PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23939757-1 2013 Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions. Iron 130-134 heme oxygenase 1 Homo sapiens 0-16 23939757-1 2013 Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions. Iron 130-134 heme oxygenase 1 Homo sapiens 18-23 23714423-2 2013 Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme. Iron 167-171 heme oxygenase 1 Homo sapiens 0-16 24179613-2 2013 HO-1, a stress-responsive enzyme that catabolizes heme into carbon monoxide (CO), biliverdin and iron, has previously been shown to protect grafts from ischemia/reperfusion and rejection. Iron 97-101 heme oxygenase 1 Homo sapiens 0-4 23850497-1 2013 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that is induced by intraplaque hemorrhage and degrades free heme and releases ferrous iron, which is rapidly sequestered by ferritin. Iron 137-141 heme oxygenase 1 Homo sapiens 0-16 23850497-1 2013 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme that is induced by intraplaque hemorrhage and degrades free heme and releases ferrous iron, which is rapidly sequestered by ferritin. Iron 137-141 heme oxygenase 1 Homo sapiens 18-22 23714423-2 2013 Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme. Iron 167-171 heme oxygenase 1 Homo sapiens 18-22 23714423-2 2013 Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. We show in this study that HO-1 expression is reduced in PBMCs of MS patients and that during exacerbation of the disease there is a significant downregulation of this enzyme. Iron 167-171 heme oxygenase 1 Homo sapiens 207-211 23454680-0 2013 Role of alpha-synuclein aggregation and the nuclear factor E2-related factor 2/heme oxygenase-1 pathway in iron-induced neurotoxicity. Iron 107-111 heme oxygenase 1 Homo sapiens 44-95 23615401-8 2013 HO-1 end products, such as carbon monoxide, free iron and bilirubin, suppressed the TPA-induced MMP-9 mRNA and protein expression, enzyme activity, migration and invasion in MCF-7 cells. Iron 49-53 heme oxygenase 1 Homo sapiens 0-4 23184650-0 2013 Akt/Nrf2 activated upregulation of heme oxygenase-1 involves in the role of Rg1 against ferrous iron-induced neurotoxicity in SK-N-SH cells. Iron 96-100 heme oxygenase 1 Homo sapiens 35-51 23454680-8 2013 These results support a new hypothesis of synergistic alpha-syn/iron cytotoxicity, whereby ferrous iron induces alpha-syn aggregation and neurotoxicity by inhibiting Nrf2/HO-1. Iron 64-68 heme oxygenase 1 Homo sapiens 171-175 23454680-3 2013 Here, we report that down-regulation of nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) may contribute to iron-induced alpha-syn aggregation. Iron 128-132 heme oxygenase 1 Homo sapiens 86-102 23454680-9 2013 Inhibition of Nrf2/HO-1 leads to more alpha-syn aggregation and greater toxicity induced by iron, creating a vicious cycle of iron accumulation, alpha-syn aggregation and HO-1 disruption in PD. Iron 92-96 heme oxygenase 1 Homo sapiens 19-23 23454680-3 2013 Here, we report that down-regulation of nuclear factor E2-related factor 2 (Nrf2) and heme oxygenase-1 (HO-1) may contribute to iron-induced alpha-syn aggregation. Iron 128-132 heme oxygenase 1 Homo sapiens 104-108 23454680-9 2013 Inhibition of Nrf2/HO-1 leads to more alpha-syn aggregation and greater toxicity induced by iron, creating a vicious cycle of iron accumulation, alpha-syn aggregation and HO-1 disruption in PD. Iron 126-130 heme oxygenase 1 Homo sapiens 19-23 23090785-1 2013 Heme oxygenase-1 (HO-1) is both beneficial and detrimental to the host in some viral infections by catalyzing the conversion of heme to biliverdin, iron, and carbon monoxide. Iron 148-152 heme oxygenase 1 Homo sapiens 18-22 23350672-8 2013 Hemopexin sequesters heme, thus preventing unregulated heme uptake that leads to toxicity; it safely delivers heme to neuronal cells; and it activates the induction of proteins including HO1 and hAPP that keep heme and iron at safe levels in neurons. Iron 219-223 heme oxygenase 1 Homo sapiens 187-190 23403148-4 2013 One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron. Iron 176-180 heme oxygenase 1 Homo sapiens 59-75 23403148-4 2013 One of the key molecules implicated in sPE pathogenesis is heme oxygenase-1 (HO-1), a rate-limiting enzyme that breaks down heme into carbon monoxide (CO), biliverdin and free iron. Iron 176-180 heme oxygenase 1 Homo sapiens 77-81 23092328-6 2013 HO-1 is a heme-degrading enzyme generating carbon monoxide, iron, and biliverdin/bilirubin, while BCRP is a heme efflux transporter. Iron 60-64 heme oxygenase 1 Homo sapiens 0-4 22989377-5 2013 However, HO-1-overexpressing cells contain only ~25% as much "loose" (probably redox active) iron. Iron 93-97 heme oxygenase 1 Homo sapiens 9-13 22989377-9 2013 We conclude that, at least in many cases, the cytoprotective effects of HO-1 induction or forced overexpression may derive from elevated expression of ferritin and consequent reduction of redox active "loose" iron. Iron 209-213 heme oxygenase 1 Homo sapiens 72-76 22564156-3 2012 Hence, the ability of exogenously-added copper, iron and zinc to influence HO-1 expression in HCT-116 cells was evaluated. Iron 48-52 heme oxygenase 1 Homo sapiens 75-79 23874015-4 2013 HO-1, a microsomal enzyme, catalyzes the breakdown of pro-oxidant heme, which is released from heme proteins to equimolar quantities of iron, carbon monoxide, and biliverdin. Iron 136-140 heme oxygenase 1 Homo sapiens 0-4 22419571-1 2012 Heme-oxygenase 1 is an endoplasmic reticulum-anchored enzyme that breaks down heme into iron, carbon monoxide and biliverdin. Iron 88-92 heme oxygenase 1 Homo sapiens 0-16 22881289-2 2012 The stress protein, HO-1 mediates the degradation of cellular heme to biliverdin/bilirubin, free iron, and CO and is up-regulated in the brains of persons with Alzheimer"s disease and Parkinson"s disease. Iron 97-101 heme oxygenase 1 Homo sapiens 20-24 23140858-2 2013 The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally. Iron 150-154 heme oxygenase 1 Homo sapiens 11-27 23140858-2 2013 The enzyme heme oxygenase-1 (HO-1) generates three separate signaling molecules through the catalysis of heme - carbon monoxide (CO), biliverdin, and iron - each of which acts via distinct molecular targets to influence cell function, both proximally and distally. Iron 150-154 heme oxygenase 1 Homo sapiens 29-33 22923613-1 2012 Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin. Iron 140-144 heme oxygenase 1 Homo sapiens 6-29 22923613-1 2012 Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin. Iron 140-144 heme oxygenase 1 Homo sapiens 31-44 22587389-4 2012 One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron. Iron 181-185 heme oxygenase 1 Homo sapiens 64-80 22819264-1 2012 INTRODUCTION: Heme oxygenase-1 (HO-1) is the rate limiting enzyme that catalyzes the conversion of heme into biliverdin, free iron, and carbon monoxide (CO). Iron 126-130 heme oxygenase 1 Homo sapiens 14-30 22587389-4 2012 One of the key enzymes that control monocyte and DC function is haem oxygenase-1 (HO-1), which catalyses the degradation of the haem group into biliverdin, carbon monoxide and free iron. Iron 181-185 heme oxygenase 1 Homo sapiens 82-86 22492492-1 2012 Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion. Iron 135-139 heme oxygenase 1 Homo sapiens 0-16 22579918-0 2012 Sustained expression of heme oxygenase-1 alters iron homeostasis in nonerythroid cells. Iron 48-52 heme oxygenase 1 Homo sapiens 24-40 22579918-7 2012 Together, our results reveal a novel and coordinated adaptive response of nonerythroid cells to sustained HO-1 induction that has an impact on cellular iron homeostasis. Iron 152-156 heme oxygenase 1 Homo sapiens 106-110 22440905-8 2012 In iron-challenged, cultured proximal tubule cells, we observed a positive correlation between HO-1 mRNA level and HO-1 release. Iron 3-7 heme oxygenase 1 Homo sapiens 95-99 22440905-8 2012 In iron-challenged, cultured proximal tubule cells, we observed a positive correlation between HO-1 mRNA level and HO-1 release. Iron 3-7 heme oxygenase 1 Homo sapiens 115-119 22302482-1 2012 Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress. Iron 84-88 heme oxygenase 1 Homo sapiens 0-16 22302482-1 2012 Heme oxygenase-1 (HO-1) catabolizes heme into carbon monoxide, biliverdin, and free iron which mediate its protective effect against oxidative stress. Iron 84-88 heme oxygenase 1 Homo sapiens 18-22 22503972-4 2012 Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein. Iron 77-81 heme oxygenase 1 Homo sapiens 0-16 22503972-4 2012 Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein. Iron 77-81 heme oxygenase 1 Homo sapiens 18-21 22492492-1 2012 Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion. Iron 135-139 heme oxygenase 1 Homo sapiens 18-22 22088544-1 2011 BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron. Iron 115-119 heme oxygenase 1 Homo sapiens 12-28 21647550-2 2012 On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences. Iron 253-257 heme oxygenase 1 Homo sapiens 162-167 21647550-2 2012 On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences. Iron 253-257 heme oxygenase 1 Homo sapiens 122-138 21647550-2 2012 On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences. Iron 253-257 heme oxygenase 1 Homo sapiens 140-144 22037960-3 2012 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme catabolism and results in the production of iron, carbon monoxide (CO), and biliverdin IXalpha. Iron 114-118 heme oxygenase 1 Homo sapiens 0-16 22037960-3 2012 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme catabolism and results in the production of iron, carbon monoxide (CO), and biliverdin IXalpha. Iron 114-118 heme oxygenase 1 Homo sapiens 18-22 23095372-5 2012 RESULTS: CD163-expressing macrophages, HO-1 and NADPH-p22 expression were located in areas surrounding tubules with iron deposits and filled with erythrocyte casts. Iron 116-120 heme oxygenase 1 Homo sapiens 39-43 22090784-1 2011 Heme oxygenase-1 (HO-1) system catalyzes heme to biologically active products: carbon monoxide, biliverdin/bilirubin and free iron. Iron 126-130 heme oxygenase 1 Homo sapiens 0-16 22088544-1 2011 BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron. Iron 115-119 heme oxygenase 1 Homo sapiens 30-34 21171611-12 2011 The induction of oxidative stress and inflammatory responses (evaluated by HO-1 mRNA expression and TNF-alpha mRNA and protein expression) revealed a reduction in inflammogenicity upon iron loading and a more inflammogenic potency of DQ12 ascribed to undissociated SiOH interacting via H-bonding with cell membrane components. Iron 185-189 heme oxygenase 1 Homo sapiens 75-79 21079975-3 2011 Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron. Iron 123-127 heme oxygenase 1 Homo sapiens 17-33 21079975-3 2011 Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron. Iron 123-127 heme oxygenase 1 Homo sapiens 35-38 21079975-6 2011 OBJECTIVE: This study focused on the uptake and transport of heme iron and on the role of heme oxygenase-1 on heme iron metabolism. Iron 115-119 heme oxygenase 1 Homo sapiens 90-106 21079975-8 2011 A full-length heme oxygenase-1 cDNA was expressed in Caco-2 cells and intracellular iron and heme-Fe content, heme uptake, heme and iron transport and heme oxygenase-1 immunolocalization were assessed in these cells. Iron 84-88 heme oxygenase 1 Homo sapiens 14-30 21079975-10 2011 In cells overexpressing HO1, heme-Fe uptake and transepithelial Fe transport was higher than in controls. Iron 34-36 heme oxygenase 1 Homo sapiens 24-27 21079975-10 2011 In cells overexpressing HO1, heme-Fe uptake and transepithelial Fe transport was higher than in controls. Iron 64-66 heme oxygenase 1 Homo sapiens 24-27 21079975-14 2011 CONCLUSIONS: These results suggest that heme oxygenase-1 catabolizes most of the heme-Fe and favors iron influx and efflux in intestinal cells. Iron 100-104 heme oxygenase 1 Homo sapiens 40-56 21622183-1 2011 Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin. Iron 124-136 heme oxygenase 1 Homo sapiens 0-16 21622183-1 2011 Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting step in the metabolism of free heme into equimolar amounts of ferrous iron, carbon monoxide (CO), and biliverdin. Iron 124-136 heme oxygenase 1 Homo sapiens 18-22 20563825-3 2011 Astroglial induction of the Hmox1 gene by beta-amyloid, pro-inflammatory cytokines and hydrogen peroxide promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergy failure amply documented in AD-affected neural tissues. Iron 161-165 heme oxygenase 1 Homo sapiens 28-33 20563825-3 2011 Astroglial induction of the Hmox1 gene by beta-amyloid, pro-inflammatory cytokines and hydrogen peroxide promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergy failure amply documented in AD-affected neural tissues. Iron 232-236 heme oxygenase 1 Homo sapiens 28-33 20563825-5 2011 Suppression of glial HO-1 activity by pharmacological or other means may confer neuroprotection in AD by curtailing iron-mediated neurotoxicity. Iron 116-120 heme oxygenase 1 Homo sapiens 21-25 21544718-7 2011 Heme oxygenase-1 is considered to be an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron and biliverdin, while SIRT1 is the mammalian homologue of the yeast silent information regulator (Sir)-2, which are involved in the suppression of inflammatory mediators or factors that may be used to improve atopy-related symptoms. Iron 106-110 heme oxygenase 1 Homo sapiens 0-16 21462044-5 2011 HO-1 is an antioxidant enzyme that catabolizes heme to carbon monoxide, free iron, and biliverdin, all of which are involved in the suppression of inflammatory mediators. Iron 77-81 heme oxygenase 1 Homo sapiens 0-4 21185934-3 2011 Under hypoxia, the expression of major iron homeostasis genes including transferrin, transferrin receptor, ceruloplasmin, and heme oxygenase-1 is activated by hypoxia-inducible factors to provide increased iron availability for erythropoiesis in an attempt to enhance oxygen uptake and delivery to hypoxic cells. Iron 39-43 heme oxygenase 1 Homo sapiens 126-142 21185934-3 2011 Under hypoxia, the expression of major iron homeostasis genes including transferrin, transferrin receptor, ceruloplasmin, and heme oxygenase-1 is activated by hypoxia-inducible factors to provide increased iron availability for erythropoiesis in an attempt to enhance oxygen uptake and delivery to hypoxic cells. Iron 206-210 heme oxygenase 1 Homo sapiens 126-142 21373265-1 2011 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO). Iron 122-126 heme oxygenase 1 Homo sapiens 0-16 21373265-1 2011 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme, followed by production of biliverdin, free iron and carbon monoxide (CO). Iron 122-126 heme oxygenase 1 Homo sapiens 18-22 22162689-0 2011 Heme Oxygenase-1: A Critical Link between Iron Metabolism, Erythropoiesis, and Development. Iron 42-46 heme oxygenase 1 Homo sapiens 0-16 22162689-4 2011 Null mutation of Hmox1 results in significant embryonic mortality as well as anemia and defective iron recycling. Iron 98-102 heme oxygenase 1 Homo sapiens 17-22 21182221-2 2010 Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide. Iron 104-108 heme oxygenase 1 Homo sapiens 0-16 22254194-3 2011 Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron. Iron 101-105 heme oxygenase 1 Homo sapiens 0-16 22254194-3 2011 Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron. Iron 101-105 heme oxygenase 1 Homo sapiens 18-22 20941616-1 2011 Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli. Iron 167-171 heme oxygenase 1 Homo sapiens 0-16 20941616-1 2011 Heme oxygenase-1 (HO-1) is one of the three isoforms of the heme oxygenase enzyme that catabolyzes the degradation of heme into biliverdin with the production of free iron and CO. HO-1 is induced by its substrate and by other stimuli, including agents involved in oxidative stress and proinflammatory cytokines as well as several anti-inflammatory stimuli. Iron 167-171 heme oxygenase 1 Homo sapiens 18-22 20934533-0 2011 Cellular iron depletion weakens induction of heme oxygenase-1 by cadmium. Iron 9-13 heme oxygenase 1 Homo sapiens 45-61 20934533-4 2011 This effect of cadmium was weaker in cells made iron-deficient with the iron chelator, desferrioxamine, which was associated with repression of heme oxygenase-1 protein and mRNA expression. Iron 48-52 heme oxygenase 1 Homo sapiens 144-160 20934533-4 2011 This effect of cadmium was weaker in cells made iron-deficient with the iron chelator, desferrioxamine, which was associated with repression of heme oxygenase-1 protein and mRNA