PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23840483-4 2013 Since heme molecules are essential for the NADPH oxidase maturation and activity, we therefore investigated the consequences of the modulation of Heme oxygenase-1 (HO-1), the limiting enzyme in heme catabolism, on the IL-1beta signaling pathway and more specifically on Nox4 activity. Heme 6-10 heme oxygenase 1 Homo sapiens 164-168 23840483-8 2013 Therefore, the downregulation of Nox4 activity by HO-1 induction appeared to be mediated by carbon monoxide (CO) generated from the heme degradation process. Heme 132-136 heme oxygenase 1 Homo sapiens 50-54 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. Heme 128-132 heme oxygenase 1 Homo sapiens 18-22 23536693-1 2013 Heme oxygenase-1 (HO-1) is a stress-inducible rate-limiting enzyme in heme degradation that confers cytoprotection against oxidative injury and performs a vital function in the maintenance of cell hemostasis. Heme 70-74 heme oxygenase 1 Homo sapiens 0-16 23536693-1 2013 Heme oxygenase-1 (HO-1) is a stress-inducible rate-limiting enzyme in heme degradation that confers cytoprotection against oxidative injury and performs a vital function in the maintenance of cell hemostasis. Heme 70-74 heme oxygenase 1 Homo sapiens 18-22 23583009-7 2013 Ethanol-stimulated (100mM) CYP2E1 upregulation was suppressed by quercetin but further enhanced by HO-1 inhibition with resultant heme accumulation. Heme 130-134 heme oxygenase 1 Homo sapiens 99-103 25506596-6 2013 Heme also induces a cytoprotective response that includes Nrf2 responsive genes such as heme oxygenase-1, ferritin, haptoglobin, hemopexin, and other antioxidant response genes. Heme 0-4 heme oxygenase 1 Homo sapiens 88-104 23538684-4 2013 RESULTS: Changes in mRNA levels were most numerous and striking at 6 h after heme treatment but were similar and still numerous at 24 h. After 6 h of heme exposure, the increase in heme oxygenase 1 gene expression was 60-fold by mRNA and 88-fold by quantitative reverse transcription-polymerase chain reaction. Heme 77-81 heme oxygenase 1 Homo sapiens 181-197 23538684-4 2013 RESULTS: Changes in mRNA levels were most numerous and striking at 6 h after heme treatment but were similar and still numerous at 24 h. After 6 h of heme exposure, the increase in heme oxygenase 1 gene expression was 60-fold by mRNA and 88-fold by quantitative reverse transcription-polymerase chain reaction. Heme 150-154 heme oxygenase 1 Homo sapiens 181-197 23068042-0 2013 Development of a heme sensor using fluorescently labeled heme oxygenase-1. Heme 17-21 heme oxygenase 1 Homo sapiens 57-73 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 15-19 heme oxygenase 1 Homo sapiens 98-114 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 15-19 heme oxygenase 1 Homo sapiens 116-120 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 58-62 heme oxygenase 1 Homo sapiens 98-114 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 58-62 heme oxygenase 1 Homo sapiens 116-120 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 58-62 heme oxygenase 1 Homo sapiens 98-114 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 58-62 heme oxygenase 1 Homo sapiens 116-120 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 58-62 heme oxygenase 1 Homo sapiens 98-114 23068042-2 2013 To detect free heme at low concentrations, we developed a heme sensor using fluorescently labeled heme oxygenase-1 (HO-1), an enzyme that catalyzes oxidative heme degradation and has a high affinity for heme. Heme 58-62 heme oxygenase 1 Homo sapiens 116-120 23068042-4 2013 Each of the three fluorescently labeled HO-1s exhibits a 1:1 binding stoichiometry and an absorption spectrum similar to that of the heme complex of the wild-type HO-1. Heme 133-137 heme oxygenase 1 Homo sapiens 40-44 23068042-5 2013 Titration of the labeled proteins with hemin resulted in fluorescence quenching in a hemin concentration-dependent manner, presumably due to an energy transfer from the fluorophore to the heme bound to HO-1. Heme 188-192 heme oxygenase 1 Homo sapiens 202-206 23092328-9 2013 Heme-induced cell death was significantly attenuated when cells overexpressed HO-1, BCRP, or both. Heme 0-4 heme oxygenase 1 Homo sapiens 78-82 23092328-11 2013 Also cells treated with the anti-oxidants N-acetylcysteine or HO-effector molecule bilirubin showed protection against heme insults, which may explain the increased protection by HO-1 compared to BCRP. Heme 119-123 heme oxygenase 1 Homo sapiens 179-183 23092328-12 2013 In conclusion, both HO-1 and BCRP protect against heme-induced toxicity and may thus form novel therapeutic targets for heme-mediated pathologies. Heme 50-54 heme oxygenase 1 Homo sapiens 20-24 23092328-12 2013 In conclusion, both HO-1 and BCRP protect against heme-induced toxicity and may thus form novel therapeutic targets for heme-mediated pathologies. Heme 120-124 heme oxygenase 1 Homo sapiens 20-24 23103292-1 2013 Heme oxygenase (HO)-1, the inducible isoform of the first and rate-limiting enzyme of heme degradation, affords anti-inflammatory protection via its cell-type-specific effects in endothelial cells (ECs). Heme 86-90 heme oxygenase 1 Homo sapiens 0-21 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. Heme 59-63 heme oxygenase 1 Homo sapiens 77-81 23403148-6 2013 These collective actions of the heme breakdown metabolites generated by HO-1 offer protection against cytotoxicity, inflammation, hypoxia and other forms of cellular stress that are central to the pathogenesis of sPE. Heme 32-36 heme oxygenase 1 Homo sapiens 72-76 23026155-2 2013 The intracellular levels of CO can increase under stressful conditions following the induction of HO-1 (heme oxygnase-1), a ubiquitous enzyme responsible for the catabolism of heme. Heme 104-108 heme oxygenase 1 Homo sapiens 98-102 23720291-6 2013 The rate-controlling step of heme breakdown is catalyzed by heme oxygenase (HMOX), of which there are two isoforms, called HMOX1 and HMOX2. Heme 29-33 heme oxygenase 1 Homo sapiens 123-128 23092328-0 2013 Heme Oxygenase-1 and breast cancer resistance protein protect against heme-induced toxicity. Heme 70-74 heme oxygenase 1 Homo sapiens 0-16 23092328-5 2013 We postulated that overexpression of Heme Oxygenase-1 (HO-1) and Breast Cancer Resistance Protein (BCRP) would protect against heme-induced cytotoxicity. Heme 127-131 heme oxygenase 1 Homo sapiens 37-53 23092328-5 2013 We postulated that overexpression of Heme Oxygenase-1 (HO-1) and Breast Cancer Resistance Protein (BCRP) would protect against heme-induced cytotoxicity. Heme 127-131 heme oxygenase 1 Homo sapiens 55-59 23536765-2 2013 Since the heme catabolic pathway plays an important role in antioxidant protection, we attempted to assess the gene expression of key enzymes of heme catabolism, heme oxygenase 1 (HMOX1), heme oxygenase 2 (HMOX2), and biliverdin reductase A (BLVRA) in the liver and peripheral blood leukocytes (PBL) of patients chronically infected with HCV. Heme 10-14 heme oxygenase 1 Homo sapiens 162-178 23536765-2 2013 Since the heme catabolic pathway plays an important role in antioxidant protection, we attempted to assess the gene expression of key enzymes of heme catabolism, heme oxygenase 1 (HMOX1), heme oxygenase 2 (HMOX2), and biliverdin reductase A (BLVRA) in the liver and peripheral blood leukocytes (PBL) of patients chronically infected with HCV. Heme 10-14 heme oxygenase 1 Homo sapiens 180-185 22750196-4 2012 Induction of HO-1 during chronic hypoxia is necessary for the continued breakdown of heme for the enhanced production of hemoglobin and the increased respiratory and sympathetic responses. Heme 85-89 heme oxygenase 1 Homo sapiens 13-17 23171578-2 2012 CO-RMs containing transition metal carbonyls were initially implemented to mimic the function of heme oxygenase-1 (HMOX1), a stress inducible defensive protein that degrades heme to CO and biliverdin leading to anti-oxidant and anti-inflammatory actions. Heme 97-101 heme oxygenase 1 Homo sapiens 115-120 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. Heme 66-70 heme oxygenase 1 Homo sapiens 0-4 23874015-6 2013 The beneficial effects of HO-1 expression are not merely due to heme degradation but are also attributed to the cytoprotective properties of the byproducts of the reaction. Heme 64-68 heme oxygenase 1 Homo sapiens 26-30 22882835-4 2012 The binding of the most active compound 11 with heme or heme-conjugated human heme oxygenase-1 was also examined by spectral analyses. Heme 56-60 heme oxygenase 1 Homo sapiens 78-94 23100518-2 2012 This acquired neutrophil dysfunction is a consequence of induction of the cytoprotective, heme-degrading enzyme heme oxygenase-1 (HO-1) in neutrophil progenitors in bone marrow. Heme 90-94 heme oxygenase 1 Homo sapiens 112-128 23100518-2 2012 This acquired neutrophil dysfunction is a consequence of induction of the cytoprotective, heme-degrading enzyme heme oxygenase-1 (HO-1) in neutrophil progenitors in bone marrow. Heme 90-94 heme oxygenase 1 Homo sapiens 130-134 22419571-1 2012 Heme-oxygenase 1 is an endoplasmic reticulum-anchored enzyme that breaks down heme into iron, carbon monoxide and biliverdin. Heme 78-82 heme oxygenase 1 Homo sapiens 0-16 22965812-2 2012 The expression of heme oxygenase-1 (HO-1), the rate-limiting enzyme involved in heme degradation, correlates well with the severity of psoriasis, and is a heritable trait. Heme 