PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29700330-5 2018 Silencing of PrPC in 1.1B4 cells resulted in significant depletion of intracellular (IC) iron, and remarkably, upregulation of glucose transporter GLUT2 and insulin. Iron 89-93 prion protein Homo sapiens 13-17 29700330-6 2018 Iron overloading, on the other hand, resulted in downregulation of GLUT2 and insulin in a PrPC-dependent manner. Iron 0-4 prion protein Homo sapiens 90-94 25862412-6 2015 Expression of exogenous PrP(C) in HepG2 cells increased uptake and storage of ferric iron (Fe(3+)), not ferrous iron (Fe(2+)), from the medium, supporting the function of PrP(C) as a plasma membrane FR. Iron 85-89 prion protein Homo sapiens 24-30 28769992-13 2017 With tannin consumption, PRP production is increased, and may be an initial line of defense against tannin-non-heme iron chelation in vivo. Iron 116-120 prion protein Homo sapiens 25-28 19212444-4 2009 In this report, we provide evidence that PrP(C) mediates cellular iron uptake and transport, and mutant PrP forms alter cellular iron levels differentially. Iron 66-70 prion protein Homo sapiens 41-47 19283067-9 2009 These results suggest that sequestration of iron in PrP(Sc)-ferritin complexes induces a state of iron bio-insufficiency in prion disease-affected brains, resulting in increased uptake and a state of iron dyshomeostasis. Iron 44-48 prion protein Homo sapiens 52-55 19283067-9 2009 These results suggest that sequestration of iron in PrP(Sc)-ferritin complexes induces a state of iron bio-insufficiency in prion disease-affected brains, resulting in increased uptake and a state of iron dyshomeostasis. Iron 98-102 prion protein Homo sapiens 52-55 19212444-9 2009 Neither PrP(C) nor the mutant PrP forms influence the rate or amount of iron released into the medium, suggesting a functional role for PrP(C) in cellular iron uptake and transport to ferritin, and dysfunction of PrP(C) as a significant contributing factor of brain iron imbalance in prion disorders. Iron 155-159 prion protein Homo sapiens 136-142 19212444-4 2009 In this report, we provide evidence that PrP(C) mediates cellular iron uptake and transport, and mutant PrP forms alter cellular iron levels differentially. Iron 66-70 prion protein Homo sapiens 41-44 19212444-9 2009 Neither PrP(C) nor the mutant PrP forms influence the rate or amount of iron released into the medium, suggesting a functional role for PrP(C) in cellular iron uptake and transport to ferritin, and dysfunction of PrP(C) as a significant contributing factor of brain iron imbalance in prion disorders. Iron 155-159 prion protein Homo sapiens 136-142 19212444-5 2009 Using human neuroblastoma cells as models, we demonstrate that over-expression of PrP(C) increases intra-cellular iron relative to non-transfected controls as indicated by an increase in total cellular iron, the cellular labile iron pool (LIP), and iron content of ferritin. Iron 114-118 prion protein Homo sapiens 82-88 19212444-9 2009 Neither PrP(C) nor the mutant PrP forms influence the rate or amount of iron released into the medium, suggesting a functional role for PrP(C) in cellular iron uptake and transport to ferritin, and dysfunction of PrP(C) as a significant contributing factor of brain iron imbalance in prion disorders. Iron 155-159 prion protein Homo sapiens 136-142 19212444-9 2009 Neither PrP(C) nor the mutant PrP forms influence the rate or amount of iron released into the medium, suggesting a functional role for PrP(C) in cellular iron uptake and transport to ferritin, and dysfunction of PrP(C) as a significant contributing factor of brain iron imbalance in prion disorders. Iron 155-159 prion protein Homo sapiens 136-142 19212444-5 2009 Using human neuroblastoma cells as models, we demonstrate that over-expression of PrP(C) increases intra-cellular iron relative to non-transfected controls as indicated by an increase in total cellular iron, the cellular labile iron pool (LIP), and iron content of ferritin. Iron 202-206 prion protein Homo sapiens 82-88 19212444-5 