expression. Iron 72-76 heme oxygenase 1 Homo sapiens 144-160 20934533-5 2011 The repression by desferrioxamine of cadmium-induced heme oxygenase-1 upregulation was reversed upon iron replenishment of the cells. Iron 101-105 heme oxygenase 1 Homo sapiens 53-69 20934533-10 2011 It is concluded that adequate amounts of iron, which at the atomic level can serve as the pivotal element of heme in NADPH oxidase, must be present in cells to permit what appears to be thiol redox-sensitive, NADPH oxidase-dependent upregulation of heme oxygenase-1. Iron 41-45 heme oxygenase 1 Homo sapiens 249-265 20950636-7 2011 ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell. Iron 111-115 heme oxygenase 1 Homo sapiens 32-48 20950636-7 2011 ATO, on the other hand, induced heme oxygenase-1 (HO-1) to catalyze heme degradation, thereby provided ferrous iron for EGCG-induced hydrogen peroxide to precede Fenton reaction, which in turn generated deleterious reactive oxygen species to damage cell. Iron 111-115 heme oxygenase 1 Homo sapiens 50-54 21182221-2 2010 Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide. Iron 104-108 heme oxygenase 1 Homo sapiens 18-22 20730621-8 2010 The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1). Iron 99-103 heme oxygenase 1 Homo sapiens 441-457 20704546-1 2010 Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron. Iron 79-91 heme oxygenase 1 Homo sapiens 0-16 20704546-1 2010 Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron. Iron 79-91 heme oxygenase 1 Homo sapiens 18-22 20704548-3 2010 HO-1 catalyzes the degradation of free cellular heme to iron, carbon monoxide (CO) and biliverdin which is eventually converted to bilirubin by biliverdin reductase. Iron 56-60 heme oxygenase 1 Homo sapiens 0-4 20704549-1 2010 Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection. Iron 75-79 heme oxygenase 1 Homo sapiens 0-16 20704549-1 2010 Heme oxygenase-1 (HO-1), an enzyme degrading heme to carbon monoxide, free iron, and biliverdin, participates in the cell defence against oxidative stress and it has been speculated that it might be a new therapeutic target for neuroprotection. Iron 75-79 heme oxygenase 1 Homo sapiens 18-22 20704550-1 2010 Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron. Iron 91-95 heme oxygenase 1 Homo sapiens 0-16 21383490-4 2010 HO-1 breaks down heme to yield CO, iron and biliverdin. Iron 35-39 heme oxygenase 1 Homo sapiens 0-4 20713168-4 2010 Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin. Iron 98-102 heme oxygenase 1 Homo sapiens 0-16 20713168-4 2010 Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin. Iron 98-102 heme oxygenase 1 Homo sapiens 18-22 20868356-4 2010 HO-1 is the enzyme responsible for the conversion of the heme group to billiverdin, carbon monoxide and iron; a highly regulated cytoprotective enzyme able to respond to numerous chemical or physical stressors, many of which decrease oxygen availability and generate oxidative stress. Iron 104-108 heme oxygenase 1 Homo sapiens 0-4 20704550-1 2010 Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron. Iron 91-95 heme oxygenase 1 Homo sapiens 18-22 20704552-4 2010 HO-1 degrades heme to biliverdin-IXalpha, carbon monoxide (CO), and iron. Iron 68-72 heme oxygenase 1 Homo sapiens 0-4 20730621-8 2010 The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1). Iron 105-107 heme oxygenase 1 Homo sapiens 459-463 20730621-8 2010 The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1). Iron 99-103 heme oxygenase 1 Homo sapiens 459-463 20730621-8 2010 The increased level of oxidative stress in AD brain is reflected by the increased brain content of iron (Fe) and copper (Cu) both capable of stimulating free radical formation (e.g. hydroxyl radicals via Fenton reaction), increased protein and DNA oxidation in the AD brain, enhanced lipid peroxidation, decreased level of cytochrome c oxidase and advanced glycation end products (AGEs), carbonyls, malondialdehyde (MDA), peroxynitrite, and heme oxygenase-1 (HO-1). Iron 105-107 heme oxygenase 1 Homo sapiens 441-457 20732302-8 2010 Loss of HO-1 activity may result in increased oxidative neurotoxicity, anemia, growth retardation and iron deposition. Iron 102-106 heme oxygenase 1 Homo sapiens 8-12 20679134-1 2010 Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV). Iron 128-132 heme oxygenase 1 Homo sapiens 0-16 20679134-1 2010 Heme oxygenase 1 (HO-1) uses molecular oxygen and electrons from NADPH cytochrome P450 reductase to convert heme to CO, ferrous iron, and biliverdin (BV). Iron 128-132 heme oxygenase 1 Homo sapiens 18-22 20679134-4 2010 The goal of this study was to determine whether HO-1 activity could be monitored directly by following BV generation or iron release (using the ferrous iron chelator, ferrozine) in the absence of BVR. Iron 120-124 heme oxygenase 1 Homo sapiens 48-52 20819190-1 2010 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin. Iron 93-97 heme oxygenase 1 Homo sapiens 0-16 20819190-1 2010 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism that converts heme to Fe++, carbon monoxide and biliverdin. Iron 93-97 heme oxygenase 1 Homo sapiens 18-22 20709802-0 2010 Adiponectin-mediated heme oxygenase-1 induction protects against iron-induced liver injury via a PPARalpha dependent mechanism. Iron 65-69 heme oxygenase 1 Homo sapiens 21-37 20709802-2 2010 Herein, we show that the deleterious effects of iron dextran on liver function and iron deposition were significantly reversed by adiponectin gene therapy, which was accompanied by AMP-activated protein kinase (AMPK) phosphorylation and heme oxygenase (HO)-1 induction. Iron 48-52 heme oxygenase 1 Homo sapiens 237-258 20580464-3 2010 A different iron metabolism gene signature was detected in both macrophage types, with the heme regulatory molecules CD163 and Heme Oxygenase-1 (HO-1) being preferentially expressed by M2 (M-CSF) macrophages. Iron 12-16 heme oxygenase 1 Homo sapiens 145-149 20822529-3 2010 Deleterious free heme is degraded by HO-1 to carbon monoxide, iron and biliverdin, which have potent anti-oxidant and anti-inflammatory properties. Iron 62-66 heme oxygenase 1 Homo sapiens 37-41 20504881-0 2010 Parenteral iron formulations differentially affect MCP-1, HO-1, and NGAL gene expression and renal responses to injury. Iron 11-15 heme oxygenase 1 Homo sapiens 58-62 20832528-1 2010 BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron. Iron 115-119 heme oxygenase 1 Homo sapiens 12-28 20832528-1 2010 BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron. Iron 115-119 heme oxygenase 1 Homo sapiens 30-34 20689484-1 2010 OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe). Iron 135-139 heme oxygenase 1 Homo sapiens 12-28 20689484-1 2010 OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe). Iron 135-139 heme oxygenase 1 Homo sapiens 30-34 20689484-1 2010 OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe). Iron 141-143 heme oxygenase 1 Homo sapiens 12-28 20689484-1 2010 OBJECTIVES: Heme oxygenase 1 (HO-1) is rapidly induced by stress, degrading pro-oxidant heme into carbon monoxide, bilirubin, and free iron (Fe). Iron 141-143 heme oxygenase 1 Homo sapiens 30-34 20504881-12 2010 We conclude that 1) parenteral iron formulations that stimulate redox signaling can evoke cyto/nephrotoxicity; 2) secondary adaptive responses to this injury (e.g., HO-1/NGAL induction) can initiate a renal tubular cytoresistant state; this suggests a potential new clinical application for intravenous Fe therapy; and 3) FMX is bioneutral regarding these responses. Iron 31-35 heme oxygenase 1 Homo sapiens 165-169 20676377-2 2010 However, HO-1 protein levels are increased in dopaminergic neurons of Parkinson"s disease (PD) patients, suggesting its participation in free-iron deposition, oxidative stress and neurotoxicity. Iron 142-146 heme oxygenase 1 Homo sapiens 9-13 20336713-6 2010 The attenuation of iron-induced augmentation of heme oxygenase-1 was also confirmed in HepG2 cells expressing the core protein. Iron 19-23 heme oxygenase 1 Homo sapiens 48-64 20378668-7 2010 The transcriptional up-regulation of HO1 in plants responds to many agents, such as light, UV, iron deprivation, reactive oxygen species (ROS), abscisic acid (ABA), and haematin. Iron 95-99 heme oxygenase 1 Homo sapiens 37-40 20518085-1 2010 Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron. Iron 116-120 heme oxygenase 1 Homo sapiens 0-16 20518085-1 2010 Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron. Iron 116-120 heme oxygenase 1 Homo sapiens 18-22 20118244-1 2010 Heme oxygenases (HOs) -1 and -2 catalyze the breakdown of heme to release carbon monoxide, biliverdin, and ferrous iron, which may preserve cell function during oxidative stress. Iron 115-119 heme oxygenase 1 Homo sapiens 0-31 20223678-9 2010 This is supported by the fact that during PDT ferritin is readily up-regulated, able to bind excess iron formed by the HO-1 action. Iron 100-104 heme oxygenase 1 Homo sapiens 119-123 20333281-4 2010 Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites. Iron 82-86 heme oxygenase 1 Homo sapiens 0-16 20020468-6 2010 Furthermore, downstream products of HO-1, bilirubin, carbon monoxide, and iron, are involved in the inhibitory action of HO-1. Iron 74-78 heme oxygenase 1 Homo sapiens 121-125 20333281-4 2010 Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites. Iron 82-86 heme oxygenase 1 Homo sapiens 18-22 20333281-4 2010 Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites. Iron 149-153 heme oxygenase 1 Homo sapiens 0-16 20333281-4 2010 Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites. Iron 149-153 heme oxygenase 1 Homo sapiens 18-22 19961840-2 2010 To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron. Iron 258-262 heme oxygenase 1 Homo sapiens 122-138 19961840-2 2010 To delineate the underlying molecular mechanisms, we recently found that Rhizoma Chuanxiong extract significantly induced heme oxygenase-1 (HO-1), an enzyme that degrades intracellular heme into three bioactive products: biliverdin, carbon monoxide and free iron. Iron 258-262 heme oxygenase 1 Homo sapiens 140-144 19925812-1 2010 Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin. Iron 147-151 heme oxygenase 1 Homo sapiens 0-16 19925812-1 2010 Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin. Iron 147-151 heme oxygenase 1 Homo sapiens 18-22 19874266-2 2009 Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide. Iron 93-97 heme oxygenase 1 Homo sapiens 0-16 19954435-8 2010 The inhibitor binds to the human heme oxygenase-1 distal pocket through the coordination of heme iron by the N4 in the triazole moiety, whereas the phenyl group is stabilized by hydrophobic interactions from residues within the binding pocket. Iron 97-101 heme oxygenase 1 Homo sapiens 33-49 19874266-5 2009 Induction of the astroglial ho-1 gene may constitute a "common pathway" leading to pathological brain iron deposition, intracellular oxidative damage and bioenergetic failure in AD and other human CNS disorders. Iron 102-106 heme oxygenase 1 Homo sapiens 28-32 19874266-2 2009 Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide. Iron 93-97 heme oxygenase 1 Homo sapiens 18-22 18774956-1 2009 Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism. Iron 40-44 heme oxygenase 1 Homo sapiens 0-16 19777608-0 2009 Iron increases HMOX1 and decreases hepatitis C viral expression in HCV-expressing cells. Iron 0-4 heme oxygenase 1 Homo sapiens 15-20 19777608-4 2009 RESULTS: Iron, in the form of ferric nitrilotriacetate, increased oxidative stress and up-regulated HMOX1 gene expression. Iron 9-13 heme oxygenase 1 Homo sapiens 100-105 19777608-9 2009 CONCLUSION: Excess iron up-regulates HMOX1 and down-regulates HCV gene expression in hepatoma cells. Iron 19-23 heme oxygenase 1 Homo sapiens 37-42 19694439-2 2009 In humans, heme oxygenase-1 (hHO-1) is overexpressed in tumor tissues, where it helps to protect cancer cells from anticancer agents, while HOs in fungal pathogens, such as Candida albicans, function as the primary means of iron acquisition. Iron 224-228 heme oxygenase 1 Homo sapiens 11-27 19694439-2 2009 In humans, heme oxygenase-1 (hHO-1) is overexpressed in tumor tissues, where it helps to protect cancer cells from anticancer agents, while HOs in fungal pathogens, such as Candida albicans, function as the primary means of iron acquisition. Iron 224-228 heme oxygenase 1 Homo sapiens 29-34 18774956-1 2009 Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism. Iron 40-44 heme oxygenase 1 Homo sapiens 18-22 18774956-1 2009 Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism. Iron 101-105 heme oxygenase 1 Homo sapiens 0-16 18774956-1 2009 Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism. Iron 101-105 heme oxygenase 1 Homo sapiens 18-22 18774956-1 2009 Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism. Iron 101-105 heme oxygenase 1 Homo sapiens 0-16 18774956-1 2009 Heme oxygenase-1 (HO-1) contribution to iron homeostasis has been postulated, because it facilitates iron recycling by liberating iron mostly from heme catabolism. Iron 101-105 heme oxygenase 1 Homo sapiens 18-22 18774956-4 2009 Here we postulated that HO-1 is critical in the regulation of ferroportin, the major cellular iron exporter, and hepcidin, the key regulator of iron homeostasis central in the pathogenesis of anemia of inflammation. Iron 94-98 heme oxygenase 1 Homo sapiens 24-28 18774956-4 2009 Here we postulated that HO-1 is critical in the regulation of ferroportin, the major cellular iron exporter, and hepcidin, the key regulator of iron homeostasis central in the pathogenesis of anemia of inflammation. Iron 144-148 heme oxygenase 1 Homo sapiens 24-28 18774956-5 2009 Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling. Iron 79-83 heme oxygenase 1 Homo sapiens 66-70 18774956-5 2009 Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling. Iron 79-83 heme oxygenase 1 Homo sapiens 153-157 18774956-5 2009 Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling. Iron 161-165 heme oxygenase 1 Homo sapiens 66-70 18774956-5 2009 Our current experiments in human THP-1 monocytic cells indicate a HO-1-induced iron-mediated surface-ferroportin expression, consistent with the role of HO-1 in iron recycling. Iron 161-165 heme oxygenase 1 Homo sapiens 153-157 18774956-12 2009 This study therefore shows a crucial role for HO-1 in maintaining body iron balance. Iron 71-75 heme oxygenase 1 Homo sapiens 46-50 19727608-3 2009 One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide. Iron 185-189 heme oxygenase 1 Homo sapiens 57-73 19727608-3 2009 One of the key components of cellular stress response is heme oxygenase-1 (HO-1), the rate limiting enzyme in the process of degrading potentially toxic free heme into biliverdin, free iron and carbon monoxide. Iron 185-189 heme oxygenase 1 Homo sapiens 75-79 18619522-8 2009 Heme oxygenase 1 (HO1) is an important component of the system for mobilization of iron from macrophages. Iron 83-87 heme oxygenase 1 Homo sapiens 0-16 18619522-8 2009 Heme oxygenase 1 (HO1) is an important component of the system for mobilization of iron from macrophages. Iron 83-87 heme oxygenase 1 Homo sapiens 18-21 19362144-3 2009 HO-1 serves a vital metabolic function as the rate-limiting step in the heme degradation pathway and in the maintenance of iron homeostasis. Iron 123-127 heme oxygenase 1 Homo sapiens 0-4 19362144-5 2009 The cytoprotective functions of HO-1 may be attributed to heme turnover, as well as to beneficial properties of its enzymatic reaction products: biliverdin-IXalpha, iron, and carbon monoxide (CO). Iron 165-169 heme oxygenase 1 Homo sapiens 32-36 19457084-3 2009 Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors. Iron 62-66 heme oxygenase 1 Homo sapiens 0-16 19457084-3 2009 Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors. Iron 62-66 heme oxygenase 1 Homo sapiens 18-22 19457084-7 2009 Likewise, treatment of HO-1 over-expressing cells with the HO-1 inhibitor, tin mesoporphyrin, the iron chelator deferoxamine or antagonist of CO-dependent cGMP activation, methylene blue, mitigated the HO-1-induced reduction in alpha-synuclein levels. Iron 98-102 heme oxygenase 1 Homo sapiens 23-27 19457088-8 2009 In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure amply documented in Alzheimer disease, Parkinson disease and other aging-related neurodegenerative disorders. Iron 100-104 heme oxygenase 1 Homo sapiens 25-29 19508729-14 2009 The metabolites biliverdin and iron seem to be involved in HO-1-mediated resistance to anticancer treatment. Iron 31-35 heme oxygenase 1 Homo sapiens 59-63 19457088-8 