 62-75 2045141-8 1991 At the lower levels of copper intake, sodium chloride-induced hypertension increased red blood cell superoxide dismutase activity in a manner consistent with the plasma copper and ceruloplasmin changes observed. Copper 23-29 ceruloplasmin Rattus norvegicus 180-193 2045141-8 1991 At the lower levels of copper intake, sodium chloride-induced hypertension increased red blood cell superoxide dismutase activity in a manner consistent with the plasma copper and ceruloplasmin changes observed. Sodium Chloride 38-53 ceruloplasmin Rattus norvegicus 180-193 1996664-7 1991 Exposure of adult rats to 95% O2 resulted in a five- to sixfold induction of ceruloplasmin mRNA in lung tissue within 46 h, and this response was time dependent, reaching maximum values at 86 h. Hyperoxic induction of ceruloplasmin mRNA was specific to the lung and not the result of systemic inflammation because hepatic ceruloplasmin mRNA content remained constant. Oxygen 30-32 ceruloplasmin Rattus norvegicus 77-90 1996664-7 1991 Exposure of adult rats to 95% O2 resulted in a five- to sixfold induction of ceruloplasmin mRNA in lung tissue within 46 h, and this response was time dependent, reaching maximum values at 86 h. Hyperoxic induction of ceruloplasmin mRNA was specific to the lung and not the result of systemic inflammation because hepatic ceruloplasmin mRNA content remained constant. Oxygen 30-32 ceruloplasmin Rattus norvegicus 218-231 2085622-9 1990 The mechanism of production of multiple molecular forms of CP and their roles in copper metabolism are postulated. Copper 81-87 ceruloplasmin Rattus norvegicus 59-61 1916310-0 1991 Effects of age and turpentine-induced inflammation on the activity of ceruloplasmin from blood of CFY rats. Turpentine 19-29 ceruloplasmin Rattus norvegicus 70-83 1916310-2 1991 The increase in NaCl and KCl concentrations in vitro resulted in the same exponential decrease in activities of CP from both young and old animals. Sodium Chloride 16-20 ceruloplasmin Rattus norvegicus 112-114 1916310-2 1991 The increase in NaCl and KCl concentrations in vitro resulted in the same exponential decrease in activities of CP from both young and old animals. Potassium Chloride 25-28 ceruloplasmin Rattus norvegicus 112-114 1916310-3 1991 Turpentine-induced inflammation caused an increase in blood CP levels in both young (52%) and old (25%) animals compared to age-matched controls (p less than 0.001 and p less than 0.01, respectively). Turpentine 0-10 ceruloplasmin Rattus norvegicus 60-62 2230804-7 1990 Ceruloplasmin, the copper transport protein, was a weak inhibitor of 125I-ferrotransferrin binding. 125i-ferrotransferrin 69-90 ceruloplasmin Rattus norvegicus 0-13 2172537-10 1990 Enzymes such as tyrosinase, ceruloplasmin, and peroxidase and rat brain mitochondria catalyze the oxidation of 5,6-DHT to form dimer 7 and, ultimately, indolic melanin. 5,6-Dihydroxytryptamine 111-118 ceruloplasmin Rattus norvegicus 28-41 2172537-10 1990 Enzymes such as tyrosinase, ceruloplasmin, and peroxidase and rat brain mitochondria catalyze the oxidation of 5,6-DHT to form dimer 7 and, ultimately, indolic melanin. indolic melanin 152-167 ceruloplasmin Rattus norvegicus 28-41 2221093-1 1990 Bilirubin and phthalein dyes are taken up by the liver via a carrier-mediated mechanism operated at least in part by bilitranslocase (BTL). Bilirubin 0-9 ceruloplasmin Rattus norvegicus 117-132 2178323-1 1990 Rat ceruloplasmin (rCp) has been labeled with the fluorophores fluorescein and rhodamine by using the isothiocyanate derivatives (FITC, RBITC). Fluorescein 63-74 ceruloplasmin Rattus norvegicus 4-17 2178323-1 1990 Rat ceruloplasmin (rCp) has been labeled with the fluorophores