18-22 heme oxygenase 1 Homo sapiens 36-40 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. Heme 6-10 heme oxygenase 1 Homo sapiens 31-44 22777293-4 2012 SUMMARY: Treatments based on direct heme-mimetics or other agonists of this pathway have enormous potential for linked antioxidant protection via heme oxygenase 1 and reduced foam cell formation via liver X receptor, a potent combination for treating atherosclerosis. Heme 36-40 heme oxygenase 1 Homo sapiens 146-162 22966170-2 2012 Heme oxygenase-1 (gene HMOX1; protein HO-1) is the inducible, rate-limiting enzyme in the catabolism of heme and might attenuate the severity of outcomes from vaso-occlusive and hemolytic crises. Heme 104-108 heme oxygenase 1 Homo sapiens 0-16 22966170-2 2012 Heme oxygenase-1 (gene HMOX1; protein HO-1) is the inducible, rate-limiting enzyme in the catabolism of heme and might attenuate the severity of outcomes from vaso-occlusive and hemolytic crises. Heme 104-108 heme oxygenase 1 Homo sapiens 23-28 22954673-4 2012 Additionally, heme activates redox-sensitive proliferation-related signaling routes, such as mitogen activated protein kinase (MAPK) and NF-kappaB, and induces heme oxygenase-1 (HO-1) expression. Heme 14-18 heme oxygenase 1 Homo sapiens 160-176 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. Heme 62-66 heme oxygenase 1 Homo sapiens 20-24 22836558-7 2012 Free Hb binds to haptoglobin (Hp) and once Hp-Hb complex is endocytosed by CD163, liberated heme is converted into less toxic compounds by heme oxygenase-1. Heme 92-96 heme oxygenase 1 Homo sapiens 139-155 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). Heme 99-103 heme oxygenase 1 Homo sapiens 14-30 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. Heme 36-40 heme oxygenase 1 Homo sapiens 0-16 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. Heme 64-68 heme oxygenase 1 Homo sapiens 82-86 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. Heme 36-40 heme oxygenase 1 Homo sapiens 18-22 22593583-2 2012 Many cancer cells constitutively express heme oxygenase-1 (HO-1), which catabolizes heme to generate biliverdin, Fe(2+), and carbon monoxide (CO). Heme 41-45 heme oxygenase 1 Homo sapiens 59-63 22579918-2 2012 Sustained induction of heme oxygenase-1 (HO-1) in nonerythroid cells plays a key role in many pathological processes, yet the effect of long-term HO-1 expression on cellular iron metabolism in the absence of exogenous heme is poorly understood. Heme 23-27 heme oxygenase 1 Homo sapiens 41-45 22579918-3 2012 Here we report that in a model nonerythroid cell, both transient and stable HO-1 expression increased heme oxygenase activity, but total cellular heme content was decreased only with transient enzyme expression. Heme 102-106 heme oxygenase 1 Homo sapiens 76-80 22579918-4 2012 Sustained HO-1 activity increased the expression of both the mitochondrial iron importer mitoferrin-2 and the rate-limiting enzyme in heme synthesis, aminolevulinate synthase-1, and it augmented the mitochondrial content of heme. Heme 134-138 heme oxygenase 1 Homo sapiens 10-14 22579918-4 2012 Sustained HO-1 activity increased the expression of both the mitochondrial iron importer mitoferrin-2 and the rate-limiting enzyme in heme synthesis, aminolevulinate synthase-1, and it augmented the mitochondrial content of heme. Heme 224-228 heme oxygenase 1 Homo sapiens 10-14 22503972-4 2012 Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein. Heme 32-36 heme oxygenase 1 Homo sapiens 0-16 22586396-7 2012 Heme is degraded by heme oxygenase (HO) that exists as two isoforms: inducible HO-1 and constitutively expressed HO-2. Heme 0-4 heme oxygenase 1 Homo sapiens 79-83 22271370-2 2012 Heme oxygenase (HO)-1, a rate-limiting enzyme of heme degradation, plays a protective role against oxidative stress. Heme 49-53 heme oxygenase 1 Homo sapiens 0-21 22394342-6 2012 Due to the cumulative effects of HO-1 on heme catabolism and the generation of biologically active downstream products, induction of HO-1 might serve as a protective mechanism against oxidative stress and inflammation-induced injury. Heme 41-45 heme oxygenase 1 Homo sapiens 33-37 22394342-6 2012 Due to the cumulative effects of HO-1 on heme catabolism and the generation of biologically active downstream products, induction of HO-1 might serve as a protective mechanism against oxidative stress and inflammation-induced injury. Heme 41-45 heme oxygenase 1 Homo sapiens 133-137 22503972-4 2012 Heme oxygenase 1 (HO1) degrades heme to biliverdin, carbon monoxide and free iron, and is a stress-responsive protein. Heme 32-36 heme oxygenase 1 Homo sapiens 18-21 22503972-10 2012 Taken together, our findings point to three novel functions of STC2, and suggest that STC2 interacts with HO1 to form a eukaryotic "stressosome" involved in the degradation of heme. Heme 176-180 heme oxygenase 1 Homo sapiens 106-109 21725851-1 2012 Heme oxygenase-1 (HO-1) which is a rate-limiting enzyme in heme degradation processes shows a dinucleotide GT repeat in the promoter that alters the level of gene transcription. Heme 59-63 heme oxygenase 1 Homo sapiens 0-16 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. Heme 73-77 heme oxygenase 1 Homo sapiens 0-16 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. Heme 73-77 heme oxygenase 1 Homo sapiens 18-22 21725851-1 2012 Heme oxygenase-1 (HO-1) which is a rate-limiting enzyme in heme degradation processes shows a dinucleotide GT repeat in the promoter that alters the level of gene transcription. Heme 59-63 heme oxygenase 1 Homo sapiens 18-22 22037960-15 2012 These results suggest that HO-1-mediated heme breakdown is caused by I/R during LDLT, since it is associated with increased exhaled CO levels and liver damage. Heme 41-45 heme oxygenase 1 Homo sapiens 27-31 22200625-5 2012 Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin. Heme 102-106 heme oxygenase 1 Homo sapiens 0-16 22200625-5 2012 Heme oxygenase-1 (HO-1) is the inducible isoform of the first and rate-limiting enzyme which degrades heme into carbon monoxide, ferritin and bilirubin. Heme 102-106 heme oxygenase 1 Homo sapiens 18-22 21091076-3 2011 By degrading the oxidant heme and generating the antioxidant bilirubin and anti-inflammatory molecule carbon monoxide, HO-1 may protect cell from injury due to oxidative and pathological stress. Heme 25-29 heme oxygenase 1 Homo sapiens 119-123 22052915-4 2012 OBJECTIVE: This study aimed to define the key transcription factor(s) involved in HO-1 induction by heme. Heme 100-104 heme oxygenase 1 Homo sapiens 82-86 22052915-9 2012 Heme-induced HO-1 and LXR-beta were suppressed by knockdown of ATF-1, and HO-1 and LXR-beta were induced by ATF-1 transfection. Heme 0-4 heme oxygenase 1 Homo sapiens 13-17 22052915-9 2012 Heme-induced HO-1 and LXR-beta were suppressed by knockdown of ATF-1, and HO-1 and LXR-beta were induced by ATF-1 transfection. Heme 0-4 heme oxygenase 1 Homo sapiens 74-78 22052915-13 2012 CONCLUSIONS: These results show that ATF-1 mediates HO-1 induction by heme and drives macrophage adaptation to intraplaque hemorrhage. Heme 70-74 heme oxygenase 1 Homo sapiens 52-56 22438807-1 2012 Heme oxygenase 1 (HO-1) is an essential enzyme induced by heme and multiple stimuli associated with critical illness. Heme 58-62 heme oxygenase 1 Homo sapiens 0-16 22438807-1 2012 Heme oxygenase 1 (HO-1) is an essential enzyme induced by heme and multiple stimuli associated with critical illness. Heme 58-62 heme oxygenase 1 Homo sapiens 18-22 22438807-6 2012 Neutrophils were the main HO-1-expressing cells in peripheral blood, and HMOX1 mRNA expression was upregulated by heme-moieties of lysed erythrocytes. Heme 114-118 heme oxygenase 1 Homo sapiens 73-78 21868703-0 2011 Heme induces heme oxygenase 1 via Nrf2: role in the homeostatic macrophage response to intraplaque hemorrhage. Heme 0-4 heme oxygenase 1 Homo sapiens 13-29 21868703-7 2011 Challenge of macrophages with purified heme provoked nuclear translocation of Nrf2, and Nrf2 small interfering RNA resulted in significant inhibition of the ability of heme to induce HO-1 protein. Heme 39-43 heme oxygenase 1 Homo sapiens 183-187 21868703-7 2011 Challenge of macrophages with purified heme provoked nuclear translocation of Nrf2, and Nrf2 small interfering RNA resulted in significant inhibition of the ability of heme to induce HO-1 protein. Heme 168-172 heme oxygenase 1 Homo sapiens 183-187 22138245-10 2012 Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia. Heme 68-72 heme oxygenase 1 Homo sapiens 48-52 22138245-10 2012 Taken together with the biochemical function of HO-1 that catalyzes heme into CO and bilirubin, HO-1 expression may improve the circulation and compensate with oxidative tissue damages induced by hypoxia. Heme 68-72 heme oxygenase 1 Homo sapiens 96-100 22457802-2 2012 The inducible form of the enzyme heme oxygenase, HO-1, which conducts heme degradation, is absent in erythroblasts where hemoglobin (Hb) is synthesized. Heme 33-37 heme oxygenase 1 Homo sapiens 49-53 22457802-3 2012 Yet, the central macrophage, which retains high HO-1 activity, might be suitable to take over degradation of extra, harmful, Hb heme. Heme 128-132 heme oxygenase 1 Homo sapiens 48-52 21593686-8 2011 HO-1 activity was determined in microsomal fractions from HUVECs by monitoring the conversion of heme into bilirubin. Heme 97-101 heme oxygenase 1 Homo sapiens 0-4 21079975-10 