2009 In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial sequestration of non-transferrin iron and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure amply documented in Alzheimer disease, Parkinson disease and other aging-related neurodegenerative disorders. Iron 171-175 heme oxygenase 1 Homo sapiens 25-29 19475336-3 2009 Therefore, it is tempting that the iron-releasing key enzyme in heme catabolism, heme oxygenase-1 (HO-1), may represent a candidate for a genetic susceptibility to PD. Iron 35-39 heme oxygenase 1 Homo sapiens 81-97 19475336-3 2009 Therefore, it is tempting that the iron-releasing key enzyme in heme catabolism, heme oxygenase-1 (HO-1), may represent a candidate for a genetic susceptibility to PD. Iron 35-39 heme oxygenase 1 Homo sapiens 99-103 19039664-2 2009 Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron. Iron 114-118 heme oxygenase 1 Homo sapiens 71-87 19039664-2 2009 Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron. Iron 114-118 heme oxygenase 1 Homo sapiens 89-94 19039664-2 2009 Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron. Iron 168-172 heme oxygenase 1 Homo sapiens 71-87 19039664-2 2009 Heme uptake via endocytosis of heme-HPX followed by heme catabolism by heme oxygenase-1 (HMOX1) raises regulatory iron pools, thus linking heme metabolism with that of iron. Iron 168-172 heme oxygenase 1 Homo sapiens 89-94 19250338-6 2009 Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways. Iron 92-96 heme oxygenase 1 Homo sapiens 6-10 19251588-9 2009 In contrast, heme oxygenase-1 was strongly suppressed by DFO, both in the absence and presence of LPS or iron. Iron 105-109 heme oxygenase 1 Homo sapiens 13-29 19250338-6 2009 Thus, HO-1 activity promotes mitochondrial macroautophagy and sequestration of redox-active iron in astroglia independently of classical iron mobilization pathways. Iron 137-141 heme oxygenase 1 Homo sapiens 6-10 19250338-0 2009 HO-1-mediated macroautophagy: a mechanism for unregulated iron deposition in aging and degenerating neural tissues. Iron 58-62 heme oxygenase 1 Homo sapiens 0-4 19250338-2 2009 We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria. Iron 140-144 heme oxygenase 1 Homo sapiens 32-48 19250338-7 2009 Glial HO-1 may be a rational therapeutic target in AD, PD, and other human CNS conditions characterized by the unregulated deposition of brain iron. Iron 143-147 heme oxygenase 1 Homo sapiens 6-10 19250338-2 2009 We previously demonstrated that heme oxygenase-1 (HO-1) is up-regulated in AD and PD brain and promotes the accumulation of non-transferrin iron in astroglial mitochondria. Iron 140-144 heme oxygenase 1 Homo sapiens 50-54 19250338-5 2009 HO-1 promoted trapping of redox-active iron and sulfur within many cytopathological profiles without impacting ferroportin, transferrin receptor, ferritin, and IRP2 protein levels or IRP1 activity. Iron 39-43 heme oxygenase 1 Homo sapiens 0-4 19136476-0 2009 15-Deoxy-Delta12,14-prostaglandin J2 upregulates the expression of heme oxygenase-1 and subsequently matrix metalloproteinase-1 in human breast cancer cells: possible roles of iron and ROS. Iron 176-180 heme oxygenase 1 Homo sapiens 67-127 19136476-9 2009 We hypothesize that excess iron, released as a consequence HO-1 activity induced by 15d-PGJ2, is transiently available for the stimulation of intracellular ROS generation and subsequently MMP-1 expression. Iron 27-31 heme oxygenase 1 Homo sapiens 59-63 18528644-10 2008 Heme oxygenase 1 expression increased and DMT1 expression decreased with higher heme Fe concentrations in the media. Iron 85-87 heme oxygenase 1 Homo sapiens 0-16 20107533-1 2009 Heme oxygenase (HO)-1 is an inducible enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of free heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV), the latter being subsequently converted into bilirubin (BR). Iron 140-152 heme oxygenase 1 Homo sapiens 0-21 19123922-1 2009 Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR). Iron 109-113 heme oxygenase 1 Homo sapiens 0-16 19123922-1 2009 Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR). Iron 109-113 heme oxygenase 1 Homo sapiens 18-22 19123922-1 2009 Heme oxygenase-1 (HO-1) catalyzes the oxidative degradation of heme to biliverdin, carbon monoxide, and free iron in a reaction requiring the interaction of HO-1 with NADPH-cytochrome P450 reductase (CPR). Iron 109-113 heme oxygenase 1 Homo sapiens 157-161 18799798-1 2008 Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin. Iron 147-151 heme oxygenase 1 Homo sapiens 0-16 18799798-1 2008 Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron, and bilirubin. Iron 147-151 heme oxygenase 1 Homo sapiens 18-22 19135260-0 2009 Covalent heme attachment to the protein in human heme oxygenase-1 with selenocysteine replacing the His25 proximal iron ligand. Iron 115-119 heme oxygenase 1 Homo sapiens 49-65 19036700-1 2009 Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe). Iron 99-103 heme oxygenase 1 Homo sapiens 27-43 19036700-1 2009 Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe). Iron 99-103 heme oxygenase 1 Homo sapiens 45-49 19036700-1 2009 Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe). Iron 105-107 heme oxygenase 1 Homo sapiens 27-43 19036700-1 2009 Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe). Iron 105-107 heme oxygenase 1 Homo sapiens 45-49 19162549-1 2009 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase). Iron 103-107 heme oxygenase 1 Homo sapiens 0-16 19162549-1 2009 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase). Iron 103-107 heme oxygenase 1 Homo sapiens 18-22 19162549-1 2009 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase). Iron 166-170 heme oxygenase 1 Homo sapiens 0-16 19162549-1 2009 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that catabolizes free heme into carbon monoxide, iron (which induces the expression of heavy-chain ferritin, an iron-sequestering protein) and biliverdin (which is converted to bilirubin by biliverdin reductase). Iron 166-170 heme oxygenase 1 Homo sapiens 18-22 19046352-3 2009 In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia. Iron 91-95 heme oxygenase 1 Homo sapiens 51-55 18769232-1 2008 PURPOSE OF REVIEW: Heme oxygenase-1 apart from converting heme to carbon monoxide, iron and biliverdin has been shown to exert anti-inflammatory, antiapoptotic and antioxidant actions. Iron 83-87 heme oxygenase 1 Homo sapiens 19-35 18576916-1 2008 Heme oxygenase-1, an enzyme degrading heme to carbon monoxide, iron, and biliverdin, has been recognized as playing a crucial role in cellular defense against stressful conditions, not only related to heme release. Iron 63-67 heme oxygenase 1 Homo sapiens 0-16 18289069-3 2008 The precise underlying mechanisms for HO-1-based protection are not yet completely understood, but appear to involve the protective effects of HO-1 by-products, carbon monoxide (CO), biliverdin/bilirubin and free iron. Iron 213-217 heme oxygenase 1 Homo sapiens 38-42 18786476-1 2008 Hemoxygenase (HO)-1 is an inducible isoform of the first and rate-controlling enzyme of the degradation of heme into iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin. Iron 117-121 heme oxygenase 1 Homo sapiens 0-19 18487208-2 2008 Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron. Iron 115-119 heme oxygenase 1 Homo sapiens 6-22 18487208-2 2008 Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron. Iron 115-119 heme oxygenase 1 Homo sapiens 24-29 18371544-3 2008 HO-1, an integral component of an important cytoprotective mechanism, mediates its action through removal of heme, the generation of heme breakdown reaction products (biliverdin, free iron, and carbon monoxide), and modulation of key cellular molecules. Iron 184-188 heme oxygenase 1 Homo sapiens 0-4 18443197-3 2008 The aim of this study was to assess the association of the length of (GT)(n) repeats in the HO-1 gene promoter with serum bilirubin, markers of iron status, and the development of coronary artery disease (CAD). Iron 144-148 heme oxygenase 1 Homo sapiens 92-96 18174022-4 2008 Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites. Iron 41-45 heme oxygenase 1 Homo sapiens 0-16 18174022-4 2008 Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites. Iron 41-45 heme oxygenase 1 Homo sapiens 18-22 18174022-4 2008 Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites. Iron 103-107 heme oxygenase 1 Homo sapiens 0-16 18174022-4 2008 Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites. Iron 103-107 heme oxygenase 1 Homo sapiens 18-22 18174022-4 2008 Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites. Iron 103-107 heme oxygenase 1 Homo sapiens 0-16 18174022-4 2008 Heme oxygenase-1 (HO-1) is important for iron homeostasis via catalysis of heme degradation to release iron, carbon monoxide and biliverdin/bilirubin, and may influence iron supply to the intra-erythrocyte falciparum parasites. Iron 103-107 heme oxygenase 1 Homo sapiens 18-22 18216035-10 2008 CONCLUSIONS: The haemoglobin-HO-1 system may be required to ensure adequate regulation of the bioavailability of haeme, iron and oxygen in human endometrium. Iron 120-124 heme oxygenase 1 Homo sapiens 29-33 18289070-1 2008 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron. Iron 107-111 heme oxygenase 1 Homo sapiens 0-16 18289070-1 2008 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to generate carbon monoxide, biliverdin and free iron. Iron 107-111 heme oxygenase 1 Homo sapiens 18-22 18289070-4 2008 However, experimental observations indicate that the extent of HO-1 induction may be critical because excessive heme degradation may result in toxic levels of CO, bilirubin and, more importantly, iron. Iron 196-200 heme oxygenase 1 Homo sapiens 63-67 18289074-1 2008 Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. Iron 110-114 heme oxygenase 1 Homo sapiens 0-16 18289074-1 2008 Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. Iron 110-114 heme oxygenase 1 Homo sapiens 18-22 17919067-2 2007 The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron. Iron 192-196 heme oxygenase 1 Homo sapiens 39-55 17822372-1 2007 Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron. Iron 127-139 heme oxygenase 1 Homo sapiens 0-16 17822372-1 2007 Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron. Iron 127-139 heme oxygenase 1 Homo sapiens 18-22 17919067-2 2007 The inducible form of these enzymes is heme oxygenase-1 (HO-1), which is the rate-limiting enzyme that can degrade heme into equimolar quantities of carbon monoxide (CO), biliverdin, and free iron. Iron 192-196 heme oxygenase 1 Homo sapiens 57-61 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Iron 148-152 heme oxygenase 1 Homo sapiens 88-104 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Iron 148-152 heme oxygenase 1 Homo sapiens 106-110 17726138-0 2007 Genetic variability in iron-related oxidative stress pathways (Nrf2, NQ01, NOS3, and HO-1), iron intake, and risk of postmenopausal breast cancer. Iron 23-27 heme oxygenase 1 Homo sapiens 85-89 17991645-0 2007 Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with iron status in persons with type 2 diabetes mellitus. Iron 85-89 heme oxygenase 1 Homo sapiens 35-51 17991645-3 2007 Heme oxygenase (HO) 1 expression is increased when intracellular iron increases. Iron 65-69 heme oxygenase 1 Homo sapiens 0-21 18044280-1 2007 INTRODUCTION: Heme-Oxygenase-1 catalyzes hemoglobin into bilirubin, iron, and carbon monoxide, a well known vasodilator. Iron 68-72 heme oxygenase 1 Homo sapiens 14-30 17915953-2 2007 In the process of heme degradation, HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase (CPR), releasing free iron and carbon monoxide. Iron 164-168 heme oxygenase 1 Homo sapiens 36-40 17408452-8 2007 HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide. Iron 142-146 heme oxygenase 1 Homo sapiens 14-18 17569621-7 2007 Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1). Iron 171-175 heme oxygenase 1 Homo sapiens 28-32 17569621-7 2007 Upon organ transplantation, HO-1 is ubiquitously expressed in a transplanted organ, becoming the rate-limiting enzyme in the catabolism of heme into carbon monoxide (CO), iron (Fe) and biliverdin (1). Iron 177-179 heme oxygenase 1 Homo sapiens 28-32 17095152-11 2007 Based on these results, we conclude that HO-1 plays a major role in mediating cytoprotection and iron homeostasis against NO toxicity in immortalized and malignant oral keratinocytes. Iron 97-101 heme oxygenase 1 Homo sapiens 41-45 16980551-2 2007 HO-1 catalyzes the degradation of heme, a potent oxidant, into biliverdin, iron, and carbon monoxide (CO). Iron 75-79 heme oxygenase 1 Homo sapiens 0-4 16990612-3 2007 One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron). Iron 279-283 heme oxygenase 1 Homo sapiens 54-70 16495208-1 2006 Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin. Iron 118-122 heme oxygenase 1 Homo sapiens 61-77 16990612-3 2007 One protein providing such cytoprotective activity is heme oxygenase-1 (HO-1), an enzyme that catalyzes the rate-limiting reaction in heme catabolism (i.e., the oxidative cleavage of b-type heme molecules to yield equimolar quantities of biliverdin IXalpha, carbon monoxide, and iron). Iron 279-283 heme oxygenase 1 Homo sapiens 72-76 17095719-4 2007 Three genes involved in iron-heme homeostasis, CD163, HO-1, and transferrin receptor, were further analyzed in 40 independent plaques. Iron 24-28 heme oxygenase 1 Homo sapiens 54-84 17095719-6 2007 The expression of HO-1 and CD163 correlated with tissue iron content but iron itself was not associated with the symptom status. Iron 56-60 heme oxygenase 1 Homo sapiens 18-22 16950787-7 2006 Because we observed notably high levels of phosphorylated protein kinase C alpha and its suppression by EGCG and deferoxamine (an iron chelator), a possible mechanism involving phosphorylated protein kinase C alpha and iron in Nrf2-HO-1 activation was further investigated. Iron 130-134 heme oxygenase 1 Homo sapiens 232-236 16959797-1 2006 Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO. Iron 55-59 heme oxygenase 1 Homo sapiens 0-16 16959797-1 2006 Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO. Iron 55-59 heme oxygenase 1 Homo sapiens 18-22 17018578-1 2007 Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic. Iron 72-76 heme oxygenase 1 Homo sapiens 0-16 17018578-1 2007 Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic. Iron 72-76 heme oxygenase 1 Homo sapiens 18-21 17168739-5 2006 Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1). Iron 115-119 heme oxygenase 1 Homo sapiens 240-256 17168739-5 2006 Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1). Iron 115-119 heme oxygenase 1 Homo sapiens 258-262 17168739-5 2006 Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1). Iron 202-206 heme oxygenase 1 Homo sapiens 240-256 17168739-5 2006 Concurrently, the hypoxia-inducible factor (HIF) has also been shown in previous studies to regulate intracellular iron by binding to HIF-responsive elements (HREs) that are located within the genes of iron-related proteins such as TfR and heme oxygenase-1 (HO-1). Iron 202-206 heme oxygenase 1 Homo sapiens 258-262 16950787-7 2006 Because we observed notably high levels of phosphorylated protein kinase C alpha and its suppression by EGCG and deferoxamine (an iron chelator), a possible mechanism involving phosphorylated protein kinase C alpha and iron in Nrf2-HO-1 activation was further investigated. Iron 219-223 heme oxygenase 1 Homo sapiens 232-236 17042977-2 2006 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide. Iron 110-114 heme oxygenase 1 Homo sapiens 0-16 17042977-2 2006 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in the catabolism of heme into biliverdin, releasing free iron and carbon monoxide. Iron 110-114 heme oxygenase 1 Homo sapiens 18-22 16787441-2 2006 Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide. Iron 152-156 heme oxygenase 1 Homo sapiens 62-78 16495208-1 2006 Heme is a strong inducer and substrate of the stress protein heme oxygenase-1 (HO-1), which produces carbon monoxide, iron, and bilirubin. Iron 118-122 heme oxygenase 1 Homo sapiens 79-83 16631522-7 2006 Intracellular free iron determined with the fluorescent probe calcein rose to approximately 160% of the control level 6 h after SPNO, but declined to approximately 70% after 24 h. Immunoblot analyses revealed a rapid early (approximately 2 h post-NO) increase in heme oxygenase-1 level, followed by a gradual (4-20 h post-NO) increase in ferritin. Iron 19-23 heme oxygenase 1 Homo sapiens 263-279 16476785-4 2006 (p. 1633) demonstrate that the effects of SNP on expression of HO-1 are mainly due to free iron released from SNP in aqueous solution, whereas NO plays a negligible role, if any, as the mediator of response to SNP. Iron 91-95 heme oxygenase 1 Homo sapiens 63-67 16476785-5 2006 Downstream effects of iron, after being dissociated from SNP, include increases in intracellular cAMP that are causally linked to subsequent phosphorylation of specific MAPK targets and enhanced HO-1 protein levels. Iron 22-26 heme oxygenase 1 Homo sapiens 195-199 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Iron 262-266 heme oxygenase 1 Homo sapiens 75-79 16545694-1 2006 BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin. Iron 139-143 heme oxygenase 1 Homo sapiens 95-111 16545694-1 2006 BACKGROUND: Skin injury leads to the release of heme, a potent prooxidant which is degraded by heme oxygenase-1 (HO-1) to carbon monoxide, iron, and biliverdin, subsequently reduced to bilirubin. Iron 139-143 heme oxygenase 1 Homo sapiens 113-117 16629181-7 2006 These results suggested that heme oxygenase-1 mediates heme iron influx and efflux in intestinal cells. Iron 60-64 heme oxygenase 1 Homo sapiens 29-45 16222706-2 2006 Up-regulation of HO-1 in rat astroglia has been shown to facilitate iron sequestration by the mitochondrial compartment. Iron 68-72 heme oxygenase 1 Homo sapiens 17-21 16222706-9 2006 Glial HO-1 hyperactivity may contribute to cellular oxidative stress, pathological iron deposition, and bioenergetic failure characteristic of degenerating and inflamed neural tissues and may constitute a rational target for therapeutic intervention in these conditions. Iron 83-87 heme oxygenase 1 Homo sapiens 6-10 16386335-10 2006 The synaptosomes isolated from gerbil pre-injected with FAEE and subsequently treated with AAPH or Fe(2+)/H(2)O(2) showed induction of heme oxygenase (HO-1) and heat shock protein 70 (HSP-70) but reduced inducible nitric oxide synthase (iNOS) levels. Iron 99-101 heme oxygenase 1 Homo sapiens 151-155 16137675-3 2006 Biodegradation of extravasated hemoglobin (exvHb) and deposition of iron in alveoli occurred at 3-56 h post-exposure and was preceded by LKC degranulation and accumulation of MPO, HO-1, and SOD-1 in HLs. Iron 68-72 heme oxygenase 1 Homo sapiens 180-184 16461755-1 2006 Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron. Iron 201-205 heme oxygenase 1 Homo sapiens 0-16 16461755-1 2006 Heme oxygenase 1 (HO-1) is induced in response to cellular stress and is responsible for converting the prooxidant heme molecule into equimolar quantities of biliverdin (BV), carbon monoxide (CO), and iron. Iron 201-205 heme oxygenase 1 Homo sapiens 18-22 16629181-0 2006 Heme oxygenase 1 overexpression increases iron fluxes in caco-2 cells. Iron 42-46 heme oxygenase 1 Homo sapiens 0-16 16629181-2 2006 Heme oxygenase-1 participates in the cleavage of the heme ring producing biliverdin, CO and ferrous Fe. Iron 100-102 heme oxygenase 1 Homo sapiens 0-16 16943657-2 2006 HO-1 degradation of heme yields biliverdin, bilirubin, carbon monoxide and iron. Iron 75-79 heme oxygenase 1 Homo sapiens 0-4 16249618-2 2005 Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide. Iron 83-87 heme oxygenase 1 Homo sapiens 0-16 16208635-8 2005 Heme oxygenase-1 is a heme-degrading enzyme that opens the porphyrin ring, producing biliverdin, carbon monoxide, and the most dangerous product - free redox active iron. Iron 165-169 heme oxygenase 1 Homo sapiens 0-16 16249618-2 2005 Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide. Iron 83-87 heme oxygenase 1 Homo sapiens 18-22 15546873-2 2005 Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO). Iron 106-110 heme oxygenase 1 Homo sapiens 0-16 16309585-2 2005 HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Iron 65-69 heme oxygenase 1 Homo sapiens 0-4 15649645-1 2005 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO). Iron 177-181 heme oxygenase 1 Homo sapiens 0-16 15649645-1 2005 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO). Iron 177-181 heme oxygenase 1 Homo sapiens 18-22 15649645-1 2005 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO). Iron 183-185 heme oxygenase 1 Homo sapiens 0-16 15649645-1 2005 Heme oxygenase-1 (HO-1) is a stress-responsive enzyme that acts during inflammatory reactions as the rate-limiting step in the catabolism of heme, yielding equimolar amounts of iron (Fe), biliverdin, and the gas carbon monoxide (CO). Iron 183-185 heme oxygenase 1 Homo sapiens 18-22 15546873-2 2005 Heme oxygenase-1 (HO-1) is a cytoprotective protein that catalyzes the degradation of heme to biliverdin, iron, and carbon monoxide (CO). Iron 106-110 heme oxygenase 1 Homo sapiens 18-22 15589375-1 2005 Heme oxygenases (HO-1 and HO-2) catalyze the NADPH-cytochrome P(450) reductase (CPR)-dependent degradation of heme into iron, carbon monoxide, and biliverdin, which is reduced into bilirubin. Iron 120-124 heme oxygenase 1 Homo sapiens 0-30 15933765-1 2005 Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase. Iron 126-130 heme oxygenase 1 Homo sapiens 0-16 15933765-1 2005 Heme oxygenase-1 (HO-1) is an enzyme which catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide and biliverdin, which is subsequently converted to bilirubin by biliverdin reductase. Iron 126-130 heme oxygenase 1 Homo sapiens 18-22 15659834-5 2004 In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin. Iron 185-189 heme oxygenase 1 Homo sapiens 72-88 15465821-1 2004 Heme oxygenase-1 is an antioxidant defense enzyme that converts heme to biliverdin, iron, and carbon monoxide. Iron 84-88 heme oxygenase 1 Homo sapiens 0-16 15659834-5 2004 In this study, we investigated the effect of cyPGs on the expression of heme oxygenase-1 (HO-1), a ubiquitous stress-responsive enzyme that catalyzes oxidative cleavage of heme to form iron, carbon monoxide, and biliverdin. Iron 185-189 heme oxygenase 1 Homo sapiens 90-94 15231239-4 2004 These findings indicate aberrations in iron homeostasis that, we suspect, arise primarily from heme, since heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in AD, and mitochondria, since mitochondria turnover, mitochondrial DNA, and cytochrome C oxidative activity are all increased in AD. Iron 39-43 heme oxygenase 1 Homo sapiens 107-123 15297453-1 2004 Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron. Iron 104-108 heme oxygenase 1 Homo sapiens 6-22 15297453-1 2004 Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron. Iron 104-108 heme oxygenase 1 Homo sapiens 24-29 15642322-11 2004 Initial upregulation of message for HO-1 occurred a few hours before any upregulation of MnSOD could be detected, suggesting that release of free iron from the degradation of heme by HO-1 may have played a role in the upregulation of the dismutase. Iron 146-150 heme oxygenase 1 Homo sapiens 36-40 15642322-11 2004 Initial upregulation of message for HO-1 occurred a few hours before any upregulation of MnSOD could be detected, suggesting that release of free iron from the degradation of heme by HO-1 may have played a role in the upregulation of the dismutase. Iron 146-150 heme oxygenase 1 Homo sapiens 183-187 15560792-12 2004 A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1. Iron 92-96 heme oxygenase 1 Homo sapiens 28-32 15560792-12 2004 A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1. Iron 92-96 heme oxygenase 1 Homo sapiens 155-159 15560792-12 2004 A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1. Iron 138-142 heme oxygenase 1 Homo sapiens 28-32 15560792-12 2004 A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1. Iron 138-142 heme oxygenase 1 Homo sapiens 155-159 15345147-3 2004 In various models of oxidative tissue injuries, the induction of HO-1 confers protection on tissues from further damages by removing the prooxidant heme, or by virtue of the antioxidative, antiinflammatory, and/or antiapoptotic actions of one or more of the three products, i.e., carbon monoxide, biliverdin IXalpha, and iron by HO reaction. Iron 321-325 heme oxygenase 1 Homo sapiens 65-69 15231239-4 2004 These findings indicate aberrations in iron homeostasis that, we suspect, arise primarily from heme, since heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in AD, and mitochondria, since mitochondria turnover, mitochondrial DNA, and cytochrome C oxidative activity are all increased in AD. Iron 176-180 heme oxygenase 1 Homo sapiens 107-123 15190962-1 2004 OBJECTIVE: We aimed to quantify concentrations of inducible heme oxygenase (HO)-1 in the lungs of patients with acute respiratory distress syndrome (ARDS) and to investigate its role as a source of ferrous iron and as a signaling agent for iron regulation. Iron 206-210 heme oxygenase 1 Homo sapiens 60-81 15233805-3 2004 HO-1 catalyzes heme breakdown to release iron, carbon monoxide, and biliverdin, which is reduced to bilirubin, a potent radical scavenger. Iron 41-45 heme oxygenase 1 Homo sapiens 0-4 15219989-0 2004 Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex. Iron 54-58 heme oxygenase 1 Homo sapiens 71-87 15213303-2 2004 Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects. Iron 67-71 heme oxygenase 1 Homo sapiens 0-16 15213303-2 2004 Heme oxygenase-1 (HO-1), which degrades heme into biliverdin, free iron (Fe(2+)), and carbon monoxide (CO), has also been known to have antiproliferative and antiapoptotic effects. Iron 67-71 heme oxygenase 1 Homo sapiens 18-22 15190962-1 2004 OBJECTIVE: We aimed to quantify concentrations of inducible heme oxygenase (HO)-1 in the lungs of patients with acute respiratory distress syndrome (ARDS) and to investigate its role as a source of ferrous iron and as a signaling agent for iron regulation. Iron 240-244 heme oxygenase 1 Homo sapiens 60-81 15067050-1 2004 Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions. Iron 71-75 heme oxygenase 1 Homo sapiens 0-16 15086901-1 2004 BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme. Iron 114-118 heme oxygenase 1 Homo sapiens 12-28 15086901-1 2004 BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme. Iron 114-118 heme oxygenase 1 Homo sapiens 30-34 15067050-1 2004 Heme oxygenase-1 (HO-1) catabolizes heme into CO, biliverdin, and free iron and serves as a protective enzyme by virtue of its anti-inflammatory, antiapoptotic, and antiproliferative actions. Iron 71-75 heme oxygenase 1 Homo sapiens 18-22 14735461-1 2004 Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo. Iron 135-139 heme oxygenase 1 Homo sapiens 0-16 14977880-1 2004 Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO). Iron 43-47 heme oxygenase 1 Homo sapiens 0-16 14977880-1 2004 Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO). Iron 43-47 heme oxygenase 1 Homo sapiens 18-22 14973545-1 2004 Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models. Iron 139-143 heme oxygenase 1 Homo sapiens 23-39 14973545-1 2004 Elevated expression of heme oxygenase-1 (HO-1), an intracellular enzyme that degrades heme into carbon monoxide (CO), biliverdine and free iron, has anti-inflammatory and antiapoptotic effects in diverse models. Iron 139-143 heme oxygenase 1 Homo sapiens 41-45 14735461-1 2004 Heme oxygenase-1 (HO-1), an inducible enzyme that catalyzes oxidative degradation of heme to form biliverdin, carbon monoxide and free iron, may protect tumor cells against oxidative stress, thus contributing to rapid tumor growth in vivo. Iron 135-139 heme oxygenase 1 Homo sapiens 18-22 15019971-0 2004 Overexpression of heme oxygenase (HO)-1 renders Jurkat T cells resistant to fas-mediated apoptosis: involvement of iron released by HO-1. Iron 115-119 heme oxygenase 1 Homo sapiens 18-39 15019971-0 2004 Overexpression of heme oxygenase (HO)-1 renders Jurkat T cells resistant to fas-mediated apoptosis: involvement of iron released by HO-1. Iron 115-119 heme oxygenase 1 Homo sapiens 132-136 14766239-1 2004 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin. Iron 87-91 heme oxygenase 1 Homo sapiens 0-16 14766239-1 2004 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide (CO), and biliverdin. Iron 87-91 heme oxygenase 1 Homo sapiens 18-22 15105257-0 2004 Heme oxygenase-1: transducer of pathological brain iron sequestration under oxidative stress. Iron 51-55 heme oxygenase 1 Homo sapiens 0-16 15105257-2 2004 Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide. Iron 90-94 heme oxygenase 1 Homo sapiens 0-16 15105257-2 2004 Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that degrades heme to biliverdin, free iron, and carbon monoxide. Iron 90-94 heme oxygenase 1 Homo sapiens 18-22 15105257-4 2004 A model is presented implicating glial HO-1 induction as a "final common pathway" leading to pathological iron sequestration and mitochondrial insufficiency in a host of human CNS disorders. Iron 106-110 heme oxygenase 1 Homo sapiens 39-43 13678532-2 2003 Heme oxygenase (HO) is a microsomal enzyme that catalyzes the degradation of heme into biliverdin, which is subsequently reduced to bilirubin, free iron, and carbon monoxide, and induction of HO-1 is potentially associated with cellular protection, especially against oxidative insults. Iron 148-152 heme oxygenase 1 Homo sapiens 192-196 15777021-6 2004 The existence of a constitutive haem oxygenase (HO-2), mainly present in the vasculature and nervous system, and an inducible haem oxygenase (HO-1), which is highly expressed during stress conditions in all tissues, also suggests that cells have evolved a fine control of this enzymic pathway to ultimately regulate haem consumption and to ensure production of CO, biliverdin/bilirubin and iron during physiological and pathophysiological situations. Iron 390-394 heme oxygenase 1 Homo sapiens 142-146 14968347-8 2004 HO-1 induction subsequently led to a marked increase in protein expression of a second antioxidant protein, ferritin, via the HO-1-dependent release of free iron from endogenous heme sources (Figures 1 and 5). Iron 157-161 heme oxygenase 1 Homo sapiens 0-4 14968347-8 2004 HO-1 induction subsequently led to a marked increase in protein expression of a second antioxidant protein, ferritin, via the HO-1-dependent release of free iron from endogenous heme sources (Figures 1 and 5). Iron 157-161 heme oxygenase 1 Homo sapiens 126-130 14960194-1 2004 INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron. Iron 159-163 heme oxygenase 1 Homo sapiens 14-30 14960194-1 2004 INTRODUCTION: Heme oxygenase-1 (HO-1) is a stress response enzyme, which catalyses the breakdown of heme into biliverdin-IX alpha, carbon monoxide and ferrous iron. Iron 159-163 heme oxygenase 1 Homo sapiens 32-36 14683741-1 2004 AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO). Iron 111-115 heme oxygenase 1 Homo sapiens 6-22 14683741-1 2004 AIMS: Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation, leading to the generation of free iron, biliverdin, and carbon monoxide (CO). Iron 111-115 heme oxygenase 1 Homo sapiens 24-28 14504288-3 2003 The small Maf proteins appear to be critical regulators of heme oxygenase (HO)-1, an anti-oxidant defense enzyme that degrades heme into iron, carbon monoxide, and biliverdin. Iron 137-141 heme oxygenase 1 Homo sapiens 59-80 12907459-8 2003 Comparative Northern analyses of iron-related genes after erythrophagocytosis revealed a 16-fold increase in FPN1 levels after 3 hours, a 10-fold increase in heme oxygenase-1 (HO-1) after 3 hours, a 2-fold increase in natural resistance macrophage-associated protein 1 (Nramp1) levels after 6 hours, but no change in divalent metal ion transporter 1 (DMT1) levels. Iron 33-37 heme oxygenase 1 Homo sapiens 158-174 14562166-1 2003 INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). Iron 98-102 heme oxygenase 1 Homo sapiens 44-48 12783778-1 2003 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Iron 88-92 heme oxygenase 1 Homo sapiens 0-16 12783778-1 2003 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Iron 88-92 heme oxygenase 1 Homo sapiens 18-22 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Iron 153-157 heme oxygenase 1 Homo sapiens 69-85 12909459-1 2003 Heme oxygenase (HO)-1 catabolizes heme into three products: carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin) and free iron (which leads to the induction of ferritin, an iron-binding protein). Iron 144-148 heme oxygenase 1 Homo sapiens 0-21 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Iron 153-157 heme oxygenase 1 Homo sapiens 87-91 12585963-4 2003 Either N-acetylcysteine, an antioxidant, or deferoxamine, an iron chelator, resulted in a dose-dependent inhibition of HO-1 mRNA and protein induction during glucose deprivation, suggesting