fluorescein and rhodamine by using the isothiocyanate derivatives (FITC, RBITC). Rhodamines 79-88 ceruloplasmin Rattus norvegicus 4-17 2178323-1 1990 Rat ceruloplasmin (rCp) has been labeled with the fluorophores fluorescein and rhodamine by using the isothiocyanate derivatives (FITC, RBITC). isothiocyanic acid 102-116 ceruloplasmin Rattus norvegicus 4-17 2178323-1 1990 Rat ceruloplasmin (rCp) has been labeled with the fluorophores fluorescein and rhodamine by using the isothiocyanate derivatives (FITC, RBITC). Fluorescein-5-isothiocyanate 130-134 ceruloplasmin Rattus norvegicus 4-17 2178323-1 1990 Rat ceruloplasmin (rCp) has been labeled with the fluorophores fluorescein and rhodamine by using the isothiocyanate derivatives (FITC, RBITC). rbitc 136-141 ceruloplasmin Rattus norvegicus 4-17 2171432-1 1990 Ceruloplasmin (CP), a circulating glycoprotein, is known for its copper transport. Copper 65-71 ceruloplasmin Rattus norvegicus 0-13 2171432-1 1990 Ceruloplasmin (CP), a circulating glycoprotein, is known for its copper transport. Copper 65-71 ceruloplasmin Rattus norvegicus 15-17 2171432-6 1990 Membrane proteins were labeled with 125I and passed through an affinity column in which CP was covalently linked to Sepharose 4B. Sepharose 116-125 ceruloplasmin Rattus norvegicus 88-90 2221093-1 1990 Bilirubin and phthalein dyes are taken up by the liver via a carrier-mediated mechanism operated at least in part by bilitranslocase (BTL). Bilirubin 0-9 ceruloplasmin Rattus norvegicus 134-137 2221093-1 1990 Bilirubin and phthalein dyes are taken up by the liver via a carrier-mediated mechanism operated at least in part by bilitranslocase (BTL). phthalein 14-23 ceruloplasmin Rattus norvegicus 117-132 2221093-1 1990 Bilirubin and phthalein dyes are taken up by the liver via a carrier-mediated mechanism operated at least in part by bilitranslocase (BTL). phthalein 14-23 ceruloplasmin Rattus norvegicus 134-137 2221093-7 1990 Competitive inhibition was observed with both unconjugated bilirubin (Ki, 2.9 +/- 0.2 microM) and rifamycin SV (Ki, 76 +/- 10 microM), known competitors for hepatic BTL-mediated transport of BSP. Bilirubin 59-68 ceruloplasmin Rattus norvegicus 165-168 2221093-7 1990 Competitive inhibition was observed with both unconjugated bilirubin (Ki, 2.9 +/- 0.2 microM) and rifamycin SV (Ki, 76 +/- 10 microM), known competitors for hepatic BTL-mediated transport of BSP. rifamycin SV 98-110 ceruloplasmin Rattus norvegicus 165-168 2399253-2 1990 Rats became copper-depleted after 4 weeks on diets containing less than 0.5 micrograms of copper/g as evidenced by significant decreases in liver copper and serum ceruloplasmin. Copper 12-18 ceruloplasmin Rattus norvegicus 163-176 2213250-1 1990 Stress such as inflammation produces an acute phase response that includes elevated levels of ceruloplasmin, the main copper component of plasma. Copper 118-124 ceruloplasmin Rattus norvegicus 94-107 2213250-3 1990 Cu-Zn superoxide dismutase (SOD) activities in liver, the main site of ceruloplasmin secretion, decreased with turpentine-induced inflammation (0.1 mL, intramuscular, leg) in rats fed any of three copper levels (adequate = 6 mg/kg, marginal = 2.5 mg/kg and deficient less than 0.5 mg/kg). Turpentine 111-121 ceruloplasmin Rattus norvegicus 71-84 2213250-8 1990 Inflammatory effects on other copper enzyme activities did occur as evidenced by increases in ceruloplasmin and decreases in serum extracellular SOD. Copper 30-36 ceruloplasmin Rattus norvegicus 94-107 2399253-2 1990 Rats became copper-depleted after 4 weeks on diets containing less than 0.5 micrograms of copper/g as evidenced by significant decreases in liver copper and serum ceruloplasmin. Copper 