2011 In cells overexpressing HO1, heme-Fe uptake and transepithelial Fe transport was higher than in controls. Heme 29-33 heme oxygenase 1 Homo sapiens 24-27 21079975-13 2011 In a high heme-Fe condition, HO1 is found near the plasma membrane. Heme 10-14 heme oxygenase 1 Homo sapiens 29-32 22088544-1 2011 BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron. Heme 68-72 heme oxygenase 1 Homo sapiens 12-28 22088544-1 2011 BACKGROUND: Heme oxygenase-1 (HO-1) is an enzyme, which catabolizes heme into carbon monoxide, biliverdin and free iron. Heme 68-72 heme oxygenase 1 Homo sapiens 30-34 21902835-2 2011 Heme oxygenase-1 (HMOX1) is an essential enzyme in heme catabolism that is induced by oxidative stress and may play a protective role as an antioxidant in the lung. Heme 51-55 heme oxygenase 1 Homo sapiens 0-16 21902835-2 2011 Heme oxygenase-1 (HMOX1) is an essential enzyme in heme catabolism that is induced by oxidative stress and may play a protective role as an antioxidant in the lung. Heme 51-55 heme oxygenase 1 Homo sapiens 18-23 21741353-1 2011 Genetic variations in POR, encoding NADPH-cytochrome P450 oxidoreductase (CYPOR), can diminish the function of numerous cytochromes P450, and also have the potential to block degradation of heme by heme oxygenase-1 (HO-1). Heme 190-194 heme oxygenase 1 Homo sapiens 198-214 21741353-1 2011 Genetic variations in POR, encoding NADPH-cytochrome P450 oxidoreductase (CYPOR), can diminish the function of numerous cytochromes P450, and also have the potential to block degradation of heme by heme oxygenase-1 (HO-1). Heme 190-194 heme oxygenase 1 Homo sapiens 216-220 21741353-6 2011 When mixed with WT CYPOR, only the Y181D CYPOR variant inhibited heme degradation by sequestering HO-1, whereas Y459H and V492E were unable to inhibit HO-1 activity suggesting that CYPOR variants might have differential binding affinities with redox partners. Heme 65-69 heme oxygenase 1 Homo sapiens 98-102 21079975-3 2011 Intracellularly, heme oxygenase-1 (HO1) participates in the cleavage of the heme ring producing biliverdin, CO and ferrous iron. Heme 17-21 heme oxygenase 1 Homo sapiens 35-38 21529713-5 2011 Carbon monoxide (CO), a byproduct of heme catabolism by HO-1, prevents further accumulation of circulating free heme after Plasmodium infection, suppressing the pathogenesis of ECM. Heme 37-41 heme oxygenase 1 Homo sapiens 56-60 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. Heme 93-97 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. Heme 93-97 heme oxygenase 1 Homo sapiens 18-22 21622183-4 2011 HO-1 represses inflammation by removing the pro-inflammatory molecule heme and by generating CO and the bile pigments, biliverdin and bilirubin. Heme 70-74 heme oxygenase 1 Homo sapiens 0-4 21693314-2 2011 MATERIALS AND METHODS: To increase the expression of HO-1, both donors and recipients were injected with heme through the abdomen before the operation. Heme 105-109 heme oxygenase 1 Homo sapiens 53-57 21529713-5 2011 Carbon monoxide (CO), a byproduct of heme catabolism by HO-1, prevents further accumulation of circulating free heme after Plasmodium infection, suppressing the pathogenesis of ECM. Heme 112-116 heme oxygenase 1 Homo sapiens 56-60 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. Heme 76-80 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). Heme 73-77 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. Heme 47-51 heme oxygenase 1 Homo sapiens 0-4 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). Heme 73-77 heme oxygenase 1 Homo sapiens 18-22 20563825-1 2011 Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders. Heme 78-82 heme oxygenase 1 Homo sapiens 0-16 20563825-1 2011 Heme oxygenase-1 (HO-1), a 32 kDa stress protein mediating the degradation of heme to ferrous iron, carbon monoxide and biliverdin/bilirubin, has been implicated in the pathogenesis of Alzheimer disease (AD) and other aging-related neurodegenerative disorders. Heme 78-82 heme oxygenase 1 Homo sapiens 18-22 21106538-1 2011 Heme oxygenase-1 (HO-1) enzyme plays a critical role in metabolizing the excess heme generated during hemolysis. Heme 80-84 heme oxygenase 1 Homo sapiens 0-16 21106538-1 2011 Heme oxygenase-1 (HO-1) enzyme plays a critical role in metabolizing the excess heme generated during hemolysis. Heme 80-84 heme oxygenase 1 Homo sapiens 18-22 21081499-1 2011 Heme oxygenase-1 (HO-1) degrades heme and protects cells from oxidative challenge. Heme 33-37 heme oxygenase 1 Homo sapiens 18-22 21081499-2 2011 This antioxidant activity is thought to result from the HO-1 enzymatic activity, manifested by a decrease in the concentration of the pro-oxidant substrate heme, and an increase in the antioxidant product bilirubin. Heme 156-160 heme oxygenase 1 Homo sapiens 56-60 22254194-3 2011 Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron. Heme 51-55 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. Heme 51-55 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. Heme 60-64 heme oxygenase 1 Homo sapiens 0-16 20561893-3 2011 METHODS: A PowerWave XS plate reader was used to monitor the absorbance (as a function of time) of heme bound to purified truncated human heme oxygenase-1 (hHO-1) in the individual wells of a standard 96-well plate (with or without the addition of a test compound). Heme 99-103 heme oxygenase 1 Homo sapiens 138-154 20561893-3 2011 METHODS: A PowerWave XS plate reader was used to monitor the absorbance (as a function of time) of heme bound to purified truncated human heme oxygenase-1 (hHO-1) in the individual wells of a standard 96-well plate (with or without the addition of a test compound). Heme 99-103 heme oxygenase 1 Homo sapiens 156-161 20561893-4 2011 The degradation of heme by heme oxygenase-1 was initiated using l-ascorbic acid, and the collected relevant absorbance data were analyzed by three different methods to calculate the percent control activity occurring in wells containing test compounds relative to that occurring in control wells with no test compound present. Heme 19-23 heme oxygenase 1 Homo sapiens 27-43 21088618-1 2011 Heme oxygenase-1 (HO-1) is a stress-induced enzyme that catalyses the oxidation of heme to biliverdin. Heme 83-87 heme oxygenase 1 Homo sapiens 0-16 21088618-1 2011 Heme oxygenase-1 (HO-1) is a stress-induced enzyme that catalyses the oxidation of heme to biliverdin. Heme 83-87 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. Heme 60-64 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. Heme 60-64 heme oxygenase 1 Homo sapiens 180-184 21765894-2 2011 Heme-oxygenase 1 (HO-1) is known to be the heme inducible isoform, whereas heme-oxygenase 2 (HO-2) is the constitutive enzyme. Heme 43-47 heme oxygenase 1 Homo sapiens 0-16 21765894-2 2011 Heme-oxygenase 1 (HO-1) is known to be the heme inducible isoform, whereas heme-oxygenase 2 (HO-2) is the constitutive enzyme. Heme 43-47 heme oxygenase 1 Homo sapiens 18-22 21182221-2 2010 Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide. Heme 77-81 heme oxygenase 1 Homo sapiens 0-16 21182221-2 2010 Heme oxygenase-1 (HO-1) is a powerful antioxidant enzyme which degrades free heme into biliverdin, free iron and carbon monoxide. Heme 77-81 heme oxygenase 1 Homo sapiens 18-22 20837117-6 2010 Importantly, Hg(2+) increased the expression of heme oxygenase-1 (HO-1), a rate limiting enzyme in heme degradation, which coincided with further decrease in the CYP1A1 catalytic activity levels. Heme 48-52 heme oxygenase 1 Homo sapiens 66-70 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. Heme 85-89 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. Heme 85-89 heme oxygenase 1 Homo sapiens 18-22 20643109-1 2010 Heme oxygenase (HO)-1 is the inducible isoform of the first and rate-limiting enzyme of heme degradation. Heme 88-92 heme oxygenase 1 Homo sapiens 0-21 20643109-4 2010 Beneficial protective effects of HO-1 in inflammation are not only mediated via enzymatic degradation of proinflammatory free heme, but also via production of the anti-inflammatory compounds bilirubin and carbon monoxide. Heme 126-130 heme oxygenase 1 Homo sapiens 33-37 20704546-1 2010 Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron. Heme 33-37 heme oxygenase 1 Homo sapiens 0-16 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. Heme 57-61 heme oxygenase 1 Homo sapiens 0-4 20704550-9 2010 Pharmacological induction of HO-1 by heme derivatives, dietary antioxidants, or currently available drugs, is a promising near-term approach, while HO-1 gene delivery is a long-term therapeutic goal. Heme 37-41 heme oxygenase 1 Homo sapiens 29-33 20704552-4 2010 HO-1 degrades heme to biliverdin-IXalpha, carbon monoxide (CO), and iron. Heme 14-18 heme oxygenase 1 Homo sapiens 0-4 20704546-1 2010 Heme oxygenase-1 (HO-1) degrades heme to carbon monoxide (CO), biliverdin, and ferrous iron. Heme 33-37 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. Heme 48-52 heme oxygenase 1 Homo sapiens 0-4 20704548-4 2010 In addition to the degradation of free heme, a pro-oxidant, HO-1 exerts anti-oxidant, anti-inflammatory and anti-apoptotic properties via its reaction products. Heme 39-43 heme oxygenase 1 Homo sapiens 60-64 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. Heme 45-49 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. Heme 45-49 heme oxygenase 1 Homo sapiens 18-22 20704549-6 2010 From the therapeutic side, the blood brain