a redox- and iron-dependent mechanism. Iron 203-207 heme oxygenase 1 Homo sapiens 119-123 12622689-1 2003 NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin. Iron 116-120 heme oxygenase 1 Homo sapiens 34-50 12622689-1 2003 NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin. Iron 116-120 heme oxygenase 1 Homo sapiens 52-56 12626517-1 2003 Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron. Iron 133-137 heme oxygenase 1 Homo sapiens 6-22 12626517-1 2003 Human heme oxygenase-1 (hHO-1) catalyzes the NADPH-cytochrome P450 reductase-dependent oxidation of heme to biliverdin, CO, and free iron. Iron 133-137 heme oxygenase 1 Homo sapiens 24-29 12585963-2 2003 One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin. Iron 145-149 heme oxygenase 1 Homo sapiens 49-65 12585963-2 2003 One such protective response is the induction of haem oxygenase 1 (HO-1), which catalyses the rate-limiting step in haem degradation, liberating iron, CO and biliverdin. Iron 145-149 heme oxygenase 1 Homo sapiens 67-71 12704646-1 2003 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin. Iron 83-87 heme oxygenase 1 Homo sapiens 0-16 12704646-1 2003 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin. Iron 83-87 heme oxygenase 1 Homo sapiens 18-22 12585963-4 2003 Either N-acetylcysteine, an antioxidant, or deferoxamine, an iron chelator, resulted in a dose-dependent inhibition of HO-1 mRNA and protein induction during glucose deprivation, suggesting a redox- and iron-dependent mechanism. Iron 61-65 heme oxygenase 1 Homo sapiens 119-123 12511571-1 2003 Heme oxygenase 1 (HO-1) catalyzes heme breakdown, eventually releasing iron, carbon monoxide, and bilirubin IXalpha. Iron 71-75 heme oxygenase 1 Homo sapiens 0-16 12709571-4 2003 The downregulation of HO-1 expression may reduce energy expenditure and local production of carbon monoxide, iron, and bilirubin and transiently increase intracellular heme pool. Iron 109-113 heme oxygenase 1 Homo sapiens 22-26 12668974-1 2003 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron. Iron 148-152 heme oxygenase 1 Homo sapiens 0-16 12668974-1 2003 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme in heme catabolism, which leads to the generation of carbon monoxide (CO), biliverdin, and free iron. Iron 148-152 heme oxygenase 1 Homo sapiens 18-22 12678694-6 2003 HO1-mediated metabolism of heme groups released from NO-damaged proteins leads to a change in the levels of redox-active iron and a release of carbon monoxide (CO) and bilirubin, all of which have been implicated in cellular resistance to oxidative stress. Iron 121-125 heme oxygenase 1 Homo sapiens 0-3 12511571-6 2003 Expression of HO-1 was also reduced in human cells when exposed to interferon-gamma or an iron chelator desferrioxamine, each of which induced Bach1 expression. Iron 90-94 heme oxygenase 1 Homo sapiens 14-18 12572666-6 2003 Heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in Alzheimer disease suggesting increased heme turnover as a source of redox-active iron. Iron 187-191 heme oxygenase 1 Homo sapiens 0-16 12498987-5 2003 Disrupted HO-1 expression was associated with decreased lung reactive iron and iron-associated proteins, decreased NADPH cytochrome cp450 reductase activity, and decreased lung peroxidase activity compared to WT. Iron 70-74 heme oxygenase 1 Homo sapiens 10-14 12572666-6 2003 Heme oxygenase-1, an enzyme that catalyzes the conversion of heme to iron and biliverdin, is increased in Alzheimer disease suggesting increased heme turnover as a source of redox-active iron. Iron 69-73 heme oxygenase 1 Homo sapiens 0-16 12935634-1 2003 Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain. Iron 101-105 heme oxygenase 1 Homo sapiens 0-16 12935634-1 2003 Heme oxygenase-1 (HO-1) is a 32 kDa heat shock protein (HSP) that catalyzes heme to biliverdin, free iron and carbon monoxide in the brain. Iron 101-105 heme oxygenase 1 Homo sapiens 18-22 12498987-5 2003 Disrupted HO-1 expression was associated with decreased lung reactive iron and iron-associated proteins, decreased NADPH cytochrome cp450 reductase activity, and decreased lung peroxidase activity compared to WT. Iron 79-83 heme oxygenase 1 Homo sapiens 10-14 12498987-7 2003 This suggests that disruption of HO-1 protects against hyperoxia by diminishing the generation of toxic reactive intermediates in the lung via iron and H(2)O(2). Iron 143-147 heme oxygenase 1 Homo sapiens 33-37 12230869-1 2002 Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin. Iron 86-90 heme oxygenase 1 Homo sapiens 0-16 12964953-5 2003 HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO). Iron 170-174 heme oxygenase 1 Homo sapiens 0-4 12382200-12 2002 Heme oxygenase 1 is essential for the catabolism of heme and in the recycling of hemoglobin iron in macrophages. Iron 92-96 heme oxygenase 1 Homo sapiens 0-16 12230868-3 2002 HO-1 is a cytoprotective enzyme that degrades heme, a potent oxidant, to generate carbon monoxide, biliverdin (subsequently reduced to bilirubin), and iron. Iron 151-155 heme oxygenase 1 Homo sapiens 0-4 12394829-2 2002 The cytoprotection may result from the elimination of heme and the function of HO-1 downstream mediators, that is, biliverdin, carbon monoxide, and free iron. Iron 153-157 heme oxygenase 1 Homo sapiens 79-83 12398878-3 2002 HO-1 expression was correlated with increased tissue iron and/or ferritin expression and increased inflammatory/oxidant load as measured by myeloperoxidase expression. Iron 53-57 heme oxygenase 1 Homo sapiens 0-4 12230869-1 2002 Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin. Iron 86-90 heme oxygenase 1 Homo sapiens 18-22 12230871-4 2002 HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin. Iron 155-159 heme oxygenase 1 Homo sapiens 0-4 12082007-0 2002 Heme oxygenase-1-mediated protection: potential role of nonheme iron-nitric oxide complexes. Iron 64-68 heme oxygenase 1 Homo sapiens 0-16 11707736-5 2001 Increased HO-1 protein was associated with a brisk and early increase in catalytically active iron and a robust increase in cellular ferritin. Iron 94-98 heme oxygenase 1 Homo sapiens 10-14 11592943-1 2001 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Iron 88-92 heme oxygenase 1 Homo sapiens 0-16 11592943-1 2001 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Iron 88-92 heme oxygenase 1 Homo sapiens 18-22 11208917-3 2001 We have also shown that reactive iron (Fe3+) and cGMP staining spatially resemble that of HO-1; which, in turn, colocalizes in motor neurons with transcription factors: Fas-associated protein containing death domain (FADD), tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) and p53. Iron 33-37 heme oxygenase 1 Homo sapiens 90-94 11668058-1 2001 Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron. Iron 103-107 heme oxygenase 1 Homo sapiens 0-16 11668058-1 2001 Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron. Iron 103-107 heme oxygenase 1 Homo sapiens 18-22 11572959-7 2001 Macrophage-inducible NOS generates NO to kill other cells, whereas HO1 generates bilirubin to exert antioxidant cytoprotective effects and also provides cytoprotection by facilitating iron extrusion from cells. Iron 184-188 heme oxygenase 1 Homo sapiens 67-70 11571246-3 2001 METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells. Iron 218-222 heme oxygenase 1 Homo sapiens 100-104 11571246-3 2001 METHODS AND RESULTS: Infection of rat aortic smooth muscle cells with adenovirus carrying the human HO-1 gene (Adv-HO-1) resulted in a high-level expression of HO-1 protein, which effectively reduced the hemin-induced iron overload in these cells. Iron 218-222 heme oxygenase 1 Homo sapiens 115-119 11551744-7 2001 Preconditioning induction of stress proteins (i.e., hemeoxygenase-1 and neuronal nitric oxide synthase) and hypothermia therapy suppress the generation of toxic reactive oxygen, lipid, and thiol species evoked by bioactive iron complexes in the brain. Iron 223-227 heme oxygenase 1 Homo sapiens 52-67 11121422-1 2001 The crystal structure of heme oxygenase-1 suggests that Asp-140 may participate in a hydrogen bonding network involving ligands coordinated to the heme iron atom. Iron 152-156 heme oxygenase 1 Homo sapiens 25-41 11015442-1 2000 Heme oxygenase 1 (HO-1) inhibits apoptosis by regulating cellular prooxidant iron. Iron 77-81 heme oxygenase 1 Homo sapiens 0-22 10942763-1 2000 The human heme oxygenase-1 crystal structure suggests that Gly-139 and Gly-143 interact directly with iron-bound ligands. Iron 102-106 heme oxygenase 1 Homo sapiens 10-26 11085891-2 2000 Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide. Iron 134-138 heme oxygenase 1 Homo sapiens 63-79 11085891-2 2000 Among the consequences of oxidative stress is the induction of heme oxygenase-1 (HO-1), an inducible isozyme that metabolizes heme to iron, biliverdin, and carbon monoxide. Iron 134-138 heme oxygenase 1 Homo sapiens 81-85 10985695-1 2000 Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin. Iron 220-224 heme oxygenase 1 Homo sapiens 119-141 10985695-1 2000 Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin. Iron 220-224 heme oxygenase 1 Homo sapiens 143-149 10985695-1 2000 Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin. Iron 226-228 heme oxygenase 1 Homo sapiens 119-141 10985695-1 2000 Extracellular heme derived from hemoglobin following hemorrhage or released from dying cells induces the expression of heme oxygenase-1 (HO-1, HSP-32) which metabolizes heme to the gaseous mediator carbon monoxide (CO), iron (Fe) and biliverdin. Iron 226-228 heme oxygenase 1 Homo sapiens 143-149 11232594-2 2000 The precipitating cause of such oxidative stress may be misregulated iron homeostasis because there are profound alterations in heme oxygenase-1 (HO-1), redox-active iron, and iron regulatory proteins. Iron 69-73 heme oxygenase 1 Homo sapiens 128-144 10997923-9 2000 We also demonstrate that, in LLC-PK(1) cells exposed to nitric oxide donors, chelatable iron is involved in eliciting the HO-1 response observed at lower concentrations of these donors, and in mediating the cytotoxic effects of these donors when present in higher concentrations. Iron 88-92 heme oxygenase 1 Homo sapiens 122-126 11023535-8 2000 Our results suggest that increased sequestration of iron as a consequence of induced HO-1 might be involved in the adaptive protection after HBO treatment and that the induction of DNA damage is not the trigger for adaptive protection. Iron 52-56 heme oxygenase 1 Homo sapiens 85-89 10733947-4 2000 The relationship between heme oxygenase-1 activation and iron metabolism was investigated by measurement of activities of both cytosolic and mitochondrial cis-aconitase enzymes. Iron 57-61 heme oxygenase 1 Homo sapiens 25-41 10733947-6 2000 We propose that modulation of cis-aconitase activity at the translational level by an increase of cellular iron is an important consequence of heme oxygenase-1 activation. Iron 107-111 heme oxygenase 1 Homo sapiens 143-159 11053673-2 2000 Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide. Iron 89-93 heme oxygenase 1 Homo sapiens 0-16 11053673-2 2000 Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide. Iron 89-93 heme oxygenase 1 Homo sapiens 18-22 11053673-4 2000 In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone. Iron 88-92 heme oxygenase 1 Homo sapiens 63-67 11053673-4 2000 In these cells and in rat astroglia transfected with the human HO-1 gene, mitochondrial iron trapping is abrogated by the HO-1 inhibitors, tin-mesoporphyrin and dexamethasone. Iron 88-92 heme oxygenase 1 Homo sapiens 122-126 11053673-7 2000 Collectively, our findings suggest that HO-1 over-expression contributes to the pathological iron deposition and mitochondrial damage documented in these aging-related neurodegenerative disorders. Iron 93-97 heme oxygenase 1 Homo sapiens 40-44 10872745-5 2000 We had previously shown that inhibitors of HO-1 and the mitochondrial permeability transition pore (MTP) block the uptake of mitochondrial iron in astrocytes exposed to the pro-oxidant effects of dopamine and several pro-inflammatory cytokines. Iron 139-143 heme oxygenase 1 Homo sapiens 43-47 10872745-7 2000 Thus, the marked enhancement of HO-1 expression previously demonstrated in AD-affected neurons and astroglia may transduce amyloid (oxidative) stress into the abnormal patterns of iron deposition and mitochondrial insufficiency characteristic of this disease. Iron 180-184 heme oxygenase 1 Homo sapiens 32-36 11232594-2 2000 The precipitating cause of such oxidative stress may be misregulated iron homeostasis because there are profound alterations in heme oxygenase-1 (HO-1), redox-active iron, and iron regulatory proteins. Iron 69-73 heme oxygenase 1 Homo sapiens 146-150 10644516-8 2000 Iron depletion by desferrioxamine mesylate, a specific iron complexon, completely inhibited hypoxic stimulation of HO-1 but did not attenuate the effect of H(2)O(2) and CCCP on HO-1 mRNA. Iron 0-4 heme oxygenase 1 Homo sapiens 115-119 10644516-8 2000 Iron depletion by desferrioxamine mesylate, a specific iron complexon, completely inhibited hypoxic stimulation of HO-1 but did not attenuate the effect of H(2)O(2) and CCCP on HO-1 mRNA. Iron 55-59 heme oxygenase 1 Homo sapiens 115-119 10644516-1 2000 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme catabolism and presumably is involved in cellular iron homeostasis. Iron 115-119 heme oxygenase 1 Homo sapiens 0-16 10644516-1 2000 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme catabolism and presumably is involved in cellular iron homeostasis. Iron 115-119 heme oxygenase 1 Homo sapiens 18-22 10581397-1 1999 Heme oxygenase-1 (HO-1) is an inducible enzyme involved in heme catabolism, tissue iron homeostasis and the cellular response to oxidative stress. Iron 83-87 heme oxygenase 1 Homo sapiens 0-16 10842752-4 2000 In fact, in oxidative stress in vitro, HO-1 is protective (91-94) but within a narrow threshold of overexpression (93,94) in some models, since iron released in the HO reaction may obviate any cytoprotective effect (Fig. Iron 144-148 heme oxygenase 1 Homo sapiens 39-43 10589693-4 1999 Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression. Iron 121-125 heme oxygenase 1 Homo sapiens 42-58 10589693-4 1999 Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression. Iron 121-125 heme oxygenase 1 Homo sapiens 60-64 10589693-4 1999 Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression. Iron 127-129 heme oxygenase 1 Homo sapiens 42-58 10589693-4 1999 Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression. Iron 127-129 heme oxygenase 1 Homo sapiens 60-64 10589693-4 1999 Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression. Iron 172-174 heme oxygenase 1 Homo sapiens 42-58 10589693-4 1999 Induction of the heme catabolizing enzyme heme oxygenase-1 (HO-1), which generates biliverdin, carbon monoxide (CO), and iron (Fe), may provide such a mechanism, as CO and Fe are two negative modulators of iNOS activity and expression. Iron 172-174 heme oxygenase 1 Homo sapiens 60-64 10581397-1 1999 Heme oxygenase-1 (HO-1) is an inducible enzyme involved in heme catabolism, tissue iron homeostasis and the cellular response to oxidative stress. Iron 83-87 heme oxygenase 1 Homo sapiens 18-22 10581397-2 1999 Elevated HO-1 expression in astrocytes has been observed in association with abnormal iron deposition and increased oxidative stress in Parkinson"s disease (PD). Iron 86-90 heme oxygenase 1 Homo sapiens 9-13 10581397-13 1999 HO-1 and its metabolites could then contribute to the oxidative stress and iron deposition associated with PD. Iron 75-79 heme oxygenase 1 Homo sapiens 0-4 12835114-4 1999 Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells. Iron 31-35 heme oxygenase 1 Homo sapiens 175-179 10517538-4 1999 UVA radiation also leads to an increase in labile iron pools (either directly or via HO-1) and eventual increases in ferritin levels. Iron 50-54 heme oxygenase 1 Homo sapiens 85-89 12835114-4 1999 Dopamine-induced mitochondrial iron trapping was abrogated by administration of the heme oxygenase inhibitors, tin mesoporphyrin (SnMP) or dexamethasone (DEX) indicating that HO-1 upregulation is necessary for subsequent mitochondrial iron deposition in these cells. Iron 235-239 heme oxygenase 1 Homo sapiens 175-179 12835114-5 1999 Overexpression of the human HO-1 gene in cultured rat astroglia by transient transfection also stimulated mitochondrial (55)Fe deposition, an effect that was again preventible by SnMP or DEX administration. Iron 124-126 heme oxygenase 1 Homo sapiens 28-32 12835114-6 1999 We