PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33335181-10 2020 These results demonstrate that the RSK-ABCB1 and HIF-1alpha-FECH axes are the downstream pathways of Ras/MEK involved in the regulation of PpIX accumulation. protoporphyrin IX 139-143 ferrochelatase Mus musculus 60-64 33620374-0 2021 Retinal Phenotyping of Ferrochelatase Mutant Mice Reveals Protoporphyrin Accumulation and Reduced Neovascular Response. protoporphyrin IX 58-72 ferrochelatase Mus musculus 23-37 33335181-0 2020 MEK reduces cancer-specific PpIX accumulation through the RSK-ABCB1 and HIF-1alpha-FECH axes. protoporphyrin IX 28-32 ferrochelatase Mus musculus 83-87 33335181-2 2020 We previously reported that inhibition of oncogenic Ras/MEK increases PpIX accumulation in cancer cells by reducing PpIX efflux through ATP-binding cassette sub-family B member 1 (ABCB1) and ferrochelatase (FECH)-catalysed PpIX conversion to haem. protoporphyrin IX 70-74 ferrochelatase Mus musculus 191-205 33335181-2 2020 We previously reported that inhibition of oncogenic Ras/MEK increases PpIX accumulation in cancer cells by reducing PpIX efflux through ATP-binding cassette sub-family B member 1 (ABCB1) and ferrochelatase (FECH)-catalysed PpIX conversion to haem. protoporphyrin IX 70-74 ferrochelatase Mus musculus 207-211 33335181-2 2020 We previously reported that inhibition of oncogenic Ras/MEK increases PpIX accumulation in cancer cells by reducing PpIX efflux through ATP-binding cassette sub-family B member 1 (ABCB1) and ferrochelatase (FECH)-catalysed PpIX conversion to haem. protoporphyrin IX 116-120 ferrochelatase Mus musculus 191-205 33335181-2 2020 We previously reported that inhibition of oncogenic Ras/MEK increases PpIX accumulation in cancer cells by reducing PpIX efflux through ATP-binding cassette sub-family B member 1 (ABCB1) and ferrochelatase (FECH)-catalysed PpIX conversion to haem. protoporphyrin IX 116-120 ferrochelatase Mus musculus 207-211 33335181-2 2020 We previously reported that inhibition of oncogenic Ras/MEK increases PpIX accumulation in cancer cells by reducing PpIX efflux through ATP-binding cassette sub-family B member 1 (ABCB1) and ferrochelatase (FECH)-catalysed PpIX conversion to haem. protoporphyrin IX 116-120 ferrochelatase Mus musculus 191-205 33335181-2 2020 We previously reported that inhibition of oncogenic Ras/MEK increases PpIX accumulation in cancer cells by reducing PpIX efflux through ATP-binding cassette sub-family B member 1 (ABCB1) and ferrochelatase (FECH)-catalysed PpIX conversion to haem. protoporphyrin IX 116-120 ferrochelatase Mus musculus 207-211 33335181-3 2020 Here, we sought to identify the downstream pathways of Ras/MEK involved in the regulation of PpIX accumulation via ABCB1 and FECH. protoporphyrin IX 93-97 ferrochelatase Mus musculus 125-129 26343413-7 2015 N-methyl PPIX strongly inhibits ferrochelatase, the enzyme that converts PPIX to heme, and leads to PPIX accumulation. protoporphyrin IX 9-13 ferrochelatase Mus musculus 32-46 29906468-1 2018 Erythropoietic protoporphyria (EPP) is a genetic disease that results from the defective mutation in the gene encoding ferrochelatase (FECH), the enzyme that converts protoporphyrin IX (PPIX) to heme. protoporphyrin IX 167-184 ferrochelatase Mus musculus 119-133 29906468-1 2018 Erythropoietic protoporphyria (EPP) is a genetic disease that results from the defective mutation in the gene encoding ferrochelatase (FECH), the enzyme that converts protoporphyrin IX (PPIX) to heme. protoporphyrin IX 167-184 ferrochelatase Mus musculus 135-139 29906468-1 2018 Erythropoietic protoporphyria (EPP) is a genetic disease that results from the defective mutation in the gene encoding ferrochelatase (FECH), the enzyme that converts protoporphyrin IX (PPIX) to heme. protoporphyrin IX 186-190 ferrochelatase Mus musculus 119-133 29906468-1 2018 