barrier represents an obstacle to directly modulate heme oxygenase activity, but drugs activating the transcription actor Nrf2, which have a very diverse molecular structure, may be good candidates to induce HO-1 in concert with other antioxidant and detoxification enzymes. Heme 95-99 heme oxygenase 1 Homo sapiens 251-255 20704550-1 2010 Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron. Heme 36-40 heme oxygenase 1 Homo sapiens 0-16 20704550-1 2010 Heme oxygenase-1 (HO-1) metabolizes heme to generate carbon monoxide (CO), biliverdin, and iron. Heme 36-40 heme oxygenase 1 Homo sapiens 18-22 21383490-3 2010 Heme-oxygenase-1 (HO-1) is a rate-limiting enzyme for heme breakdown. Heme 54-58 heme oxygenase 1 Homo sapiens 0-16 21383490-3 2010 Heme-oxygenase-1 (HO-1) is a rate-limiting enzyme for heme breakdown. Heme 54-58 heme oxygenase 1 Homo sapiens 18-22 21383490-4 2010 HO-1 breaks down heme to yield CO, iron and biliverdin. Heme 17-21 heme oxygenase 1 Homo sapiens 0-4 20594940-1 2010 Heme oxygenase (HO)-1, which is the inducible isoform of the rate-limiting enzyme of heme degradation, has potent antioxidant and anti-inflammatory effects and is an emerging therapeutic target for the treatment of cardiovascular disease. Heme 85-89 heme oxygenase 1 Homo sapiens 0-21 20732302-0 2010 Altered heme catabolism by heme oxygenase-1 caused by mutations in human NADPH cytochrome P450 reductase. Heme 8-12 heme oxygenase 1 Homo sapiens 27-43 20732302-1 2010 Human heme oxygenase-1 (HO-1) carries out heme catabolism supported by electrons supplied from the NADPH through NADPH P450 reductase (POR, CPR). Heme 6-10 heme oxygenase 1 Homo sapiens 24-28 20732302-4 2010 We used purified preparations of wild type and mutant human POR and in vitro reconstitution with purified HO-1 to measure heme degradation in a coupled assay using biliverdin reductase. Heme 122-126 heme oxygenase 1 Homo sapiens 106-110 20732302-5 2010 Here we show that mutations in POR found in patients may reduce HO-1 activity, potentially influencing heme catabolism in individuals carrying mutant POR alleles. Heme 103-107 heme oxygenase 1 Homo sapiens 64-68 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. Heme 17-21 heme oxygenase 1 Homo sapiens 37-41 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). Heme 108-112 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). Heme 108-112 heme oxygenase 1 Homo sapiens 18-22 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. Heme 55-59 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. Heme 55-59 heme oxygenase 1 Homo sapiens 18-22 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. Heme 91-95 heme oxygenase 1 Homo sapiens 145-149 20539916-3 2010 One of the proteins important for neovascularisation is heme oxygenase-1 (HO-1), an enzyme degrading heme. Heme 56-60 heme oxygenase 1 Homo sapiens 74-78 20502928-8 2010 These findings are consistent with the presence of a hydrogen-bonding network at the heme"s distal side within the active site of HO-2 with potentially significant differences from that observed in HO-1. Heme 85-89 heme oxygenase 1 Homo sapiens 198-202 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). Heme 88-92 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). Heme 88-92 heme oxygenase 1 Homo sapiens 30-34 20832528-1 2010 BACKGROUND: Heme oxygenase-1 (HO-1) is the enzyme that catabolizes heme into carbon monoxide, biliverdin, and free iron. Heme 67-71 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. Heme 67-71 heme oxygenase 1 Homo sapiens 30-34 20378845-5 2010 In the interactions between hemoglobin and atheroma lipids, hemoglobin and heme promote further lipid oxidation and subsequently endothelial reactions such as upregulation of heme oxygenase-1 and cytotoxicity to endothelium. Heme 75-79 heme oxygenase 1 Homo sapiens 175-191 20593496-1 2010 Heme oxygenase (HO)-1 is the inducible isoform of the first and rate-limiting enzyme of heme degradation. Heme 88-92 heme oxygenase 1 Homo sapiens 0-21 20155807-10 2010 Furthermore, 6-OHDA-induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO-1-catalyzed degradation of heme. Heme 129-133 heme oxygenase 1 Homo sapiens 99-103 20351094-1 2010 HO-1 (heme oxygenase-1) is an inducible microsomal enzyme that catalyzes the degradation of pro-oxidant heme. Heme 6-10 heme oxygenase 1 Homo sapiens 0-4 20518085-1 2010 Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron. Heme 43-47 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. Heme 43-47 heme oxygenase 1 Homo sapiens 18-22 20106603-4 2010 In this context, it has been shown that the rate limiting enzyme heme oxygenase I (HO-1), responsible for the catabolism of the free heme in the body, is an important resistance factor in malaria and is also important in the physiopathology of haemolytic diseases. Heme 65-69 heme oxygenase 1 Homo sapiens 83-87 20061555-5 2010 Inhibition of HIV-1 replication was associated with PKC-dependent induction of HO-1, a cytoprotective enzyme known to catabolize heme. Heme 129-133 heme oxygenase 1 Homo sapiens 79-83 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. Heme 58-62 heme oxygenase 1 Homo sapiens 0-31 20091384-1 2010 Heme oxygenase (HO)-1, a heme-degrading enzyme inducible by various stimuli, plays a key role in the regulation of inflammatory response in monocytes/macrophages. Heme 25-29 heme oxygenase 1 Homo sapiens 0-21 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. Heme 122-126 heme oxygenase 1 Homo sapiens 140-144 20020468-1 2010 Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin. Heme 139-143 heme oxygenase 1 Homo sapiens 0-16 20020468-1 2010 Heme-oxygenase-1 (HO-1), an important enzyme involved in vascular disease, transplantation, and inflammation, catalyzes the degradation of heme into carbon monoxide and biliverdin. Heme 139-143 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. Heme 48-52 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. Heme 48-52 heme oxygenase 1 Homo sapiens 18-22 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. Heme 117-121 heme oxygenase 1 Homo sapiens 0-16 19956091-1 2010 Heme oxygenase (HO)-1 degrades heme and protects against oxidative stress, but it has not been pharmacologically induced in humans. Heme 31-35 heme oxygenase 1 Homo sapiens 0-21 19797297-1 2010 HO-1 is the only inducible one of three isoenzymes that catalyzes the oxidative degradation of heme. Heme 95-99 heme oxygenase 1 Homo sapiens 0-4 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. Heme 117-121 heme oxygenase 1 Homo sapiens 18-22 19833168-1 2010 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by its substrate heme and diverse stimuli. Heme 78-82 heme oxygenase 1 Homo sapiens 0-16 19833168-1 2010 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme activated by its substrate heme and diverse stimuli. Heme 78-82 heme oxygenase 1 Homo sapiens 18-22 20184791-3 2010 Compared to HO-2, which is constitutively expressed, HO-1 is a stressresponsive protein that is highly induced by many agents, including cytokines, endotoxin, heavy metals, nitric oxide and its own substrate heme. Heme 208-212 heme oxygenase 1 Homo sapiens 53-57 19903769-3 2009 Heme oxygenase 1 (HO-1), the inducible isoform of the rate-limiting enzyme in heme degradation, counteracts oxidative and inflammatory damage. Heme 78-82 heme oxygenase 1 Homo sapiens 0-16 20062840-4 2010 Furthermore, a reduction of free heme levels led to a strong decrease in UVA-induced Nrf2 and HO-1 protein levels confirming a clear role for heme in the UV-mediated stress response. Heme 33-37 heme oxygenase 1 Homo sapiens 94-98 20062840-4 2010 Furthermore, a reduction of free heme levels led to a strong decrease in UVA-induced Nrf2 and HO-1 protein levels confirming a clear role for heme in the UV-mediated stress response. Heme 142-146 heme oxygenase 1 Homo sapiens 94-98 19952508-6 2009 HO-1 levels were increased by CdCl(2) (7.5 microM), heme (10, 100 microM), and stannic mesoporphyrin (SnMP) (10 microM), but were not changed by AAP, and were decreased by diclofenac. Heme 52-56 heme oxygenase 1 Homo sapiens 0-4 19903769-3 2009 Heme oxygenase 1 (HO-1), the inducible isoform of the rate-limiting enzyme in heme degradation, counteracts oxidative and inflammatory damage. Heme 78-82 heme oxygenase 1 Homo sapiens 18-22 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. Heme 72-76 heme oxygenase 1 Homo sapiens 0-4 19874266-2 2009 Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide. Heme 68-72 heme oxygenase 1 Homo sapiens 0-16 19874266-2 2009 Heme oxygenase-1 (HO-1) is a 32 kDa stress protein that catabolizes heme to biliverdin, free iron and carbon monoxide. Heme 68-72 heme oxygenase 1 Homo sapiens 18-22 19694439-8 2009 Steady-state activity assays showed that benzyl isocyanide was the most potent uncompetitive inhibitor with respect to heme with a KI = 0.15 microM for hHO-1. Heme 119-123 heme oxygenase 1 Homo sapiens 152-157 19686725-9 2009 These results suggest that this enhanced HO-1 expression through a combination of pathological state and pharmacological agent could be an effective strategy to improve the prognosis of heme- and oxidative stress-induced diseases, such as delayed cerebral vasospasm. Heme 186-190 heme oxygenase 1 Homo sapiens 41-45 19617398-1 2009 Heme oxygenase-1 (HO-1), a ubiquitous inducible stress-response protein, serves a major metabolic function in heme