hypothesize that free ferrous iron and carbon monoxide generated by HO-1-mediated heme degradation promote mitochondrial membrane injury and the deposition of redox-active iron within this organelle. Iron 33-37 heme oxygenase 1 Homo sapiens 71-75 12835114-6 1999 We hypothesize that free ferrous iron and carbon monoxide generated by HO-1-mediated heme degradation promote mitochondrial membrane injury and the deposition of redox-active iron within this organelle. Iron 175-179 heme oxygenase 1 Homo sapiens 71-75 12835114-8 1999 Stress-induced up-regulation of HO-1 in astroglia may be responsible for the abnormal patterns of brain iron deposition and mitochondrial insufficiency documented in various human neurodegenerative disorders. Iron 104-108 heme oxygenase 1 Homo sapiens 32-36 10193374-3 1998 HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO). Iron 41-45 heme oxygenase 1 Homo sapiens 0-4 10217256-3 1999 We also provide evidence that up-regulation of the stress protein heme oxygenase-1 (HO-1) is both necessary and sufficient for mitochondrial iron trapping in dopamine-challenged astroglia. Iron 141-145 heme oxygenase 1 Homo sapiens 66-82 10101013-0 1999 Iron regulates hyperoxia-dependent human heme oxygenase 1 gene expression in pulmonary endothelial cells. Iron 0-4 heme oxygenase 1 Homo sapiens 41-57 10101013-8 1999 We also found that HO-1 expression depended on chelatable iron. Iron 58-62 heme oxygenase 1 Homo sapiens 19-23 10101013-9 1999 The iron chelator desferrioxamine not only inhibited the iron- dependent potentiation of HO-1 in response to hyperoxia but also inhibited both hyperoxia and basal expression. Iron 4-8 heme oxygenase 1 Homo sapiens 89-93 10101013-9 1999 The iron chelator desferrioxamine not only inhibited the iron- dependent potentiation of HO-1 in response to hyperoxia but also inhibited both hyperoxia and basal expression. Iron 57-61 heme oxygenase 1 Homo sapiens 89-93 10090762-1 1999 The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized. Iron 83-87 heme oxygenase 1 Homo sapiens 35-51 10090762-1 1999 The H25C and H25Y mutants of human heme oxygenase-1 (hHO-1), in which the proximal iron ligand is replaced by a cysteine or tyrosine, have been expressed and characterized. Iron 83-87 heme oxygenase 1 Homo sapiens 53-58 9380735-0 1997 Heme oxygenase 1 is required for mammalian iron reutilization. Iron 43-47 heme oxygenase 1 Homo sapiens 0-16 9828853-3 1998 HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO). Iron 41-45 heme oxygenase 1 Homo sapiens 0-4 9514830-9 1998 In addition, excessive cellular levels of heme-derived free iron and carbon monoxide resulting from HO-1 overactivity may contribute to the pathogenesis of PD. Iron 60-64 heme oxygenase 1 Homo sapiens 100-104 9380736-1 1997 Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron. Iron 141-145 heme oxygenase 1 Homo sapiens 37-53 9380736-1 1997 Stressed mammalian cells up-regulate heme oxygenase 1 (Hmox1; EC 1.14.99.3), which catabolizes heme to biliverdin, carbon monoxide, and free iron. Iron 141-145 heme oxygenase 1 Homo sapiens 55-60 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Iron 212-216 heme oxygenase 1 Homo sapiens 17-21 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Iron 174-176 heme oxygenase 1 Homo sapiens 88-92 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Iron 174-176 heme oxygenase 1 Homo sapiens 94-99 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Iron 212-216 heme oxygenase 1 Homo sapiens 239-243 8654390-1 1996 Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide. Iron 97-101 heme oxygenase 1 Homo sapiens 0-16 8650873-1 1996 OBJECTIVES: Heme oxygenase isozymes, HO-1 and HO-2, are members of the stress/heat shock (HSP) family of proteins, with the known function of cleaving the heme molecule to biliverdin, iron, and carbon monoxide. Iron 184-188 heme oxygenase 1 Homo sapiens 37-50 8650873-12 1996 CONCLUSIONS: The finding that HO-1 expression is increased in BPH and malignant prostate tissue is consistent with a role for this stress protein in the pathogenesis of BPH and prostate cancer; in the context of iron metabolism, an argument is made in support of this possibility. Iron 212-216 heme oxygenase 1 Homo sapiens 30-34 33587911-4 2021 In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli. Iron 183-187 heme oxygenase 1 Homo sapiens 15-31 8547275-1 1996 His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1). Iron 68-72 heme oxygenase 1 Homo sapiens 83-107 8547275-1 1996 His-25 and His-132 are the primary candidates for the proximal heme iron ligand in heme oxygenase isozyme-1 (HO-1). Iron 68-72 heme oxygenase 1 Homo sapiens 109-113 33804125-1 2021 Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron. Iron 139-143 heme oxygenase 1 Homo sapiens 0-16 33804125-1 2021 Heme oxygenase-1 (HO-1) plays a vital role in the catabolism of heme and yields equimolar amounts of biliverdin, carbon monoxide, and free iron. Iron 139-143 heme oxygenase 1 Homo sapiens 18-22 33803317-5 2021 Heme oxygenase-1 (HO-1) is an iron-dependent cytoprotective enzyme that functions as the inducible form of HO. Iron 30-34 heme oxygenase 1 Homo sapiens 0-16 33803317-5 2021 Heme oxygenase-1 (HO-1) is an iron-dependent cytoprotective enzyme that functions as the inducible form of HO. Iron 30-34 heme oxygenase 1 Homo sapiens 18-22 33815094-0 2021 Elevated Heme Oxygenase-1 Correlates With Increased Brain Iron Deposition Measured by Quantitative Susceptibility Mapping and Decreased Hemoglobin in Patients With Parkinson"s Disease. Iron 58-62 heme oxygenase 1 Homo sapiens 9-25 33815094-3 2021 Objective: To explore the association of the level of HO-1 with brain iron deposition and low level of HGB in PD. Iron 70-74 heme oxygenase 1 Homo sapiens 54-58 33815094-11 2021 There was a significantly positive correlation between the serum HO-1 concentration and iron deposition within SN, an inverse correlation between the serum HO-1 concentration and HGB level in PD patients. Iron 88-92 heme oxygenase 1 Homo sapiens 65-69 33587911-4 2021 In the future, heme oxygenase-1 (HO-1) may also become a candidate ILD biomarker; it is a 32-kDa heat shock protein converting heme to carbon monoxide, biliverdin/bilirubin, and free iron to play a role in the pulmonary cytoprotective reaction in response to various stimuli. Iron 183-187 heme oxygenase 1 Homo sapiens 33-37 34841438-1 2022 Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin. Iron 91-95 heme oxygenase 1 Homo sapiens 0-16 34841438-1 2022 Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin. Iron 91-95 heme oxygenase 1 Homo sapiens 18-22 34782602-0 2021 Iron overload in endometriosis peritoneal fluid induces early embryo ferroptosis mediated by HMOX1. Iron 0-4 heme oxygenase 1 Homo sapiens 93-98 34547407-0 2021 Heme Oxygenase-1 (HMOX-1) and inhibitor of differentiation proteins (ID1, ID3) are key response mechanisms against iron-overload in pancreatic beta-cells. Iron 115-119 heme oxygenase 1 Homo sapiens 0-16 34547407-0 2021 Heme Oxygenase-1 (HMOX-1) and inhibitor of differentiation proteins (ID1, ID3) are key response mechanisms against iron-overload in pancreatic beta-cells. Iron 115-119 heme oxygenase 1 Homo sapiens 18-24 34547407-12 2021 Our findings suggest that HMOX1, ID1 and ID3 define the response mechanism against iron-overload-induced stress in beta-cells. Iron 83-87 heme oxygenase 1 Homo sapiens 26-31 34728736-8 2021 Free iron and biliverdin, which are metabolic byproducts of heme catalysis by HO-1, also suppressed the viral infection. Iron 5-9 heme oxygenase 1 Homo sapiens 78-82 34508760-9 2021 More importantly, HMOX1 knockdown attenuated Fe2+ overload, reduced iron content and ROS, and alleviated lipid peroxidation, which led to a reduction in ferroptosis in diabetic human endothelial cells. Iron 68-72 heme oxygenase 1 Homo sapiens 18-23 34530349-4 2021 In the present study, we found that iron overload promoted ferroptosis in hepatocytes by excessively inducing HO-1 expression, which contributed to the progression of liver injury and fibrosis, accompanied by the upregulation of the FGF21 protein level in vitro and in vivo. Iron 36-40 heme oxygenase 1 Homo sapiens 110-114 34269613-5 2021 Internalization of ferrylHb is accompanied by up-regulation of heme oxygenase-1 and H-ferritin and accumulation of iron within lysosomes as a result of heme/iron uptake. Iron 157-161 heme oxygenase 1 Homo sapiens 63-79 34583348-7 2021 A cross-sectional study was conducted to determine the association between plasma levels of free heme, HO-1, Hp, Hx, and malaria status in pregnant women who received routine iron supplementation and their birth outcomes. Iron 175-179 heme oxygenase 1 Homo sapiens 103-107 35603834-7 2022 Fe-R-H regulators such as lactoferrin (LF), hemoxygenase-1 (HO-1), erythropoietin (EPO) and hepcidin modulators are innate bio-replenishments that sequester iron, neutralize iron-mediated free radicals, reduce oxidative stress, and improve host defense by optimizing iron metabolism. Iron 157-161 heme oxygenase 1 Homo sapiens 60-64 34360940-3 2021 Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin. Iron 162-166 heme oxygenase 1 Homo sapiens 0-16 34360940-3 2021 Heme oxygenase-1 (HO-1) has evolved to promptly attend to such injurious potential by facilitating degradation of heme into equimolar amounts of carbon monoxide, iron, and biliverdin. Iron 162-166 heme oxygenase 1 Homo sapiens 18-22 34345202-11 2021 As a downstream gene (effector) of Nrf2, heme oxygenase-1 (HO-1) expression increased significantly with the treatment of tagitinin C. Upregulated HO-1 led to the increase in the labile iron pool, which promoted lipid peroxidation, meanwhile tagitinin C showed synergistic anti-tumor effect together with erastin. Iron 186-190 heme oxygenase 1 Homo sapiens 147-151 35598199-4 2022 METHODS AND RESULTS: Proteomic analyses found that ATO can affect the signaling pathway associated with ferroptosis, including the upregulation of iron absorption (FTL, FTH1, HO-1), ferritinophagy (LC3, P62, ATG7, NCOA4) and modifier of glutathione synthesis (GCLM); downregulation of glutamine synthetase (GS) and GPX4, which was the critical inhibitor of ferroptosis. Iron 147-151 heme oxygenase 1 Homo sapiens 175-179 35603834-7 2022 Fe-R-H regulators such as lactoferrin (LF), hemoxygenase-1 (HO-1), erythropoietin (EPO) and hepcidin modulators are innate bio-replenishments that sequester iron, neutralize iron-mediated free radicals, reduce oxidative stress, and improve host defense by optimizing iron metabolism. Iron 174-178 heme oxygenase 1 Homo sapiens 60-64 35603834-7 2022 Fe-R-H regulators such as lactoferrin (LF), hemoxygenase-1 (HO-1), erythropoietin (EPO) and hepcidin modulators are innate bio-replenishments that sequester iron, neutralize iron-mediated free radicals, reduce oxidative stress, and improve host defense by optimizing iron metabolism. Iron 267-271 heme oxygenase 1 Homo sapiens 60-64 35419301-2 2022 HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron. Iron 108-112 heme oxygenase 1 Homo sapiens 0-4 35631320-12 2022 Among products of HO-1 catalyzed heme degradation iron mimicked the anti-calcification effect of heme. Iron 50-54 heme oxygenase 1 Homo sapiens 18-22 35631320-13 2022 We concluded that heme-induced upregulation of the Nrf2/HO-1 system inhibits HuLECs calcification through the liberation of heme iron. Iron 129-133 heme oxygenase 1 Homo sapiens 56-60 35624725-1 2022 Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron. Iron 151-155 heme oxygenase 1 Homo sapiens 0-16 35624725-1 2022 Heme oxygenase-1 (HO-1) is an enzyme that catalyzes the degradation of heme, releasing equimolar amounts of carbon monoxide (CO), biliverdin (BV), and iron. Iron 151-155 heme oxygenase 1 Homo sapiens 18-22 35624725-3 2022 However, iron constitutes an important product of HO-1 activity involved in the regulation of several cellular biological processes. Iron 9-13 heme oxygenase 1 Homo sapiens 50-54 35281042-7 2022 Being a highly infectious pathogenic bacterium, Mycobacterium tuberculosis (MTB) infection causes acute oxidative stress, and increases the expression of HO-1, which may in turn facilitate MTB survival and growth due to increased iron availability. Iron 230-234 heme oxygenase 1 Homo sapiens 154-158 35281042-8 2022 Moreover, in severe cases of MTB infection, excessive reactive oxygen species (ROS) and free iron (Fe2+) due to high levels of HO-1 can lead to lipid peroxidation and ferroptosis, which may promote further MTB dissemination from cells undergoing ferroptosis. Iron 93-97 heme oxygenase 1 Homo sapiens 127-131 33863580-8 2021 In endometriosis, total iron showed a positive correlation with HO-1 (r, 0.518, p = 0.001), but there were no antioxidants that correlated with iron in non-endometriosis. Iron 24-28 heme oxygenase 1 Homo sapiens 64-68 35204159-2 2022 HO-1 and its end products, biliverdin, carbon monoxide and free iron (Fe2+), confer cytoprotection against inflammatory and oxidative injury. Iron 64-68 heme oxygenase 1 Homo sapiens 0-4 33863580-10 2021 CONCLUSIONS: HO-1 may regulate the delicate balance of iron-induced oxidative stress in endometriotic cyst fluid. Iron 55-59 heme oxygenase 1 Homo sapiens 13-17 32976958-7 2020 Both HFD-fed mice and PA/OA-induced HepG2 cells displayed ferroptosis-based panel of biomarkers such as iron overload with the up-regulation of TFR1 and the down-regulation of FTH1, lipid peroxidation and inhibition of Nrf2 activity, which further induced GPX4 and HO-1 levels. Iron 104-108 heme oxygenase 1 Homo sapiens 265-269 33537805-3 2021 HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron. Iron 113-117 heme oxygenase 1 Homo sapiens 0-4 33440611-1 2021 Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin. Iron 193-197 heme oxygenase 1 Homo sapiens 0-16 33440611-1 2021 Heme Oxygenase-1 (HO-1) is a type II detoxifying enzyme that catalyzes the rate-limiting step in heme degradation leading to the formation of equimolar quantities of carbon monoxide (CO), free iron and biliverdin. Iron 193-197 heme oxygenase 1 Homo sapiens 18-22 33075721-0 2021 Role of heme oxygenase-1 in human placenta on iron supply to fetus. Iron 46-50 heme oxygenase 1 Homo sapiens 8-24 33075721-2 2021 Recently, increasing evidence has shown that heme oxygenase (HO)-1, which is an inducible isoform of the rate-limiting enzyme in the heme degradation pathway, may be involved in the effective reutilization of iron. Iron 209-213 heme oxygenase 1 Homo sapiens 45-66 33075721-9 2021 Placenta with fetal death (miscarriage) in the first and second trimester indicate significantly higher ratio of ho-1 gene for iron production to the fpn-1 gene for iron excretion than normal. Iron 127-131 heme oxygenase 1 Homo sapiens 113-117 33075721-11 2021 DISCUSSION: These findings suggest that HO-1 in placenta plays an important role in iron supplying system in the second trimester to support fetal development. Iron 84-88 heme oxygenase 1 Homo sapiens 40-44 33276470-1 2020 Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin. Iron 121-125 heme oxygenase 1 Homo sapiens 0-16 33276470-1 2020 Heme oxygenase 1 (HO-1) is the rate-limiting enzyme of heme oxidative degradation, generating carbon monoxide (CO), free iron, and biliverdin. Iron 121-125 heme oxygenase 1 Homo sapiens 18-22 33671004-8 2021 In contrast, in ferroptosis, HO-1 may play a pro-death role via enhancing iron release. Iron 74-78 heme oxygenase 1 Homo sapiens 29-33 33643023-3 2021 However, iron and carbon monoxide produced by the catabolism of HO-1 exert detrimental effects on patients with PD. Iron 9-13 heme oxygenase 1 Homo sapiens 64-68 33514947-4 2021 In this Review, we present an introduction to HO-1 for immunologists, including an overview of its roles in iron metabolism and antioxidant defence, and the factors which regulate its expression. Iron 108-112 heme oxygenase 1 Homo sapiens 46-50 33584308-0 2020 Mitochondrial Iron Overload-Mediated Inhibition of Nrf2-HO-1/GPX4 Assisted ALI-Induced Nephrotoxicity. Iron 14-18 heme oxygenase 1 Homo sapiens 56-60 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Iron 85-89 heme oxygenase 1 Homo sapiens 31-34 33266044-1 2020 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide. Iron 111-115 heme oxygenase 1 Homo sapiens 0-16 33266044-1 2020 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme molecules releasing equimolar amounts of biliverdin, iron and carbon monoxide. Iron 111-115 heme oxygenase 1 Homo sapiens 18-22 31704097-5 2019 Accordingly, the phenotype of BVR-deficient cells can be mimicked by hemin or iron overload, whereas depletion