90-96 ceruloplasmin Rattus norvegicus 163-176 2399253-2 1990 Rats became copper-depleted after 4 weeks on diets containing less than 0.5 micrograms of copper/g as evidenced by significant decreases in liver copper and serum ceruloplasmin. Copper 90-96 ceruloplasmin Rattus norvegicus 163-176 2364072-0 1990 Arginine residues are involved in the transport function of bilitranslocase. Arginine 0-8 ceruloplasmin Rattus norvegicus 60-75 2364072-3 1990 It is concluded that the transport function of bilitranslocase depends on arginine residues, which are involved in the interaction with the molecules to be translocated. Arginine 74-82 ceruloplasmin Rattus norvegicus 47-62 2364072-2 1990 Their reaction is shown to be affected by sulfobromophthalein, Thymol blue and bilirubin, which are translocated by bilitranslocase across the plasma membrane. Sulfobromophthalein 42-61 ceruloplasmin Rattus norvegicus 116-131 2364072-2 1990 Their reaction is shown to be affected by sulfobromophthalein, Thymol blue and bilirubin, which are translocated by bilitranslocase across the plasma membrane. thymol blue 63-74 ceruloplasmin Rattus norvegicus 116-131 2364072-2 1990 Their reaction is shown to be affected by sulfobromophthalein, Thymol blue and bilirubin, which are translocated by bilitranslocase across the plasma membrane. Bilirubin 79-88 ceruloplasmin Rattus norvegicus 116-131 2344475-0 1990 In vivo effects of nickel and cadmium in rats on lipid peroxidation and ceruloplasmin activity. Nickel 19-25 ceruloplasmin Rattus norvegicus 72-85 2344475-0 1990 In vivo effects of nickel and cadmium in rats on lipid peroxidation and ceruloplasmin activity. Cadmium 30-37 ceruloplasmin Rattus norvegicus 72-85 2294965-0 1990 The sulfhydryl groups responsible for bilitranslocase transport activity respond to the interaction of the carrier with bilirubin and functional analogues. Bilirubin 120-129 ceruloplasmin Rattus norvegicus 38-53 2163530-1 1990 The paper is concerned with the experimental data on a ERP signal size in two blood plasma metalloproteins--ceruloplasmin and transferrin and their correlations after intraperitoneal hydrocortisone and corticotropin injections (5 mg and 2.5 U/100 g body weight, respectively) to Wistar adult male rats and after bilateral adrenalectomy. Hydrocortisone 183-197 ceruloplasmin Rattus norvegicus 108-121 2163530-2 1990 A conclusion has been made that antioxidant activity of the ceruloplasmin-transferrin complex in rat blood plasma is increased with a rise of the corticotropin level but it is decreased with hydrocortisone loading. Hydrocortisone 191-205 ceruloplasmin Rattus norvegicus 60-73 2294965-1 1990 Both inactivation of sulfobromophthalein transport in rat liver plasma membrane vesicles by sulfhydryl group reagents and subsequent reactivation by 2-mercaptoethanol are shown to be modulated by ligands to bilitranslocase. Sulfobromophthalein 21-40 ceruloplasmin Rattus norvegicus 207-222 2294965-1 1990 Both inactivation of sulfobromophthalein transport in rat liver plasma membrane vesicles by sulfhydryl group reagents and subsequent reactivation by 2-mercaptoethanol are shown to be modulated by ligands to bilitranslocase. Mercaptoethanol 149-166 ceruloplasmin Rattus norvegicus 207-222 2294965-4 1990 The effect brought about by remarkably low concentrations of bilirubin is in line with the physiological function of bilitranslocase as a bilirubin carrier. Bilirubin 61-70 ceruloplasmin Rattus norvegicus 117-132 2294965-4 1990 The effect brought about by remarkably low concentrations of bilirubin is in line with the physiological function of bilitranslocase as a bilirubin carrier. Bilirubin 138-147 ceruloplasmin Rattus norvegicus 117-132 