turnover. Heme 110-114 heme oxygenase 1 Homo sapiens 0-16 19617398-1 2009 Heme oxygenase-1 (HO-1), a ubiquitous inducible stress-response protein, serves a major metabolic function in heme turnover. Heme 110-114 heme oxygenase 1 Homo sapiens 18-22 19556236-1 2009 Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin. Heme 245-249 heme oxygenase 1 Homo sapiens 0-16 19556236-1 2009 Heme oxygenase-1 (HO-1), a stress-inducible enzyme anchored in the endoplasmic reticulum (ER) by a single transmembrane segment (TMS) located at the C terminus, interacts with NADPH cytochrome P450 reductase and biliverdin reductase to catalyze heme degradation to biliverdin and its metabolite, bilirubin. Heme 245-249 heme oxygenase 1 Homo sapiens 18-22 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. Heme 57-61 heme oxygenase 1 Homo sapiens 75-79 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. Heme 49-53 heme oxygenase 1 Homo sapiens 0-16 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. Heme 64-68 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. Heme 64-68 heme oxygenase 1 Homo sapiens 99-103 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. Heme 49-53 heme oxygenase 1 Homo sapiens 18-22 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. Heme 0-4 heme oxygenase 1 Homo sapiens 71-87 19039664-10 2009 A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX. Heme 71-75 heme oxygenase 1 Homo sapiens 178-183 19039664-10 2009 A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX. Heme 71-75 heme oxygenase 1 Homo sapiens 287-292 19039664-10 2009 A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX. Heme 111-115 heme oxygenase 1 Homo sapiens 178-183 19039664-10 2009 A model is presented in which copper endocytosis together with that of heme-HPX provides a means to facilitate heme export from HPX in the maturing endosomes: heme is needed for hmox1 transcription, while cytosolic copper and CCS1 provide a link for the known simultaneous regulation of hmox1 and mt1 by heme-HPX. Heme 111-115 heme oxygenase 1 Homo sapiens 287-292 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. Heme 0-4 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. Heme 52-56 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. Heme 52-56 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. Heme 52-56 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. Heme 52-56 heme oxygenase 1 Homo sapiens 89-94 19526463-3 2009 We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1. Heme 37-41 heme oxygenase 1 Homo sapiens 55-59 19526463-3 2009 We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1. Heme 87-91 heme oxygenase 1 Homo sapiens 37-53 19526463-3 2009 We hypothesize that arsenite induces heme oxygenase-1 (HO-1), which catabolizes CYP1A1 heme or cellular heme pools, thereby downregulating CYP1A1. Heme 87-91 heme oxygenase 1 Homo sapiens 55-59 19526463-7 2009 Together these findings demonstrate that a posttranslational mechanism involving decreases in the cellular heme pool by arsenite-induced HO-1 may contribute to arsenite-mediated downregulation of CYP1A1. Heme 107-111 heme oxygenase 1 Homo sapiens 137-141 19212657-1 2009 Human heme oxygenase-1 (hHO-1) is a rate-limiting enzyme in heme metabolism. Heme 6-10 heme oxygenase 1 Homo sapiens 24-29 19036700-1 2009 Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe). Heme 19-23 heme oxygenase 1 Homo sapiens 27-43 19135260-0 2009 Covalent heme attachment to the protein in human heme oxygenase-1 with selenocysteine replacing the His25 proximal iron ligand. Heme 9-13 heme oxygenase 1 Homo sapiens 49-65 19135260-5 2009 The heme-His25SeCys hHO-1 complex could be prepared by either (a) supplementing the overexpression medium with heme, or (b) reconstituting the purified apoprotein with heme. Heme 4-8 heme oxygenase 1 Homo sapiens 20-25 19135260-5 2009 The heme-His25SeCys hHO-1 complex could be prepared by either (a) supplementing the overexpression medium with heme, or (b) reconstituting the purified apoprotein with heme. Heme 111-115 heme oxygenase 1 Homo sapiens 20-25 19135260-11 2009 47 (2008) 3480-3482 ], indicate that a selenyl radical is formed in the hHO-1 His25SeCys mutant that adds to a heme vinyl group. Heme 111-115 heme oxygenase 1 Homo sapiens 72-77 19036700-1 2009 Catabolism of free heme by heme oxygenase-1 (HO-1) generates carbon monoxide, biliverdin, and free iron (Fe). Heme 19-23 heme oxygenase 1 Homo sapiens 45-49 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). Heme 63-67 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). Heme 130-134 heme oxygenase 1 Homo sapiens 0-21 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). Heme 76-80 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). Heme 76-80 heme oxygenase 1 Homo sapiens 18-22 19162549-3 2009 Here, we present a model for the beneficial actions of the products of heme degradation, and we discuss the potential clinical applications of enhancing the HO-1 system. Heme 71-75 heme oxygenase 1 Homo sapiens 157-161 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). Heme 63-67 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). Heme 63-67 heme oxygenase 1 Homo sapiens 157-161 19177185-3 2009 Cells counteract this by rapidly inducing the rate-limiting enzyme in heme breakdown, heme oxygenase-1 (HO-1), which is a low-molecular-weight stress protein. Heme 70-74 heme oxygenase 1 Homo sapiens 86-102 19177185-3 2009 Cells counteract this by rapidly inducing the rate-limiting enzyme in heme breakdown, heme oxygenase-1 (HO-1), which is a low-molecular-weight stress protein. Heme 70-74 heme oxygenase 1 Homo sapiens 104-108 19177185-4 2009 The enzymatic HO-1 reaction removes heme. Heme 36-40 heme oxygenase 1 Homo sapiens 14-18 18957281-3 2008 HO-1 is a key enzyme in physiological heme degradation. Heme 38-42 heme oxygenase 1 Homo sapiens 0-4 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. Heme 117-121 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. Heme 117-121 heme oxygenase 1 Homo sapiens 18-22 18528644-10 2008 Heme oxygenase 1 expression increased and DMT1 expression decreased with higher heme Fe concentrations in the media. Heme 80-84 heme oxygenase 1 Homo sapiens 0-16 18975324-1 2008 OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress. Heme 109-113 heme oxygenase 1 Homo sapiens 53-58 18975324-1 2008 OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress. Heme 109-113 heme oxygenase 1 Homo sapiens 131-147 18975324-1 2008 OBJECTIVE: The guanine-thymidine (GT)n repeat in the HMOX1 promoter determines the level of induction of the heme-degrading enzyme heme oxygenase 1 (HO-1), which protects against inflammatory and oxidative stress. Heme 109-113 heme oxygenase 1 Homo sapiens 149-153 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. Heme 58-62 heme oxygenase 1 Homo sapiens 19-35 18696091-12 2008 Both cell types biosynthesize HO-1 and ferritin in response to heme. Heme 63-67 heme oxygenase 1 Homo sapiens 30-34 18696091-14 2008 The persistence of HO-1 protein implies continuous exposure of CNS to free heme or an excessively sensitive transcriptional response of the HO-1 gene. Heme 75-79 heme oxygenase 1 Homo sapiens 19-23 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. Heme 38-42 heme oxygenase 1 Homo sapiens 0-16 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. Heme 201-205 heme oxygenase 1 Homo sapiens 0-16 18802114-1 2008 Heme oxygenase (HO)-1 is a stress-inducible rate-limiting enzyme in heme degradation that confers cytoprotection against oxidative injury and provides a vital function in maintaining tissue homeostasis. Heme 68-72 heme oxygenase 1 Homo sapiens 0-21 18657588-2 2008 In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1). Heme 17-21 heme oxygenase 1 Homo sapiens 101-117 18776993-2 2008 The HO-1 isozyme is induced by a variety of factors such as heat, heme, ischemia, and hydrogen peroxide. Heme 66-70 heme oxygenase 1 Homo sapiens 4-8 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. Heme 107-111 heme oxygenase 1 Homo sapiens 0-19 18786476-3 2008 Thus, the physiological induction of HO-1 may be an adaptive and beneficial response to several possibly noxious stimuli, including heme itself, suggesting a potentially autoprotective and autodefensive role in several pathophysiological states including acute coronary syndromes and stroke. Heme 132-136 heme oxygenase 1 Homo sapiens 37-41 18657588-2 2008 In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1). Heme 17-21 heme oxygenase 1 Homo sapiens 119-123 18657588-2 2008 In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1). Heme 43-47 heme oxygenase 1 Homo sapiens 101-117 18657588-2 2008 In the mammalian heme degradation process, heme is cleaved to biliverdin by the rate-limiting enzyme heme oxygenase-1 (HO-1). Heme 43-47 heme oxygenase 1 Homo sapiens 119-123 18331200-1 2008 Heme oxygenase-1 is the rate-limiting enzyme for the degradation of the prooxidant heme. Heme 83-87 heme oxygenase 1 Homo sapiens 0-16 18550526-2 2008 To prevent accumulation, the inducible enzyme heme oxygenase-1 (HMOX1) catalyzes degradation of heme. Heme 46-50 heme oxygenase 1 Homo sapiens 64-69 18550526-4 2008 Conversely, increased intracellular heme or sulfhydryl oxidation inactivate BACH1, permitting transcriptional induction of HMOX1. Heme 36-40 heme oxygenase 1 Homo sapiens 123-128 18550526-8 2008 The loss of BACH1 function in human