of HO-1 in BVR-deficient ECs abrogates the increase in intracellular free iron and oxidative stress, preventing the loss of endothelial markers. Iron 185-189 heme oxygenase 1 Homo sapiens 114-118 32968051-0 2020 Heme oxygenase 1 protects human colonocytes against ROS formation, oxidative DNA damage and cytotoxicity induced by heme iron, but not inorganic iron. Iron 121-125 heme oxygenase 1 Homo sapiens 0-16 32393788-3 2020 The fasting-mimicking diet selectivity reverses vitamin C-induced up-regulation of heme-oxygenase-1 and ferritin in KRAS-mutant cancer cells, consequently increasing reactive iron, oxygen species, and cell death; an effect further potentiated by chemotherapy. Iron 175-179 heme oxygenase 1 Homo sapiens 83-99 32112801-4 2020 This was associated with reduced ferritin induction by hemoglobin; expression of heme oxygenase-1, which catalyzes iron release from heme, was not altered. Iron 115-119 heme oxygenase 1 Homo sapiens 81-97 32059452-1 2020 Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury. Iron 110-114 heme oxygenase 1 Homo sapiens 0-16 32059452-1 2020 Heme oxygenase-1 (HO-1), an intracellular enzyme that catalyzes the degradation of heme into biliverdin, free iron, and carbon monoxide, exerts anti-inflammatory and cytoprotective effects against endothelial cell injury. Iron 110-114 heme oxygenase 1 Homo sapiens 18-22 31704095-1 2019 Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron. Iron 109-113 heme oxygenase 1 Homo sapiens 0-16 31704095-1 2019 Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron. Iron 109-113 heme oxygenase 1 Homo sapiens 18-22 33228260-1 2020 Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase. Iron 128-132 heme oxygenase 1 Homo sapiens 0-16 33228260-1 2020 Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase. Iron 128-132 heme oxygenase 1 Homo sapiens 18-22 33110194-5 2020 Growth and differentiation of cells induced by heme-albumin was dependent on heme-oxygenase 1 (HO-1) function and was accompanied with an increase of the intracellular labile iron pool (LIP). Iron 175-179 heme oxygenase 1 Homo sapiens 95-99 32968051-12 2020 Furthermore, HO-1 abrogation strongly augmented the cytotoxic effects of hemin in HCEC, revealing its pivotal function in colonocytes and highlighting the toxicity of free intracellular heme iron. Iron 191-195 heme oxygenase 1 Homo sapiens 13-17 32899732-1 2020 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin. Iron 85-89 heme oxygenase 1 Homo sapiens 0-16 32899732-1 2020 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin. Iron 85-89 heme oxygenase 1 Homo sapiens 18-22 32908636-6 2020 HO-1 activity leads to production of carbon monoxide (CO), free iron ion, and biliverdin; the latter is promptly reduced to bilirubin. Iron 64-68 heme oxygenase 1 Homo sapiens 0-4 32006543-1 2020 OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin. Iron 56-60 heme oxygenase 1 Homo sapiens 11-27 32006543-1 2020 OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin. Iron 56-60 heme oxygenase 1 Homo sapiens 29-33 32231654-2 2020 Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors. Iron 79-83 heme oxygenase 1 Homo sapiens 0-16 32231654-2 2020 Heme oxygenase-1 (HO-1) catalyzes the conversion of heme into biliverdin (BV), iron and carbon monoxide (CO), all of which have been demonstrated to protect cells from various stressors. Iron 79-83 heme oxygenase 1 Homo sapiens 18-22 31704097-8 2019 Collectively, the non-enzymatic activity of BVR contributes to the maintenance of healthy endothelial phenotype through the prevention of HO-1-dependent iron-overload, oxidative stress and subsequent endothelial-to-mesenchymal transition (EndMT). Iron 153-157 heme oxygenase 1 Homo sapiens 138-142 31279900-5 2019 RESULTS: HO1 and the endoplasmic reticulum (ER) stress marker grp78 were upregulated, together with changes in the expression of multiple iron metabolism-related genes, in post-mortem brain samples from patients with liver cirrhosis and HE. Iron 138-142 heme oxygenase 1 Homo sapiens 9-12 31725784-5 2019 The mineral absorption pathway genes, HMOX1 and VDR are involved in iron metabolism and response to vitamin D, respectively. Iron 68-72 heme oxygenase 1 Homo sapiens 38-43 31279900-7 2019 Upregulation of HO1 by NH4Cl triggered ER stress and was associated with elevated levels of free ferrous iron and expression changes in iron metabolism-related genes, which were largely abolished after knockdown or inhibition of GS, GFAT1/2, HO1 or iron chelation. Iron 105-109 heme oxygenase 1 Homo sapiens 16-19 31279900-7 2019 Upregulation of HO1 by NH4Cl triggered ER stress and was associated with elevated levels of free ferrous iron and expression changes in iron metabolism-related genes, which were largely abolished after knockdown or inhibition of GS, GFAT1/2, HO1 or iron chelation. Iron 136-140 heme oxygenase 1 Homo sapiens 16-19 31421070-6 2019 In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2. Iron 153-157 heme oxygenase 1 Homo sapiens 9-12 30804804-7 2019 The cytoprotective effects of HO-1 depend on several cellular mechanisms including the generation of bilirubin, an anti-oxidant molecule, from the degradation of heme; the induction of ferritin, a strong chelator of free iron; and the release of CO, that displays multiple anti-inflammatory and anti-apoptotic actions. Iron 221-225 heme oxygenase 1 Homo sapiens 30-34 31273911-8 2019 However, the process of HO-1 metabolism can be toxic owing to iron overload and the activation of succedent pathways, for example, the Fenton reaction and oxidative damage; the overall effect of HO-1 in SAH and ICH tends to be protective and harmful, respectively, given the different pathophysiological changes in these two types of haemorrhagic stroke. Iron 62-66 heme oxygenase 1 Homo sapiens 24-28 31396090-3 2019 Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR). Iron 83-87 heme oxygenase 1 Homo sapiens 0-22 31344980-1 2019 Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin. Iron 100-112 heme oxygenase 1 Homo sapiens 0-16 31344980-1 2019 Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin. Iron 100-112 heme oxygenase 1 Homo sapiens 18-22 30009872-1 2019 Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1). Iron 73-77 heme oxygenase 1 Homo sapiens 127-143 30580021-1 2019 BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR). Iron 187-191 heme oxygenase 1 Homo sapiens 12-28 30580021-1 2019 BACKGROUND: Heme oxygenase-1 (HO-1), a cellular stress protein, serves a vital metabolic function as the rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin (BR). Iron 187-191 heme oxygenase 1 Homo sapiens 30-34 30009872-1 2019 Under stressful conditions, cellular heme catabolism to carbon monoxide, iron and biliverdin is mediated by the 32 kDa enzyme, heme oxygenase-1 (HO-1). Iron 73-77 heme oxygenase 1 Homo sapiens 145-149 30009872-7 2019 A comprehensive model of astroglial stress is presented wherein sustained Hmox1 induction promotes oxidative mitochondrial membrane damage, iron sequestration and mitophagy (macroautophagy). Iron 140-144 heme oxygenase 1 Homo sapiens 74-79 30583467-7 2018 The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Iron 142-146 heme oxygenase 1 Homo sapiens 108-112 30213580-3 2019 Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin. Iron 112-116 heme oxygenase 1 Homo sapiens 0-16 30213580-3 2019 Heme oxygenase-1 (HO-1) plays a crucial role in heme degradation and in this way releases carbon monoxide, free iron, and biliverdin. Iron 112-116 heme oxygenase 1 Homo sapiens 18-22 30583467-1 2018 Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions. Iron 106-110 heme oxygenase 1 Homo sapiens 0-21 30583467-7 2018 The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Iron 23-27 heme oxygenase 1 Homo sapiens 108-112 30583467-7 2018 The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Iron 142-146 heme oxygenase 1 Homo sapiens 171-175 30583467-7 2018 The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Iron 23-27 heme oxygenase 1 Homo sapiens 171-175 28793787-7 2018 Constitutive NRF2 activation and subsequent deregulation of iron metabolism have been implicated in cancer development: NRF2-mediated upregulation of the iron storage protein ferritin or heme oxygenase 1 can lead to enhanced proliferation and therapy resistance. Iron 60-64 heme oxygenase 1 Homo sapiens 187-203 30145824-2 2018 Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities. Iron 134-138 heme oxygenase 1 Homo sapiens 57-62 30145824-2 2018 Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities. Iron 134-138 heme oxygenase 1 Homo sapiens 78-94 30145824-2 2018 Bach1 is a mammalian transcription factor that represses Hmox1, which encodes heme oxygenase-1 (HO-1) that can degrade heme into free iron, carbon monoxide, and biliverdin, to play an important role in antioxidant, anti-inflammatory, and antiapoptotic activities. Iron 134-138 heme oxygenase 1 Homo sapiens 96-100 30327713-1 2018 Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress. Iron 81-85 heme oxygenase 1 Homo sapiens 0-16 29959986-6 2018 Long-term iron exposure resulted in iron accumulation, cytosolic ROS formation and increased heme oxygenase 1 (HMOX-1) mRNA expression (all p < 0.001). Iron 10-14 heme oxygenase 1 Homo sapiens 93-109 29959986-6 2018 Long-term iron exposure resulted in iron accumulation, cytosolic ROS formation and increased heme oxygenase 1 (HMOX-1) mRNA expression (all p < 0.001). Iron 10-14 heme oxygenase 1 Homo sapiens 111-117 30040983-1 2018 Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways. Iron 91-95 heme oxygenase 1 Homo sapiens 0-16 30040983-1 2018 Heme Oxygenase-1 (HO-1), a stress- responsive enzyme which catalyzes heme degradation into iron, carbon monoxide, and biliverdin, exerts a neuroprotective role involving many different signaling pathways. Iron 91-95 heme oxygenase 1 Homo sapiens 18-22 30327713-1 2018 Heme oxygenase 1 (Hmox1), a ubiquitous enzyme degrading heme to carbon monoxide, iron, and biliverdin, is one of the cytoprotective enzymes induced in response to a variety of stimuli, including cellular oxidative stress. Iron 81-85 heme oxygenase 1 Homo sapiens 18-23 29974998-6 2018 Moreover, the expression of HO-1, a functional modulator of Tregs, was decreased in vitiligo Tregs, and the concentrations of HO-1 metabolites, including bilirubin, CoHb and iron, were correspondingly decreased in serum of vitiligo patients. Iron 174-178 heme oxygenase 1 Homo sapiens 28-32 29761622-4 2018 HMOX1 is a cytoprotective enzyme that degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron. Iron 112-116 heme oxygenase 1 Homo sapiens 0-5 29753693-2 2018 The aim of this study is to determine whether the combination of 5-aminolevulinic acid (ALA) and iron induces HO-1 expression in healthy human peripheral blood mononuclear cells (PBMC). Iron 97-101 heme oxygenase 1 Homo sapiens 110-114 30354985-1 2018 Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron. Iron 125-129 heme oxygenase 1 Homo sapiens 24-40 30354985-1 2018 Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron. Iron 125-129 heme oxygenase 1 Homo sapiens 42-46 29753693-6 2018 Study C aimed to investigate HO-1 changes during a three-day, repetitive administration of ALA and iron. Iron 99-103 heme oxygenase 1 Homo sapiens 29-33 30159103-1 2018 Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron. Iron 126-130 heme oxygenase 1 Homo sapiens 6-22 30159103-1 2018 Aims: Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate CO, biliverdin, and iron. Iron 126-130 heme oxygenase 1 Homo sapiens 24-28 29452096-1 2018 Heme oxygenase (HO)-1, the inducible isoform of the heme-degrading enzyme HO, plays a critical role in inflammation and iron homeostasis. Iron 120-124 heme oxygenase 1 Homo sapiens 0-21 29698685-3 2018 In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2. Iron 117-121 heme oxygenase 1 Homo sapiens 40-56 29698685-3 2018 In mammalian cells, the accumulation of heme oxygenase-1 (HO-1), which catalyzes the breakdown of heme into CO, free iron and biliverdin, was reported to protect cells against potentially lethal concentrations of CdCl2. Iron 117-121 heme oxygenase 1 Homo sapiens 58-62 29753142-3 2018 Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties. Iron 130-134 heme oxygenase 1 Homo sapiens 0-16 29753142-3 2018 Heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme to produce carbon monoxide (CO), biliverdin and ferrous iron (Fe2+), exerts anti-oxidant, antiinflammatory and anti-apoptotic properties. Iron 130-134 heme oxygenase 1 Homo sapiens 18-22 29302043-3 2018 Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe). Iron 149-153 heme oxygenase 1 Homo sapiens 0-16 29772541-2 2018 Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide. Iron 123-127 heme oxygenase 1 Homo sapiens 0-16 29772541-2 2018 Heme oxygenase-1 (HO-1), a microsomal enzyme discovered decades ago, can metabolize pro-oxidant heme into biliverdin, free iron, and carbon monoxide. Iron 123-127 heme oxygenase 1 Homo sapiens 18-22 29921869-9 2018 Iron deposition associated with oxidative injury as indicated by heme oxygenase-1 abundance. Iron 0-4 heme oxygenase 1 Homo sapiens 65-81 29783634-4 2018 Molecular modeling studies confirmed a consolidated binding mode in which the nitrogen of the imidazolyl moiety coordinated the heme ferrous iron, meanwhile the hydrophobic groups were located in the western region of HO-1 binding pocket. Iron 141-145 heme oxygenase 1 Homo sapiens 218-222 29302043-3 2018 Heme oxygenase-1 (HO) is the rate limiting enzyme in heme metabolism leading to the equimolar production of bilirubin, carbon monoxide (CO) and free iron (Fe). Iron 155-157 heme oxygenase 1 Homo sapiens 0-16 29394034-7 2018 Furthermore, Fe-binding and Fe-regulatory proteins, such as hepcidin, lipocalin-2/NGAL, heme oxygenase-1, ferritin, and iron-sulfur clusters can display antitumor properties under specific conditions and in particular cancer types. Iron 13-15 heme oxygenase 1 Homo sapiens 88-104 29274359-8 2018 The ferroptotic process induced by hHO-1 overexpression further indicated that HO-1 is a key mediator of BAY-induced ferroptosis that operates through cellular redox regulation and iron accumulation. Iron 181-185 heme oxygenase 1 Homo sapiens 35-40 28206992-2 2017 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide. Iron 185-189 heme oxygenase 1 Homo sapiens 0-16 29163402-3 2017 Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin. Iron 28-32 heme oxygenase 1 Homo sapiens 14-18 29163402-3 2017 Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin. Iron 54-66 heme oxygenase 1 Homo sapiens 14-18 28655775-0 2017 The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Iron 4-8 heme oxygenase 1 Homo sapiens 73-89 28655775-1 2017 Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Iron 51-55 heme oxygenase 1 Homo sapiens 93-109 28655775-1 2017 Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Iron 51-55 heme oxygenase 1 Homo sapiens 111-114 28655775-1 2017 Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Iron 208-212 heme oxygenase 1 Homo sapiens 93-109 28655775-1 2017 Mammals incorporate a major proportion of absorbed iron as heme, which is catabolized by the heme oxygenase 1 (HO1)-NADPH-cytochrome P450 reductase (CPR) complex into biliverdin, carbon monoxide, and ferrous iron. Iron 208-212 heme oxygenase 1 Homo sapiens 111-114 28756878-1 2017 Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin. Iron 116-120 heme oxygenase 1 Homo sapiens 0-16 28756878-1 2017 Heme oxygenase-1 (HO-1) is the enzyme catalyzing the rate-limiting oxidative degradation of cellular heme into free iron, carbon monoxide (CO), and biliverdin, which is then rapidly converted into bilirubin. Iron 116-120 heme oxygenase 1 Homo sapiens 18-22 28206992-2 2017 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme by which heme is catabolized to biliverdin and thence to bilirubin, with the simultaneous release of equimolar quantities of ferrous iron (Fe3+) and carbon monoxide. Iron 185-189 heme oxygenase 1 Homo sapiens 18-22 28704474-6 2017 In these animals the catalytic activity of heme oxygenase 1 contributed to the release of elemental iron from the protoporphyrin ring of heme within enterocytes, which may then be transported by the strongly expressed ferroportin across the basolateral membrane to the circulation. Iron 100-104 heme oxygenase 1 Homo sapiens 43-59 27571925-5 2016 Iron, one of HO-1 catalytic products, was an important mediator in this regulation. Iron 0-4 heme oxygenase 1 Homo sapiens 13-17 28347842-2 2017 