Erythropoietic protoporphyria (EPP) is a genetic disease that results from the defective mutation in the gene encoding ferrochelatase (FECH), the enzyme that converts protoporphyrin IX (PPIX) to heme. protoporphyrin IX 186-190 ferrochelatase Mus musculus 135-139 29906468-4 2018 As expected, we observed the accumulation of PPIX in the liver of Fech-mut mice. protoporphyrin IX 45-49 ferrochelatase Mus musculus 66-70 29906468-7 2018 Furthermore, we found that the major phosphatidylcholines (PC) in the liver and the ratio of total PC to PPIX in the bile were decreased in Fech-mut mice compared to wild type mice. protoporphyrin IX 105-109 ferrochelatase Mus musculus 140-144 27438535-6 2016 We also found that INH downregulates ferrochelatase (FECH), the enzyme that converts PPIX to heme. protoporphyrin IX 85-89 ferrochelatase Mus musculus 37-51 27438535-6 2016 We also found that INH downregulates ferrochelatase (FECH), the enzyme that converts PPIX to heme. protoporphyrin IX 85-89 ferrochelatase Mus musculus 53-57 31990410-1 2020 Reduced ferrochelatase activity in erythropoietic protoporphyria (EPP) causes the accumulation of protoporphyrin IX (PPIX) leading to acute cutaneous photosensitivity and liver injury. protoporphyrin IX 98-115 ferrochelatase Mus musculus 8-22 31990410-1 2020 Reduced ferrochelatase activity in erythropoietic protoporphyria (EPP) causes the accumulation of protoporphyrin IX (PPIX) leading to acute cutaneous photosensitivity and liver injury. protoporphyrin IX 117-121 ferrochelatase Mus musculus 8-22 31748741-3 2019 Haem synthesis is completed in mitochondria, with ferrochelatase adding iron to protoporphyrin IX. protoporphyrin IX 80-97 ferrochelatase Mus musculus 50-64 28093505-1 2017 Erythropoietic protoporphyria (EPP) is caused by deficiency of ferrochelatase (FECH), which incorporates iron into protoporphyrin IX (PPIX) to form heme. protoporphyrin IX 115-132 ferrochelatase Mus musculus 79-83 28093505-1 2017 Erythropoietic protoporphyria (EPP) is caused by deficiency of ferrochelatase (FECH), which incorporates iron into protoporphyrin IX (PPIX) to form heme. protoporphyrin IX 134-138 ferrochelatase Mus musculus 79-83 28093505-8 2017 F1 hybrids obtained by crossing these mice with another inbred line carrying a severe Fech mutation (named m1Pas) show a very strong EPP phenotype that includes elevated PPIX in the blood, enlargement of liver and spleen, anemia, as well as strong pain reactions and skin lesions after a short period of light exposure. protoporphyrin IX 170-174 ferrochelatase Mus musculus 86-90 26343413-7 2015 N-methyl PPIX strongly inhibits ferrochelatase, the enzyme that converts PPIX to heme, and leads to PPIX accumulation. protoporphyrin IX 73-77 ferrochelatase Mus musculus 32-46 25659899-5 2015 ET-1 increased superoxide production and the detection of protoporphyrin IX fluorescence, suggesting oxidant conditions might impair heme biosynthesis by ferrochelatase. protoporphyrin IX 58-75 ferrochelatase Mus musculus 154-168 24284092-1 2013 BACKGROUND: The aim of this study was to clarify the mechanism of accumulation of 5-aminolevulinic acid (ALA)-dependent protoporphyrin IX (PpIX), ALA-photodynamic therapy (PDT)-induced cell death and enhanced efficiency by a ferrochelatase inhibitor in prostate cancer PC-3 cells. protoporphyrin IX 120-137 ferrochelatase Mus musculus 225-239 24284092-1 2013 BACKGROUND: The aim of this study was to clarify the mechanism of accumulation of 5-aminolevulinic acid (ALA)-dependent protoporphyrin IX (PpIX), ALA-photodynamic therapy (PDT)-induced cell death and enhanced efficiency by a ferrochelatase inhibitor in prostate cancer PC-3 cells. protoporphyrin IX 139-143 ferrochelatase Mus musculus 225-239 24284092-8 2013 Inhibition of ferrochelatase by deferoxamine and NOC-18 led to increase of PpIX accumulation and enhanced