2009 Using human neuroblastoma cells as models, we demonstrate that over-expression of PrP(C) increases intra-cellular iron relative to non-transfected controls as indicated by an increase in total cellular iron, the cellular labile iron pool (LIP), and iron content of ferritin. Iron 202-206 prion protein Homo sapiens 82-88 19212444-5 2009 Using human neuroblastoma cells as models, we demonstrate that over-expression of PrP(C) increases intra-cellular iron relative to non-transfected controls as indicated by an increase in total cellular iron, the cellular labile iron pool (LIP), and iron content of ferritin. Iron 202-206 prion protein Homo sapiens 82-88 19212444-7 2009 The positive effect of PrP(C) on ferritin iron content is enhanced by stimulating PrP(C) endocytosis, and reversed by cross-linking PrP(C) on the plasma membrane. Iron 42-46 prion protein Homo sapiens 23-29 19212444-7 2009 The positive effect of PrP(C) on ferritin iron content is enhanced by stimulating PrP(C) endocytosis, and reversed by cross-linking PrP(C) on the plasma membrane. Iron 42-46 prion protein Homo sapiens 82-88 19212444-7 2009 The positive effect of PrP(C) on ferritin iron content is enhanced by stimulating PrP(C) endocytosis, and reversed by cross-linking PrP(C) on the plasma membrane. Iron 42-46 prion protein Homo sapiens 82-88 19212444-8 2009 Expression of mutant PrP forms lacking the octapeptide-repeats, the membrane anchor, or carrying the pathogenic mutation PrP(102L) decreases ferritin iron content significantly relative to PrP(C) expressing cells, but the effect on cellular LIP and levels of Tf, TfR, and ferritin is complex, varying with the mutation. Iron 150-154 prion protein Homo sapiens 21-24 19212444-8 2009 Expression of mutant PrP forms lacking the octapeptide-repeats, the membrane anchor, or carrying the pathogenic mutation PrP(102L) decreases ferritin iron content significantly relative to PrP(C) expressing cells, but the effect on cellular LIP and levels of Tf, TfR, and ferritin is complex, varying with the mutation. Iron 150-154 prion protein Homo sapiens 121-124 17567949-3 2007 In this report, we demonstrate that PrP(C) binds iron and transforms to a PrP(Sc)-like form (*PrP(Sc)) when human neuroblastoma cells are exposed to an inorganic source of redox iron. Iron 49-53 prion protein Homo sapiens 36-42 17567949-3 2007 In this report, we demonstrate that PrP(C) binds iron and transforms to a PrP(Sc)-like form (*PrP(Sc)) when human neuroblastoma cells are exposed to an inorganic source of redox iron. Iron 49-53 prion protein Homo sapiens 36-39 17567949-3 2007 In this report, we demonstrate that PrP(C) binds iron and transforms to a PrP(Sc)-like form (*PrP(Sc)) when human neuroblastoma cells are exposed to an inorganic source of redox iron. Iron 178-182 prion protein Homo sapiens 36-42 17567949-3 2007 In this report, we demonstrate that PrP(C) binds iron and transforms to a PrP(Sc)-like form (*PrP(Sc)) when human neuroblastoma cells are exposed to an inorganic source of redox iron. Iron 178-182 prion protein Homo sapiens 36-39 17567949-3 2007 In this report, we demonstrate that PrP(C) binds iron and transforms to a PrP(Sc)-like form (*PrP(Sc)) when human neuroblastoma cells are exposed to an inorganic source of redox iron. Iron 178-182 prion protein Homo sapiens 74-77 17567949-6 2007 Furthermore, we demonstrate increased redox-active ferrous iron levels in prion disease-affected brains, suggesting that accumulation of PrP(Sc) is modulated by the combined effect of imbalance in brain iron homeostasis and the redox-active nature of PrP(Sc). Iron 59-63 prion protein Homo sapiens 137-140 16212360-10 2005 The orbital interactions between iron(III) and porphyrin have been examined on the basis of these chemical shifts, from which we have found that both the d(xy)-a(2u) interaction in the ruffled Fe(T(i)PrP)L2+ and d(xy)-a(1u) interaction in the saddled Fe(OETPP)L2+ are quite weak in the high-spin and probably in the intermediate-spin complexes as well. Iron 33-37 prion protein Homo sapiens 200-203