The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals. Iron 109-113 heme oxygenase 1 Homo sapiens 11-27 28347842-2 2017 The enzyme heme oxygenase-1 (HO-1), involved in the degradation of heme, forms carbon monoxide (CO), ferrous iron, and bilirubin in conjunction with biliverdin reductase, and is induced by various stimuli including oxidative stress and heavy metals. Iron 109-113 heme oxygenase 1 Homo sapiens 29-33 28347842-10 2017 GENERAL SIGNIFICANCE: The key role of heme metabolism in the stress-inducible expression of HO-1 may promote further studies on heme and its degradation products as protective factors of cellular stresses and iron homeostasis in specialized cells, organs, and whole animal systems. Iron 209-213 heme oxygenase 1 Homo sapiens 92-96 28186648-1 2017 Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide. Iron 78-82 heme oxygenase 1 Homo sapiens 0-16 28186648-1 2017 Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide. Iron 78-82 heme oxygenase 1 Homo sapiens 18-22 28421060-3 2017 HO-1 catalyzes the rate-limiting step in the conversion of heme into iron, biliverdin and the gasotransmitter carbon monoxide (CO), all of which share anti-apoptotic, anti-inflammatory, pro-survival, and tumorigenic activities. Iron 69-73 heme oxygenase 1 Homo sapiens 0-4 28082120-2 2017 Under several stress stimuli, HO-1 expression and activity is up-regulated to catalyze the rate-limiting enzymatic step of heme degradation into carbon monoxide, free iron, and biliverdin. Iron 167-171 heme oxygenase 1 Homo sapiens 30-34 28088947-1 2017 Heme oxygenase (HO-1) catalyzes heme to carbon monoxide (CO), biliverdin/bilirubin, and iron and is known to prevent the pathogenesis of several human diseases. Iron 88-92 heme oxygenase 1 Homo sapiens 16-20 28120861-5 2017 CNT exposure activates an oxidative stress-dependent production of iron via Nrf2 nuclear translocation, Ferritin H and Heme oxygenase 1 translation. Iron 67-71 heme oxygenase 1 Homo sapiens 119-135 28503569-7 2017 These results indicate that TNFRI-Fc and hHO-1 overexpression may apparently induce free iron in the liver and exert oxidative stress by enhancing reactive oxygen species production and block normal postneonatal liver metabolism. Iron 89-93 heme oxygenase 1 Homo sapiens 41-46 28243792-0 2017 HMOX1 as a marker of iron excess-induced adipose tissue dysfunction, affecting glucose uptake and respiratory capacity in human adipocytes. Iron 21-25 heme oxygenase 1 Homo sapiens 0-5 28243792-2 2017 Here, we aimed to investigate the possible role of haem oxygenase 1 (HMOX1) in iron excess-induced adipose tissue dysfunction. Iron 79-83 heme oxygenase 1 Homo sapiens 51-67 28243792-2 2017 Here, we aimed to investigate the possible role of haem oxygenase 1 (HMOX1) in iron excess-induced adipose tissue dysfunction. Iron 79-83 heme oxygenase 1 Homo sapiens 69-74 28243792-5 2017 RESULTS: Adipose tissue HMOX1 was increased in obese participants (p = 0.01) and positively associated with obesity-related metabolic disturbances, and markers of iron accumulation, inflammation and oxidative stress (p < 0.01). Iron 163-167 heme oxygenase 1 Homo sapiens 24-29 28243792-10 2017 In human adipocytes, iron excess and inflammation led to increased HMOX1 mRNA levels. Iron 21-25 heme oxygenase 1 Homo sapiens 67-72 28243792-11 2017 HMOX1 induction (by haem arginate [hemin] administration), resulted in a significant reduction of mitochondrial respiratory capacity (including basal respiration and spare respiratory capacity), glucose uptake and adipogenesis in parallel with increased expression of inflammatory- and iron excess-related genes. Iron 286-290 heme oxygenase 1 Homo sapiens 0-5 28243792-12 2017 CONCLUSIONS/INTERPRETATION: HMOX1 is an important marker of iron excess-induced adipose tissue dysfunction and metabolic disturbances in human obesity. Iron 60-64 heme oxygenase 1 Homo sapiens 28-33 28139396-7 2017 These beneficial effects of HO-1 induction during AKI are mediated in part by the by-products of the HO reaction (iron, carbon monoxide, and bile pigments). Iron 114-118 heme oxygenase 1 Homo sapiens 28-32 27908781-3 2017 To elucidate the mechanisms involved, here we assess whether the HO-1 downstream metabolites biliverdin (BV) and/or iron mediate the HO-1 antiviral effect. Iron 116-120 heme oxygenase 1 Homo sapiens 133-137 26758041-3 2016 Using double immunofluorescence and sequential iron and immunohistochemistry staining, we showed that marrow iron colocalizes with HO1 and H-ferritin to CD163 + macrophages. Iron 109-113 heme oxygenase 1 Homo sapiens 131-134 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Iron 126-138 heme oxygenase 1 Homo sapiens 46-51 26758041-1 2016 Iron overload and transfusion dependance portend poor risk in myelodysplastic syndromes (MDS); bone marrow macrophages store iron and limit oxidative damage through heme oxygenase-1 (HO1). Iron 0-4 heme oxygenase 1 Homo sapiens 183-186 27142241-5 2016 Many nuclear processes are influenced by a spatial switch involving the proteins {KPNA2, KPNB1, PCNA, PTMA, SET} and heme/iron proteins HMOX1 and FTH1. Iron 122-126 heme oxygenase 1 Homo sapiens 136-141 26758041-1 2016 Iron overload and transfusion dependance portend poor risk in myelodysplastic syndromes (MDS); bone marrow macrophages store iron and limit oxidative damage through heme oxygenase-1 (HO1). Iron 125-129 heme oxygenase 1 Homo sapiens 183-186 27283533-4 2016 Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron. Iron 316-320 heme oxygenase 1 Homo sapiens 170-186 27283533-4 2016 Although the antioxidant and heat-shock proteins are included in this category, one enzyme that has received a great deal of attention as a master protective sentinel is heme oxygenase-1 (HO-1), the rate-limiting step in the catabolism of heme into the bioactive signaling molecules carbon monoxide, biliverdin, and iron. Iron 316-320 heme oxygenase 1 Homo sapiens 188-192 26166253-2 2016 HO-1, a cellular stress protein, serves a vital metabolic function as the rate-limiting step in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin-IXalpha (BV), the latter which is converted to bilirubin-IXalpha (BR). Iron 154-158 heme oxygenase 1 Homo sapiens 0-4 27198537-2 2016 After ICH, overproduction of iron associated with induction of heme oxygenase-1 (HO-1) in brain was observed. Iron 29-33 heme oxygenase 1 Homo sapiens 63-79 27198537-2 2016 After ICH, overproduction of iron associated with induction of heme oxygenase-1 (HO-1) in brain was observed. Iron 29-33 heme oxygenase 1 Homo sapiens 81-85 27198537-11 2016 These findings open up the prospect for male-specific neuroprotection targeting HO-1 suppression for patients suffering from striatal iron overload. Iron 134-138 heme oxygenase 1 Homo sapiens 80-84 28124024-0 2016 Iron Supplementation Alters Heme and Heme Oxygenase 1 (HO-1) Levels In Pregnant Women in Ghana. Iron 0-4 heme oxygenase 1 Homo sapiens 37-53 28124024-0 2016 Iron Supplementation Alters Heme and Heme Oxygenase 1 (HO-1) Levels In Pregnant Women in Ghana. Iron 0-4 heme oxygenase 1 Homo sapiens 55-59 28124024-4 2016 We hypothesized that pregnant women with malaria who took iron supplements will have higher levels of Heme/HO-1 than those who did not take iron supplements. Iron 58-62 heme oxygenase 1 Homo sapiens 107-111 26945724-0 2016 Iron depletion in HCT116 cells diminishes the upregulatory effect of phenethyl isothiocyanate on heme oxygenase-1. Iron 0-4 heme oxygenase 1 Homo sapiens 97-113 26945724-3 2016 Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC). Iron 51-55 heme oxygenase 1 Homo sapiens 113-129 26945724-3 2016 Herein, the objective was to ascertain if adequate iron is needed for enabling HCT116 cells to optimally express heme oxygenase-1 (HO-1) when induced by phenethyl isothiocyanate (PEITC). Iron 51-55 heme oxygenase 1 Homo sapiens 131-135 26945724-10 2016 Collectively, the results imply that the HO-1 upregulation by PEITC involves an iron-dependent, oxidant signaling pathway. Iron 80-84 heme oxygenase 1 Homo sapiens 41-45 26945724-11 2016 Therefore, it is concluded that ample iron is required to enable PEITC to fully upregulate HO-1 expression in HCT116 cells. Iron 38-42 heme oxygenase 1 Homo sapiens 91-95 26834769-2 2015 Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)). Iron 138-142 heme oxygenase 1 Homo sapiens 18-22 26834769-2 2015 Heme oxygenase-1 (HO-1) is known as a rate-liming enzyme in the degradation of heme to biliverdin IXalpha, carbon monoxide (CO), and free iron ions (Fe(2+)). Iron 149-151 heme oxygenase 1 Homo sapiens 18-22 26652036-1 2016 The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Iron 109-111 heme oxygenase 1 Homo sapiens 42-45 26423448-1 2015 The phenomenon that heme oxygenase-1 (HO-1) protects cell from injury yet its enzymatic product, iron, may facilitate generation of free radical has been long puzzling. Iron 97-101 heme oxygenase 1 Homo sapiens 20-36 26423448-1 2015 The phenomenon that heme oxygenase-1 (HO-1) protects cell from injury yet its enzymatic product, iron, may facilitate generation of free radical has been long puzzling. Iron 97-101 heme oxygenase 1 Homo sapiens 38-42 26423448-6 2015 RNA interference of HO-1 makes the cell more susceptible to hydrogen peroxide, which can be rescued by forced expression of wild-type FHC but not mutants that lose the capacity of iron storage and ferroxidase activity. Iron 180-184 heme oxygenase 1 Homo sapiens 20-24 26432957-5 2015 HO-1 degrades heme to biliverdin, carbon monoxide (CO) and free iron. Iron 64-68 heme oxygenase 1 Homo sapiens 0-4 26405158-11 2015 Thus, HO-1 is an essential enzyme for iron-dependent lipid peroxidation during ferroptotic cell death. Iron 38-42 heme oxygenase 1 Homo sapiens 6-10 26392237-2 2015 Out of three by-products of HO-1 activity, biliverdin, iron ions and carbon monoxide (CO), the latter was mostly shown to mediate many beneficial HO-1 effects, including protection against oxidative injury, regulation of apoptosis, modulation of inflammation as well as contribution to angiogenesis. Iron 55-59 heme oxygenase 1 Homo sapiens 146-150 26929573-7 2015 CONCLUSION: The present study demonstrated for the first time that the FE fraction from clove could confer UV-B protection probably through the Nrf2-ARE pathway, which included the down-regulation of Nrf2 and HO-1. Iron 71-73 heme oxygenase 1 Homo sapiens 209-213 26270345-3 2015 However, it appears that the toxic effects of heme are exerted by "loose" (probably intralysosomal) iron because cytotoxic effects of heme are lessened by pre-incubation of HO-1 deficient cells with desferrioxamine (which localizes preferentially in the lysosomal compartment). Iron 100-104 heme oxygenase 1 Homo sapiens 173-177 25574604-2 2015 We wanted to evaluate whether a functional polymorphism in the HMOX1 gene encoding heme oxygenase modifies risk of CRC or interacts with diet or lifestyle factors because this would identify heme or heme iron as a risk factor of CRC. Iron 204-208 heme oxygenase 1 Homo sapiens 63-68 25820186-1 2015 BACKGROUND: Over-expression of the heme-degrading enzyme, heme oxygenase-1 (HO-1) promotes iron deposition, mitochondrial damage, and autophagy in astrocytes and enhances the vulnerability of nearby neuronal constituents to oxidative injury. Iron 91-95 heme oxygenase 1 Homo sapiens 58-74 25820186-1 2015 BACKGROUND: Over-expression of the heme-degrading enzyme, heme oxygenase-1 (HO-1) promotes iron deposition, mitochondrial damage, and autophagy in astrocytes and enhances the vulnerability of nearby neuronal constituents to oxidative injury. Iron 91-95 heme oxygenase 1 Homo sapiens 76-80 26595496-2 2015 Heme oxygenase-1(HO-1) metabolizes heme into biliverdin, bilirubin, carbon monoxide, and iron, our recent study showed that serum level of HO-1 was increased in stroke patients, yet the association of HO-1 level with risk of intracerebral hemorrhage (ICH) is poorly known. Iron 89-93 heme oxygenase 1 Homo sapiens 0-16 25761244-1 2015 Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin. Iron 90-94 heme oxygenase 1 Homo sapiens 0-16 25885228-1 2015 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells. Iron 117-121 heme oxygenase 1 Homo sapiens 0-16 25885228-1 2015 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme catalyzing oxidative degradation of cellular heme to liberate free iron, carbon monoxide (CO) and biliverdin in mammalian cells. Iron 117-121 heme oxygenase 1 Homo sapiens 18-22 25761244-1 2015 Heme oxygenase-1 (HO-1) is a 32 kDa protein which catalyzes the breakdown of heme to free iron, carbon monoxide and biliverdin. Iron 90-94 heme oxygenase 1 Homo sapiens 18-22 25761244-3 2015 In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial iron sequestration and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure documented in Alzheimer disease, Parkinson disease and certain neurodevelopmental conditions. Iron 67-71 heme oxygenase 1 Homo sapiens 25-29 25761244-3 2015 In "stressed" astroglia, HO-1 hyperactivity promotes mitochondrial iron sequestration and macroautophagy and may thereby contribute to the pathological iron deposition and bioenergetic failure documented in Alzheimer disease, Parkinson disease and certain neurodevelopmental conditions. Iron 152-156 heme oxygenase 1 Homo sapiens 25-29 25175370-8 2014 In addition, the inhibition of HO-1 activity with the iron chelator, desferrioxamine (DFO), or HO-1 siRNA increased cilostazol-induced chondrocyte senescence. Iron 54-58 heme oxygenase 1 Homo sapiens 31-35 25111043-4 2014 Induction of the glial HMOX1 gene may lead to pathological brain iron deposition, intracellular oxidative damage, and bioenergetic failure in AD and other human CNS disorders such as PD and MS. Iron 65-69 heme oxygenase 1 Homo sapiens 23-28 25473172-9 2014 Ribavirin-induced hemolysis floods the hepatocytes and KCs with heme, which is metabolized and detoxified by heme oxygenase-1 (HMOX1) to carbon monoxide (CO), biliverdin and free iron (which induces ferritin). Iron 179-183 heme oxygenase 1 Homo sapiens 127-132 25744452-1 2015 Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions. Iron 97-101 heme oxygenase 1 Homo sapiens 0-16 25744452-1 2015 Heme oxygenase-1 (HO-1) catabolizes the degradation of heme into bilirubin, carbon monoxide, and iron ions. Iron 97-101 heme oxygenase 1 Homo sapiens 18-22 25241054-1 2014 Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin. Iron 132-136 heme oxygenase 1 Homo sapiens 0-16 25241054-1 2014 Heme oxygenase-1 (HO-1) catalyzes the first and rate-limiting enzymatic step of heme degradation and produces carbon monoxide, free iron, and biliverdin. Iron 132-136 heme oxygenase 1 Homo sapiens 18-22 24954650-7 2014 HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO). Iron 37-41 heme oxygenase 1 Homo sapiens 0-4 25355252-5 2014 Compared with the control group, the serum HO-1 was significantly increased at 6, 12, 24, 48 h after the heart valve replacement surgery in both the RIPerC and RIPostC groups (P<0.05); the SCr, BUN, urinary NGAL and serum iron values were decreased at 6, 12, 24, 48 h after the heart valve replacement surgery in both the RIPerC and RIPostC groups (P>0.05). Iron 225-229 heme oxygenase 1 Homo sapiens 43-47 24732176-3 2014 Such investigation could be important, as iron and carbon monoxide are two of the products of heme catabolism via heme oxygenase-1, an enzyme upregulated in a variety of disease states associated with thrombophilia. Iron 42-46 heme oxygenase 1 Homo sapiens 114-130 24183966-8 2014 HO-1 may also contribute to the iron accumulation in neurons, but its mechanism needs to be further investigated. Iron 32-36 heme oxygenase 1 Homo sapiens 0-4 24568186-8 2014 We speculated that iron, a by-product of HO-1-catalyzed reactions, could mediate 15d-PGJ2-induced p53 expression. Iron 19-23 heme oxygenase 1 Homo sapiens 41-45 24568186-10 2014 Iron released from heme by HO-1 activity is mostly in the Fe(2+) form. Iron 0-4 heme oxygenase 1 Homo sapiens 27-31 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Iron 122-126 heme oxygenase 1 Homo sapiens 31-35 25762501-7 2014 We also show that ER stress combined with inflammation synergistically upregulated the expression of the iron carrier protein NGAL and the stress-inducible heme degrading enzyme heme oxygenase-1 (HO-1) leading to iron liberation. Iron 213-217 heme oxygenase 1 Homo sapiens 178-194 24275768-1 2014 PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide. Iron 187-191 heme oxygenase 1 Homo sapiens 70-86 24275768-1 2014 PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide. Iron 187-191 heme oxygenase 1 Homo sapiens 88-92