effect of ALA-PDT in PC-3 cells. protoporphyrin IX 75-79 ferrochelatase Mus musculus 14-28 21222436-1 2011 The heme biosynthetic pathway culminates with the ferrochelatase-catalyzed ferrous iron chelation into protoporphyrin IX to form protoheme. protoporphyrin IX 103-120 ferrochelatase Mus musculus 50-64 22349098-2 2012 In previous studies, we demonstrated a significant downregulation of Ferrochelatase (FECH) mRNA-expression in colorectal carcinomas leading to the accumulation of protoporphyrin IX (PpIX), a fluorescent metabolite of the heme synthesis. protoporphyrin IX 163-180 ferrochelatase Mus musculus 69-83 22349098-2 2012 In previous studies, we demonstrated a significant downregulation of Ferrochelatase (FECH) mRNA-expression in colorectal carcinomas leading to the accumulation of protoporphyrin IX (PpIX), a fluorescent metabolite of the heme synthesis. protoporphyrin IX 163-180 ferrochelatase Mus musculus 85-89 22349098-2 2012 In previous studies, we demonstrated a significant downregulation of Ferrochelatase (FECH) mRNA-expression in colorectal carcinomas leading to the accumulation of protoporphyrin IX (PpIX), a fluorescent metabolite of the heme synthesis. protoporphyrin IX 182-186 ferrochelatase Mus musculus 69-83 22349098-2 2012 In previous studies, we demonstrated a significant downregulation of Ferrochelatase (FECH) mRNA-expression in colorectal carcinomas leading to the accumulation of protoporphyrin IX (PpIX), a fluorescent metabolite of the heme synthesis. protoporphyrin IX 182-186 ferrochelatase Mus musculus 85-89 22349098-3 2012 In this article, we report on first in vivo experiments in xenografted nude mice using folate-coupled liposomes or dendritic polyglycerolamine nanoparticles carrying ferrochelatase-siRNA to enhance PpIX-derived fluorescence in the tumor tissue. protoporphyrin IX 198-202 ferrochelatase Mus musculus 166-180 21222436-8 2011 The results lead us to propose that the decrease in the induced protoporphyrin IX saddling mode is associated with a less stringent metal ion preference by ferrochelatase and a slower porphyrin chelation step. protoporphyrin IX 64-81 ferrochelatase Mus musculus 156-170 19543923-2 2009 Ferrochelatase, the last enzyme in the catalytic pathway of the haem biosynthesis, catalyses the reaction of insertion of a ferrous ion into protoporphyrin IX by distorting the planar geometry of the latter reactant. protoporphyrin IX 141-158 ferrochelatase Mus musculus 0-14 20966079-1 2010 Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to form heme. protoporphyrin IX 60-77 ferrochelatase Mus musculus 0-14 16792525-1 2006 Protoporhyrin IX ferrochelatase catalyses the terminal step of the haem-biosynthetic pathway by inserting ferrous iron into protoporphyrin IX. protoporphyrin IX 124-141 ferrochelatase Mus musculus 17-31 19251765-1 2009 Ferrochelatase (FECH) catalyses the insertion of ferrous ions into protoporphyrin IX to produce haem at the haem-biosynthetic pathway. protoporphyrin IX 67-84 ferrochelatase Mus musculus 0-14 19251765-1 2009 Ferrochelatase (FECH) catalyses the insertion of ferrous ions into protoporphyrin IX to produce haem at the haem-biosynthetic pathway. protoporphyrin IX 67-84 ferrochelatase Mus musculus 16-20 19787086-1 2008 Ferrochelatase (FECH) activity is decreased in erythropoietic protoporphyria (EPP), causing increased production and excretion of protoporphyrin. protoporphyrin IX 130-144 ferrochelatase Mus musculus 0-14 19787086-1 2008 Ferrochelatase (FECH) activity is decreased in erythropoietic protoporphyria (EPP), causing increased production and excretion of protoporphyrin. protoporphyrin IX 130-144 ferrochelatase Mus musculus 16-20 17314268-2 2007 A deficiency in ferrochelatase, which mediates the final step in heme biosynthesis, leads to erythropoietic protoporphyria (EPP), a photosensitivity syndrome