2400627-3 1990 (2) Total iron absorption is significantly higher in ceruloplasmin-substituted copper-deficient animals as compared to copper-deficient controls. Iron 10-14 ceruloplasmin Rattus norvegicus 53-66 2400627-3 1990 (2) Total iron absorption is significantly higher in ceruloplasmin-substituted copper-deficient animals as compared to copper-deficient controls. Copper 79-85 ceruloplasmin Rattus norvegicus 53-66 2400627-4 1990 (3) The appearance rate of absorbed iron in the portal blood of copper-deficient animals increased several times immediately after the intravenous infusion of ceruloplasmin. Iron 36-40 ceruloplasmin Rattus norvegicus 159-172 2400627-4 1990 (3) The appearance rate of absorbed iron in the portal blood of copper-deficient animals increased several times immediately after the intravenous infusion of ceruloplasmin. Copper 64-70 ceruloplasmin Rattus norvegicus 159-172 2400627-5 1990 (5) The distribution of absorbed iron was changed due to the ceruloplasmin substitution: it was increased in the reticulocytes (+66%), plasma (+400%) and the body (+112%), whereas in the liver it was decreased by about 78%. Iron 33-37 ceruloplasmin Rattus norvegicus 61-74 2400627-7 1990 (6) The conclusion was drawn that, as for the entrance into the mucosa from the luminal side, also for the release at the contraluminal side into the portal blood, the ferrous state of iron is favoured and that ceruloplasmin accelerates the release into the portal blood by catalyzing the oxidation of ferrous iron due to its high Fe(II): oxygen oxidoreductase (EC 1.16.3.1) activity. Iron 310-314 ceruloplasmin Rattus norvegicus 211-224 2400627-7 1990 (6) The conclusion was drawn that, as for the entrance into the mucosa from the luminal side, also for the release at the contraluminal side into the portal blood, the ferrous state of iron is favoured and that ceruloplasmin accelerates the release into the portal blood by catalyzing the oxidation of ferrous iron due to its high Fe(II): oxygen oxidoreductase (EC 1.16.3.1) activity. ammonium ferrous sulfate 331-337 ceruloplasmin Rattus norvegicus 211-224 34445367-7 2021 UCB administration to animals with AIA lead to a significant decrease in hind paws volume, plasma levels of C-reactive protein (CRP) and ceruloplasmin, drop of leukocytes, lymphocytes, erythrocytes, hemoglobin and an increase in platelet count. ucb 0-3 ceruloplasmin Rattus norvegicus 137-150 2379262-2 1990 Concomitant administration of Se (6.3 mumol/kg, intraperitoneally) and 63Ni (0.12 mmol/kg subcutaneously) lowered the Ni burden of all the soft organs and the plasma ceruloplasmin levels. Selenium 30-32 ceruloplasmin Rattus norvegicus 166-179 2379262-2 1990 Concomitant administration of Se (6.3 mumol/kg, intraperitoneally) and 63Ni (0.12 mmol/kg subcutaneously) lowered the Ni burden of all the soft organs and the plasma ceruloplasmin levels. Nickel-63 71-75 ceruloplasmin Rattus norvegicus 166-179 34818604-0 2022 Tetrathiomolybdate Partially Alleviates Erectile Dysfunction of Type 1 Diabetic Rats Through Affecting Ceruloplasmin/eNOS and Inhibiting Corporal Fibrosis and Systemic Inflammation. tetrathiomolybdate 0-18 ceruloplasmin Rattus norvegicus 103-116 34818604-17 2022 Yin Y, Peng J, Zhou J, et al., Tetrathiomolybdate Partially Alleviates Erectile Dysfunction of Type 1 Diabetic Rats Through Affecting Ceruloplasmin/eNOS and Inhibiting Corporal Fibrosis and Systemic Inflammation. tetrathiomolybdate 31-49 ceruloplasmin Rattus norvegicus 134-147 35446470-8 2022 Alterations in hematological parameters, rheumatoid factor, C-reactive protein, and ceruloplasmin in arthritis were reverted by lupeol. lupeol 128-134 ceruloplasmin Rattus norvegicus 84-97