PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 17316903-0 2007 Ceruloplasmin expression and its role in iron transport in C6 cells. Iron 41-45 ceruloplasmin Rattus norvegicus 0-13 17316903-1 2007 Ceruloplasmin (CP) is essential for brain iron homeostasis. Iron 42-46 ceruloplasmin Rattus norvegicus 0-13 17316903-1 2007 Ceruloplasmin (CP) is essential for brain iron homeostasis. Iron 42-46 ceruloplasmin Rattus norvegicus 15-17 17316903-8 2007 We also examined the effects of CP on iron transport in the cells. Iron 38-42 ceruloplasmin Rattus norvegicus 32-34 17316903-2 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 17316903-10 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 17316903-6 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 17316903-10 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 17316903-6 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 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 16671455-2 2006 Ceruloplasmin is involved in iron metabolism by oxidizing ferrous iron to ferric iron. Iron 29-33 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. Iron 122-126 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 16671455-12 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 16671455-3 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 16671455-11 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 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 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 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 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 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 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 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 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 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 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 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 9647667-7 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 9647667-14 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 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 9169016-0 1997 Loading of iron into recombinant rat liver ferritin heteropolymers by ceruloplasmin. Iron 11-15 ceruloplasmin Rattus norvegicus 70-83 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 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 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 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 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 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 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 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 2400627-5 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 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 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 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 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 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 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 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 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 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+). 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 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 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 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 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 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 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 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. 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 25656940-9 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 25656940-0 2015 Ceruloplasmin is Involved in the Nigral Iron Accumulation of 6-OHDA-Lesioned Rats. Iron 40-44 ceruloplasmin Rattus norvegicus 0-13 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 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 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 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 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 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 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 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 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 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