caused by the accumulation of PPIX in the skin. protoporphyrin IX 188-192 ferrochelatase Mus musculus 16-30 18593702-1 2008 Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to form heme. protoporphyrin IX 60-77 ferrochelatase Mus musculus 0-14 18593702-4 2008 These analyses reveal that purified recombinant ferrochelatase from both murine and yeast sources inserts not only ferrous iron but also divalent cobalt, zinc, nickel, and copper into protoporphyrin IX to form the corresponding metalloporphyrins but with considerable mechanistic variability. protoporphyrin IX 184-201 ferrochelatase Mus musculus 48-62 16288996-2 2005 To investigate the role of ferrochelatase in the accumulation of protoporphyrin, we first made mouse fibroblast Balb/3T3 cells highly expressing ferrochelatase and examined the ALA-induced photo-damage as well as the accumulation of porphyrin in the cells. protoporphyrin IX 65-79 ferrochelatase Mus musculus 27-41 16288996-4 2005 The accumulation of protoporphyrin was also abolished in human erythroleukemia K562 cells stably expressing mouse ferrochelatase. protoporphyrin IX 20-34 ferrochelatase Mus musculus 114-128 16288996-8 2005 Thus, the light-induced cell death was tightly coupled with the accumulation of protoporphyrin caused by a decrease in ferrochelatase. protoporphyrin IX 80-94 ferrochelatase Mus musculus 119-133 16288996-11 2005 Taken together, not only the low level of ferrochelatase but also the augmented uptake of ALA contributes to the ALA-induced accumulation of protoporphyrin IX and subsequent photo-damage in cancer cells. protoporphyrin IX 141-158 ferrochelatase Mus musculus 42-56 15496139-1 2005 Ferrochelatase (EC 4.99.1.1), the terminal enzyme of the haem biosynthetic pathway, catalyses the chelation of Fe(II) into the protoporphyrin IX ring. protoporphyrin IX 127-144 ferrochelatase Mus musculus 0-14 15496139-7 2005 Similarly, murine ferrochelatase variants, in which the active site Glu-289 was replaced by either glutamine or alanine and, when purified, contained specifically-bound protoporphyrin, exhibited enhanced protein stability when compared with wild-type ferrochelatase. protoporphyrin IX 169-183 ferrochelatase Mus musculus 18-32 10704201-1 2000 Ferrochelatase (EC 4.99.1.1), the terminal enzyme of the heme biosynthetic pathway, catalyzes Fe(2+) chelation into protoporphyrin IX. protoporphyrin IX 116-133 ferrochelatase Mus musculus 0-14 15654982-1 2005 Erythropoietic protoporphyria (EPP) is caused by a defect in ferrochelatase, leading to the accumulation of protoporphyrin predominantly in erythrocytes and hepatocytes, and resulting in skin photosensitivity upon leaching of blood protoporphyrin into the skin. protoporphyrin IX 108-122 ferrochelatase Mus musculus 61-75 15654982-1 2005 Erythropoietic protoporphyria (EPP) is caused by a defect in ferrochelatase, leading to the accumulation of protoporphyrin predominantly in erythrocytes and hepatocytes, and resulting in skin photosensitivity upon leaching of blood protoporphyrin into the skin. protoporphyrin IX 232-246 ferrochelatase Mus musculus 61-75 14981080-1 2004 Ferrochelatase catalyzes the terminal step of the heme biosynthetic pathway by inserting ferrous iron into protoporphyrin IX. protoporphyrin IX 107-124 ferrochelatase Mus musculus 0-14 12359345-0 2002 Protoporphyrin-IX accumulation and cutaneous tumor regression in mice using a ferrochelatase inhibitor. protoporphyrin IX 0-17 ferrochelatase Mus musculus 78-92 12149233-2 2002 The enzymatic defect of protoporphyria is a deficiency in ferrochelatase, which chelates iron and protoporphyrin IX to form heme. protoporphyrin IX 98-115 ferrochelatase Mus musculus 58-72 11336654-1 2001 Ferrochelatase (EC 4.99.1.1) is the terminal enzyme of the haem biosynthetic pathway and catalyses iron chelation into the protoporphyrin IX ring. protoporphyrin IX 123-140 ferrochelatase Mus musculus 0-14 10869291-5 2000 When Fech/Fech mice received bone marrow cells from normal animals, the accumulation of protoporphyrin in red blood cells and plasma was reduced 10-fold but still remained 2.5 times above normal levels. protoporphyrin IX 88-102 ferrochelatase Mus musculus 5-9 10869291-5 2000 When Fech/Fech mice received bone marrow cells from normal animals, the accumulation of protoporphyrin in red blood cells and plasma was reduced 10-fold but still remained 2.5 times above normal levels. protoporphyrin IX 88-102 ferrochelatase Mus musculus 10-14 15284838-1 2004 Erythropoietic protoporphyria (EPP) is an inherited defect of the ferrochelatase (FECH) gene characterized by the accumulation of toxic protoporphyrin in the liver and bone marrow resulting in severe skin photosensitivity. protoporphyrin IX 136-150 ferrochelatase Mus musculus 82-86 12081474-0 2002 Binding of protoporphyrin IX and metal derivatives to the active site of wild-type mouse ferrochelatase at low porphyrin-to-protein ratios. protoporphyrin IX 11-28 ferrochelatase Mus musculus 89-103 12081474-8 2002 Similarly for free-base protoporphyrin, the natural substrate of ferrochelatase, the RR spectra of porphyrin-protein complexes reveal a saddling distortion of the porphyrin. protoporphyrin IX 24-38 ferrochelatase Mus musculus 65-79 11939775-1 2002 Ferrochelatase (EC 4.99.1.1), the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into the protoporphyrin IX ring. protoporphyrin IX 133-150 ferrochelatase Mus musculus 0-14 10523727-1 1999 This study was designed to investigate the hypothesis that the inhibition of ferrochelatase will cause in situ build up of high concentrations of protoporphyrin-IX which may act as a putative agent for photodestruction of cancer cells. protoporphyrin IX 146-163 ferrochelatase Mus musculus 77-91 8358292-10 1993 When Zn is added as a substrate for the terminal enzyme, ferrochelatase, along with coproporphyrinogen, there is formation of Zn protoporphyrin with little accumulation of free protoporphyrin. protoporphyrin IX 129-143 ferrochelatase Mus musculus 57-71 10089831-2 1999 Photosensitivity of target cells may be influenced by mitochondrial iron levels because ferrochelatase-catalyzed insertion of Fe2+ into PpIX converts it to heme, a nonsensitizer. protoporphyrin IX 136-140 ferrochelatase Mus musculus 88-102 8266338-4 1993 The porphyrin which accumulates in the liver has been identified as protoporphyrin IX and dose response and time course studies confirm prior inhibition of mitochondrial ferrochelatase as the causal lesion. protoporphyrin IX 68-85 ferrochelatase Mus musculus 170-184 10464147-1 1999 BACKGROUND & AIMS: Reduced activity of ferrochelatase in erythropoietic protoporphyria (EPP) results in protoporphyrin (PP) accumulation in erythrocytes and liver. protoporphyrin IX 108-122 ferrochelatase Mus musculus 43-57 1704134-1 1991 Ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) catalyzes the last step in the heme biosynthetic pathway, the chelation of ferrous iron and protoporphyrin to form heme. protoporphyrin IX 144-158 ferrochelatase Mus musculus 0-14 1704134-1 1991 Ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) catalyzes the last step in the heme biosynthetic pathway, the chelation of ferrous iron and protoporphyrin to form heme. protoporphyrin IX 144-158 ferrochelatase Mus musculus 16-37 1288876-5 1992 Conversely addition of precursors of haem synthesis (5-aminolaevulinic acid or protoporphyrin IX) led to an increased mRNA synthesis for ferrochelatase. protoporphyrin IX 79-96 ferrochelatase Mus musculus 137-151 1288876-6 1992 In addition to protoporphyrin synthesis the supply of another substrate, iron, is decisive for the gene expression ferrochelatase. protoporphyrin IX 15-29 ferrochelatase Mus musculus 115-129