keratinocytes results almost exclusively in HMOX1 induction, suggesting that BACH1 may function as a rheostat regulating levels of intracellular free heme. Heme 186-190 heme oxygenase 1 Homo sapiens 80-85 18487208-13 2008 Identification of an isoporphyrin intermediate in the catalytic sequence of hHO-1, the first such intermediate observed in hemoprotein catalysis, completes our understanding of the critical first step of heme oxidation. Heme 204-208 heme oxygenase 1 Homo sapiens 76-81 18487208-2 2008 Human heme oxygenase-1 (hHO-1) catalyzes the O2- and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron. Heme 6-10 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. Heme 109-113 heme oxygenase 1 Homo sapiens 0-4 18376820-0 2008 Selenolate complexes of CYP101 and the heme-bound hHO-1/H25A proximal cavity mutant. Heme 39-43 heme oxygenase 1 Homo sapiens 50-55 18376820-1 2008 Thiolate and selenolate complexes of CYP101 (P450cam) and the H25A proximal cavity mutant of heme-bound human heme oxygenase-1 (hHO-1) have been examined by UV-vis spectroscopy. Heme 93-97 heme oxygenase 1 Homo sapiens 110-126 18376820-1 2008 Thiolate and selenolate complexes of CYP101 (P450cam) and the H25A proximal cavity mutant of heme-bound human heme oxygenase-1 (hHO-1) have been examined by UV-vis spectroscopy. Heme 93-97 heme oxygenase 1 Homo sapiens 128-133 18376820-3 2008 Thiolate ligands also bound to the proximal side of the heme in the cavity created by the H25A mutation in hHO-1, giving a Soret absorption similar to that of the H25C hHO-1 mutant. Heme 56-60 heme oxygenase 1 Homo sapiens 107-112 18376820-3 2008 Thiolate ligands also bound to the proximal side of the heme in the cavity created by the H25A mutation in hHO-1, giving a Soret absorption similar to that of the H25C hHO-1 mutant. Heme 56-60 heme oxygenase 1 Homo sapiens 168-173 18545641-4 2008 The mechanism of protective actions of HO-1 has not been completely elucidated, but recent evidence suggests that one or more of heme metabolites can mediate the protective effects of HO-1. Heme 129-133 heme oxygenase 1 Homo sapiens 184-188 18048804-1 2008 Heme oxygenase-1 (HO-1) catalyzes the rate limiting reaction of heme metabolism and plays critical roles in resistance to oxidative stress and other cellular functions. Heme 64-68 heme oxygenase 1 Homo sapiens 0-16 18048804-1 2008 Heme oxygenase-1 (HO-1) catalyzes the rate limiting reaction of heme metabolism and plays critical roles in resistance to oxidative stress and other cellular functions. Heme 64-68 heme oxygenase 1 Homo sapiens 18-22 18381758-1 2008 The inducible protein heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to carbon monoxide (CO) and biliverdin, which play a concerted action in cytoprotection against oxidative stress and in the modulation of cell proliferation and differentiation. Heme 22-26 heme oxygenase 1 Homo sapiens 40-44 18286266-4 2008 Induction of HO-1 may confer protection by controlling intracellular levels of toxic heme, or by anti-inflammatory, anti-apoptotic, and blood flow-maintaining effects of its by-products biliverdin and CO. Heme 85-89 heme oxygenase 1 Homo sapiens 13-17 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. Heme 75-79 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. Heme 75-79 heme oxygenase 1 Homo sapiens 18-22 18174022-7 2008 Thus, PGD(2) may contribute to the maintenance of heme homeostasis in the brain by inducing HO-1 expression. Heme 50-54 heme oxygenase 1 Homo sapiens 92-96 18325350-1 2008 Heme oxygenase 1 (HO-1) is the first and rate-controlling enzyme in heme degradation. Heme 68-72 heme oxygenase 1 Homo sapiens 0-16 18178725-0 2008 Heme oxygenase-1 induction depletes heme and attenuates pulmonary artery relaxation and guanylate cyclase activation by nitric oxide. Heme 36-40 heme oxygenase 1 Homo sapiens 0-16 18178725-10 2008 These data suggest that increasing HO-1 activity depletes heme, and this is associated with an attenuation of pulmonary artery relaxation and sGC activation responses to NO. Heme 58-62 heme oxygenase 1 Homo sapiens 35-39 18325350-1 2008 Heme oxygenase 1 (HO-1) is the first and rate-controlling enzyme in heme degradation. Heme 68-72 heme oxygenase 1 Homo sapiens 18-22 17965015-2 2007 The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Heme 35-39 heme oxygenase 1 Homo sapiens 138-142 18215737-1 2008 The objective of this study was to determine whether heme oxygenase-1 (HO-1) or heme metabolites exert cytoprotective effects on interleukin-18-mediated endothelial cell (EC) death. Heme 53-57 heme oxygenase 1 Homo sapiens 71-75 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. Heme 112-116 heme oxygenase 1 Homo sapiens 63-67 18289072-1 2008 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme of ferroheme metabolic pathway, which has the functions of anti-oxidation, anti-inflammatory, anti-apoptosis and anti-smooth muscle hyperplasia. Heme 55-64 heme oxygenase 1 Homo sapiens 0-16 18289072-1 2008 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme of ferroheme metabolic pathway, which has the functions of anti-oxidation, anti-inflammatory, anti-apoptosis and anti-smooth muscle hyperplasia. Heme 55-64 heme oxygenase 1 Homo sapiens 18-22 18289074-1 2008 Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. Heme 83-87 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. Heme 83-87 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. Heme 39-43 heme oxygenase 1 Homo sapiens 57-61 17822372-1 2007 Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron. Heme 51-55 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. Heme 51-55 heme oxygenase 1 Homo sapiens 18-22 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. Heme 12-16 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. Heme 12-16 heme oxygenase 1 Homo sapiens 106-110 17982681-5 2007 Thus, the production and degradation of PPIX (via heme by HO-1) were simultaneously enhanced, leading to a reduced intracellular concentration of the photodynamically active substance PPIX. Heme 50-54 heme oxygenase 1 Homo sapiens 58-62 17973866-2 2007 Heme compounds, like hemin, a heme oxygenase-1 inducer, are used in the treatment of acute porphyria treatment. Heme 0-4 heme oxygenase 1 Homo sapiens 30-46 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). Heme 139-143 heme oxygenase 1 Homo sapiens 28-32 18089404-1 2007 PURPOSE: The heme oxygenase-1 (HO-1) system is associated with the rate-limiting step of conversion of heme, one of the most critical roles in cytoprotective mechanisms. Heme 13-17 heme oxygenase 1 Homo sapiens 31-35 17881360-1 2007 Heme oxygenase-1 (HO-1), an inducible enzyme that metabolizes the heme group, is highly expressed in human Kaposi sarcoma lesions. Heme 66-70 heme oxygenase 1 Homo sapiens 0-16 17881360-1 2007 Heme oxygenase-1 (HO-1), an inducible enzyme that metabolizes the heme group, is highly expressed in human Kaposi sarcoma lesions. Heme 66-70 heme oxygenase 1 Homo sapiens 18-22 17915953-1 2007 Heme oxygenase-1 (HO-1) is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin. Heme 87-91 heme oxygenase 1 Homo sapiens 0-16 17915953-1 2007 Heme oxygenase-1 (HO-1) is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin. Heme 87-91 heme oxygenase 1 Homo sapiens 18-22 17896171-8 2007 RESULTS: HO-1-overexpression reduced proliferative rates and DNA-synthesis of HUVEC, but provided potent protection from oxidative stress induced by heme and H(2)O(2). Heme 149-153 heme oxygenase 1 Homo sapiens 9-13 17919492-8 2007 Increasing HO-1 by silencing Bach1 with 50 nmol/L Bach1-short interfering RNA or by treatment with 5 mumol/L cobalt protoporphyrin or heme (known inducers of HO-1) decreased HCV RNA and protein by 50% in HCV replicon cells. Heme 134-138 heme oxygenase 1 Homo sapiens 11-15 17919492-8 2007 Increasing HO-1 by silencing Bach1 with 50 nmol/L Bach1-short interfering RNA or by treatment with 5 mumol/L cobalt protoporphyrin or heme (known inducers of HO-1) decreased HCV RNA and protein by 50% in HCV replicon cells. Heme 134-138 heme oxygenase 1 Homo sapiens 158-162 17919492-10 2007 Increasing HO-1, by silencing the Bach1 gene or by treatment with cobalt protoporphyrin or heme, decreases HCV replication. Heme 91-95 heme oxygenase 1 Homo sapiens 11-15 17567933-3 2007 HO-1 catabolizes pro-oxidant heme into substances with anti-oxidant, anti-apoptotic, anti-fibrogenic, vasodilatory and immune modulatory properties. Heme 29-33 heme oxygenase 1 Homo sapiens 0-4 17573819-9 2007 Stress-induced up-regulation of the heme-degrading enzyme, heme oxygenase-1 in AD-affected astroglia may impact central lipid homeostasis by promoting the oxidation of cholesterol to a host of oxysterol intermediates. Heme 36-40 heme oxygenase 1 Homo sapiens 59-75 17701549-2 2007 The transcription of Hmox-1 is regulated by the substrate of HO-1, heme. Heme 67-71 heme oxygenase 1 Homo sapiens 21-27 17785948-9 2007 Accordingly, under the heme-rich condition, heme binds to cysteine-proline (CP) motifs of ALAS1 and those of transcriptional repressor Bach1, thereby leading to repression of mitochondrial transport of ALAS1 and induction of HO-1 transcription, respectively. Heme 44-48 heme oxygenase 1 Homo sapiens 225-229 17785948-7 2007 Heme reduces heme synthesis by suppressing the expression of non-specific 5-aminolevulinate synthase (ALAS1) and stimulates heme breakdown by inducing heme oxygenase (HO)-1 expression. Heme 0-4 heme oxygenase 1 Homo sapiens 151-172 17785948-8 2007 ALAS1 and HO-1 are the rate limiting enzymes in heme biosynthesis and catabolism, respectively. Heme 48-52 heme oxygenase 1 Homo sapiens 10-14 17785948-9 2007 Accordingly, under the heme-rich condition, heme binds to cysteine-proline (CP) motifs of ALAS1 and those of transcriptional repressor Bach1, thereby leading to repression of mitochondrial transport of ALAS1 and induction of HO-1 transcription, respectively. Heme 23-27 heme oxygenase 1 Homo sapiens 225-229 17701549-2 2007 The transcription of Hmox-1 is regulated by the substrate of HO-1, heme. Heme 67-71 heme oxygenase 1 Homo sapiens 61-65 17701549-3 2007 Heme induces expression of Hmox-1 in part by inhibiting the binding of Bach1 to the enhancers and inducing the nuclear export of Bach1. Heme 0-4 heme oxygenase 1 Homo sapiens 27-33 17627585-2 2007 When free heme concentration is increased, it results in the induction of heme oxygenase-1 (HO-1), which then breaks free heme down. Heme 10-14 heme oxygenase 1 Homo sapiens 74-90 17430897-1 2007 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is an integral membrane protein of the smooth endoplasmic reticulum. Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 17430897-1 2007 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is an integral membrane protein of the smooth endoplasmic reticulum. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 17430897-2 2007 However, we detected an HO-1 immunoreactive signal in the nucleus of cultured cells after exposure to hypoxia and heme or heme/hemopexin. Heme 114-118 heme oxygenase 1 Homo sapiens 24-28 17430897-2 2007 However, we detected an HO-1 immunoreactive signal in the nucleus of cultured cells after exposure to hypoxia and heme or heme/hemopexin. Heme 122-126 heme oxygenase 1 Homo sapiens 24-28 17502383-9 2007 Finally, heme induced oxidative burst, neutrophil recruitment, and heme oxygenase-1 expression independently of TLR4. Heme 9-13 heme oxygenase 1 Homo sapiens 67-83 17627585-2 2007 When free heme concentration is increased, it results in the induction of heme oxygenase-1 (HO-1), which then breaks free heme down. Heme 10-14 heme oxygenase 1 Homo sapiens 92-96 17627585-2 2007 When free heme concentration is increased, it results in the induction of heme oxygenase-1 (HO-1), which then breaks free heme down. Heme 74-78 heme oxygenase 1 Homo sapiens 92-96 16980551-3 2007 These downstream products of heme catabolism have recently been found to mediate the antioxidant, antiapoptotic, antiproliferative, vasodilatory, and anti-inflammatory properties of HO-1. Heme 29-33 heme oxygenase 1 Homo sapiens 182-186 17275847-2 2007 Heme oxygenase (HO-1) is an enzyme that is induced by heme as well as oxidative stress and has been reported to be involved in mediating protection against toxic liver injury. Heme 54-58 heme oxygenase 1 Homo sapiens 16-20 17275847-8 2007 CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity. Heme 253-257 heme oxygenase 1 Homo sapiens 43-47 17275847-8 2007 CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity. Heme 253-257 heme oxygenase 1 Homo sapiens 107-111 17275847-8 2007 CONCLUSIONS: Taken together, inhibition of HO-1 in CCl(4)-hepatotoxicity protected the liver, while higher HO-1 activity harmed liver tissue, most probably due to interference of the HO-1 pathway with CCl(4)-dependent metabolism via cytochrome P450 and heme overload-associated toxicity. Heme 253-257 heme oxygenase 1 Homo sapiens 107-111 17325212-3 2007 The boy was a homozygous carrier of short alleles of the heme oxygenase-1 (HO-1) gene GT dinucleotide-repeat promoter polymorphism, which is associated with increased activity and inducibility of the heme-degrading enzyme HO-1, which catalyzes the production of bilirubin. Heme 57-61 heme oxygenase 1 Homo sapiens 75-79 17325212-3 2007 The boy was a homozygous carrier of short alleles of the heme oxygenase-1 (HO-1) gene GT dinucleotide-repeat promoter polymorphism, which is associated with increased activity and inducibility of the heme-degrading enzyme HO-1, which catalyzes the production of bilirubin. Heme 57-61 heme oxygenase 1 Homo sapiens 222-226 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). Heme 54-58 heme oxygenase 1 Homo sapiens 72-76 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). Heme 134-138 heme oxygenase 1 Homo sapiens 54-70 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). Heme 134-138 heme oxygenase 1 Homo sapiens 72-76 17204476-1 2007 Heme oxygenase-1 is a highly inducible gene, the product of which catalyzes breakdown of the prooxidant heme. Heme 104-108 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. Heme 39-43 heme oxygenase 1 Homo sapiens 0-16 17229906-4 2007 Finally, current views regarding the molecular basis for heme-induced upregulation of HO-1 are discussed. Heme 57-61 heme oxygenase 1 Homo sapiens 86-90 17018578-1 2007 Heme oxygenase-1 (HO1), which oxidizes heme to biliverdin, CO, and free iron, conveys protection against oxidative stress and is antiapoptotic. Heme 39-43 heme oxygenase 1 Homo sapiens 18-21 17018578-7 2007 We demonstrate that inhibition of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for HO1, that results in diversion of reducing equivalents from heme oxidation to oxygen reduction. Heme 190-194 heme oxygenase 1 Homo sapiens 34-37 17018578-7 2007 We demonstrate that inhibition of HO1 reflects an interaction of MGd with NADPH-cytochrome P450 reductase, the electron donor for HO1, that results in diversion of reducing equivalents from heme oxidation to oxygen reduction. Heme 190-194 heme oxygenase 1 Homo sapiens 130-133 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. Heme 73-77 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. Heme 73-77 heme oxygenase 1 Homo sapiens 18-22 16959797-1 2006 Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO. Heme 33-37 heme oxygenase 1 Homo sapiens 0-16 16959797-1 2006 Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron and CO. Heme 33-37 heme oxygenase 1 Homo sapiens 18-22 16728265-2 2006 In honor of my dear friend and colleague, Prof. Dr. Jon van Rood, I summarize here our work in this area making use of heme oxygenase-1 (HO-1) and the products that degradation of heme by HO-1 generates. Heme 119-123 heme oxygenase 1 Homo sapiens 137-141 16462769-8 2006 Neither bilirubin, biliverdin nor carbon monoxide, direct products of HO-1 catalysed heme degradation, was responsible for cytoprotection. Heme 85-89 heme oxygenase 1 Homo sapiens 70-74 16528678-1 2006 Heme oxygenase (HO)-1 is the inducible isoform of the first and rate-controlling enzyme of heme degradation. Heme 91-95 heme oxygenase 1 Homo sapiens 0-21 16849502-2 2006 This effect is mimicked by CO, generated via the catabolism of heme by HO-1. Heme 63-67 heme oxygenase 1 Homo sapiens 71-75 16728265-2 2006 In honor of my dear friend and colleague, Prof. Dr. Jon van Rood, I summarize here our work in this area making use of heme oxygenase-1 (HO-1) and the products that degradation of heme by HO-1 generates. Heme 119-123 heme oxygenase 1 Homo sapiens 188-192 16476737-1 2006 Heme oxygenase-1 (HO-1), the inducible enzyme responsible for the rate-limiting step in the heme catabolism, is expressed in AIDS-Kaposi sarcoma (KS) lesions. Heme 92-96 heme oxygenase 1 Homo sapiens 0-16 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. Heme 0-4 heme oxygenase 1 Homo sapiens 61-77 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. Heme 0-4 heme oxygenase 1 Homo sapiens 79-83 16495208-7 2006 In conclusion, our data indicate a novel role for NO in the modulation of heme transport and HO-1 induction in endothelial cells, which may be relevant for hematological disorders characterized by disruption of the heme-NO equilibrium. Heme 215-219 heme oxygenase 1 Homo sapiens 93-97 16476737-1 2006 Heme oxygenase-1 (HO-1), the inducible enzyme responsible for the rate-limiting step in the heme catabolism, is expressed in AIDS-Kaposi sarcoma (KS) lesions. Heme 92-96 heme oxygenase 1 Homo sapiens 18-22 16329999-1 2006 Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS). Heme 34-38 heme oxygenase 1 Homo sapiens 99-115 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. Heme 48-52 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. Heme 48-52 heme oxygenase 1 Homo sapiens 113-117 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). Heme 4-8 heme oxygenase 1 Homo sapiens 75-79 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. Heme 115-119 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. Heme 115-119 heme oxygenase 1 Homo sapiens 18-22 16388581-2 2006 The heme orientation within the active site, which is thought to determine the oxidation regiospecificity, is shown here for the human enzyme (hHO1) to be largely determined by interactions between the heme carboxylic acid groups and residues Arg183 and Lys18 but not Tyr134. Heme 4-8 heme oxygenase 1 Homo sapiens 143-147 16572448-1 2006 OBJECTIVE: To examine the expression and pathogenetic roles of heme oxygenase 1 (HO-1), an inducible heme-degrading enzyme with antiinflammatory properties, in rheumatoid arthritis (RA). Heme 63-67 heme oxygenase 1 Homo sapiens 81-85 16329999-1 2006 Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by the stress-inducible heme oxygenase-1 (HO-1), has recently been demonstrated to provide cytoprotection against cell death in macrophages stimulated with bacterial lipopolysaccharide (LPS). Heme 34-38 heme oxygenase 1 Homo sapiens 117-121 16329999-13 2006 Thus, upregulation of HO-1 and overproduction of CO may allow the survival of LPS-stimulated macrophages; first, by eliminating the free heme to prevent Fenton reaction, second, by limiting the availability of free heme required for induction of NO-producing heme enzyme (i.e., iNOS), third, by limiting additional production of O(2)(-) and NO via CO-derived inhibition on the activities of heme enzymes like NADPH oxidase and iNOS, respectively. Heme 137-141 heme oxygenase 1 Homo sapiens 22-26 16329999-13 2006 Thus, upregulation of HO-1 and overproduction of CO may allow the survival of LPS-stimulated macrophages; first, by eliminating the free heme to prevent Fenton reaction, second, by limiting the availability of free heme required for induction of NO-producing heme enzyme (i.e., iNOS), third, by limiting additional production of O(2)(-) and NO via CO-derived inhibition on the activities of heme enzymes like NADPH oxidase and iNOS, respectively. Heme 215-219 heme oxygenase 1 Homo sapiens 22-26 16943657-1 2006 Heme oxygenase 1 (HO-1) is an enzyme important in the catabolism of heme that is induced under conditions of oxidative stress. Heme 68-72 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. Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 16943657-1 2006 Heme oxygenase 1 (HO-1) is an enzyme important in the catabolism of heme that is induced under conditions of oxidative stress. Heme 68-72 heme oxygenase 1 Homo sapiens 18-22 16382109-3 2005 Inducible HO (HO-1) and constitutive HO (HO-2) are mostly recognized for their roles in the oxidation of heme and production of CO and biliverdin, whereas the biological function of the third HO isoform, HO-3, is still unclear. Heme 105-109 heme oxygenase 1 Homo sapiens 14-18 16183036-1 2005 In the beginning, the microsomal HO system was presumed to be made of one isozymes, now known as HO-1, which was cytP450-dependent; and, was thought to be of physiological significance solely in the context of catalysis of hemoglobin heme to bile pigments and CO. A succession of discoveries including characterization of the system as an independent mono-oxygenase, identification of a second form, called HO-2, free radical quenching activity of bile pigments, analogous function of CO in cell signaling to NO, and characterization of the system as HSP32 cognates has led to such an impressive expansion in the number of reports dealing with the HO system that surpass anyone"s expectation. Heme 234-238 heme oxygenase 1 Homo sapiens 97-101 16154530-7 2005 Ortiz de Montellano, Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1, J. Biol. Heme 100-104 heme oxygenase 1 Homo sapiens 114-130 16309585-2 2005 HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Heme 33-37 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. Heme 34-38 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. Heme 34-38 heme oxygenase 1 Homo sapiens 18-22 16356130-1 2005 Heme oxygenase (HO)-1, involved in the heme degradation process, is an important antioxidant enzyme. Heme 39-43 heme oxygenase 1 Homo sapiens 0-21 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. Heme 22-26 heme oxygenase 1 Homo sapiens 0-16 16183497-2 2005 Heme oxygenase-1 (HO-1) has recently been shown to be cytoprotective, and is known to be induced by heme moieties. Heme 100-104 heme oxygenase 1 Homo sapiens 0-16 16183497-2 2005 Heme oxygenase-1 (HO-1) has recently been shown to be cytoprotective, and is known to be induced by heme moieties. Heme 100-104 heme oxygenase 1 Homo sapiens 18-22 16309588-2 2005 We previously revealed a substantial oxidation of plasma hemoglobin to methemoglobin and a subsequent heme-catalyzed LDL oxidation generating moieties toxic to endothelium in heme oxygenase-1 (HO-1)-deficiency in human. Heme 102-106 heme oxygenase 1 Homo sapiens 175-191 16020746-6 2005 The proposed mechanisms by which HO-1 exerts its cytoprotective effects include its abilities to degrade the pro-oxidative heme, to release biliverdin and subsequently convert it bilirubin, both of which have antioxidant properties, and to generate carbon monoxide, which has antiproliferative and antiinflammatory as well as vasodilatory properties. Heme 123-127 heme oxygenase 1 Homo sapiens 33-37 16117883-1 2005 BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function. Heme 84-88 heme oxygenase 1 Homo sapiens 12-28 15920011-1 2005 Heme oxygenase-1 (HO-1) is an intracellular enzyme that degrades heme and inhibits immune responses and inflammation in vivo. Heme 65-69 heme oxygenase 1 Homo sapiens 0-16 15920011-1 2005 Heme oxygenase-1 (HO-1) is an intracellular enzyme that degrades heme and inhibits immune responses and inflammation in vivo. Heme 65-69 heme oxygenase 1 Homo sapiens 18-22 16117883-1 2005 BACKGROUND: Heme-oxygenase 1 (HO-1) is a rate-limiting enzyme in the degradation of heme to bilirubin, ferritin and carbon monoxide (CO) and may have significant anti-inflammatory function. Heme 84-88 heme oxygenase 1 Homo sapiens 30-34 16240585-1 2005 Heme oxygenase 1 (HO-1) catalyses the oxidation of heme to biliverdin, and its expression is induced by oxidative stress. Heme 51-55 heme oxygenase 1 Homo sapiens 0-16 16181113-12 2005 These results suggest that increasing HO-1 expression with a proteasome inhibitor protects astrocytes from heme-mediated oxidative injury. Heme 107-111 heme oxygenase 1 Homo sapiens 38-42 16240585-1 2005 Heme oxygenase 1 (HO-1) catalyses the oxidation of heme to biliverdin, and its expression is induced by oxidative stress. Heme 51-55 heme oxygenase 1 Homo sapiens 18-22 16044631-5 2005 In particular, heme oxygenase-1 (HO-1), the enzyme involved in heme protein metabolism, can provide antioxidant protection through the production of the antioxidant bilirubin. Heme 15-19 heme oxygenase 1 Homo sapiens 33-37 15833736-1 2005 Heme oxygenase (HO)-1 is the inducible isoform of the rate-limiting enzyme of heme degradation and modulates the inflammatory immune response. Heme 78-82 heme oxygenase 1 Homo sapiens 0-21 15690204-2 2005 Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis. Heme 68-72 heme oxygenase 1 Homo sapiens 86-90 15927501-4 2005 Heme is catabolised by heme oxygenase 1, anchored in the endoplasmic reticulum membrane. Heme 0-4 heme oxygenase 1 Homo sapiens 23-39 15890016-1 2005 Heme oxygenase isoforms (HO-1/HO-2) catalyze the conversion of heme to carbon monoxide (CO) and bilirubin. Heme 63-67 heme oxygenase 1 Homo sapiens 0-34 16181102-6 2005 Addition of heme (10 microM) increased HO-1 protein and bilirubin formation in G0/G1, in a time dependent manner peaking at 16 h. Glucose attenuated heme mediated increase in HO-1 proteins. Heme 12-16 heme oxygenase 1 Homo sapiens 39-43 16181102-6 2005 Addition of heme (10 microM) increased HO-1 protein and bilirubin formation in G0/G1, in a time dependent manner peaking at 16 h. Glucose attenuated heme mediated increase in HO-1 proteins. Heme 12-16 heme oxygenase 1 Homo sapiens 175-179 16181102-8 2005 The rate of HO-1 induction in response to heme was several fold higher in serum-starved cells compared to cells cultured in 10% FBS. Heme 42-46 heme oxygenase 1 Homo sapiens 12-16 16181102-11 2005 These results imply that expression of HO-1 in G0/G1 cells may be a key player in decreasing cellular heme, associated with increased generation of bilirubin, and in attenuating glucose mediated oxidative stress. Heme 102-106 heme oxygenase 1 Homo sapiens 39-43 15690204-2 2005 Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis. Heme 68-72 heme oxygenase 1 Homo sapiens 231-235 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). Heme 86-90 heme oxygenase 1 Homo sapiens 0-16 15611319-0 2005 Heme-induced heme oxygenase-1 (HO-1) in human monocytes inhibits apoptosis despite caspase-3 up-regulation. Heme 0-4 heme oxygenase 1 Homo sapiens 13-29 15611319-0 2005 Heme-induced heme oxygenase-1 (HO-1) in human monocytes inhibits apoptosis despite caspase-3 up-regulation. Heme 0-4 heme oxygenase 1 Homo sapiens 31-35 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). Heme 141-145 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). Heme 141-145 heme oxygenase 1 Homo sapiens 18-22 15649645-4 2005 We will argue that the protective effects exerted by HO-1 are mediated to a large extent by the end products that it generates via the catabolism of heme. Heme 149-153 heme oxygenase 1 Homo sapiens 53-57 15525643-1 2005 The ability of the human heme oxygenase-1 (hHO-1) R183E mutant to oxidize heme in reactions supported by either NADPH-cytochrome P450 reductase or ascorbic acid has been compared. Heme 25-29 heme oxygenase 1 Homo sapiens 43-48 15525643-7 2005 The crystal structure of the R183E mutant, determined in the ferric and ferrous-NO bound forms, shows that the heme primarily adopts the same orientation as in wild-type hHO-1. Heme 111-115 heme oxygenase 1 Homo sapiens 170-175 15516695-10 2005 Thus, Lys(149) and Lys(153) appear to interact with CPR in such a way as to orient the redox partners for optimal electron transfer from FMN of CPR to heme of HO-1. Heme 151-155 heme oxygenase 1 Homo sapiens 159-163 15516695-1 2005 Heme oxygenase-1 (HO-1) catalyzes the physiological degradation of heme at the expense of molecular oxygen using electrons donated by NADPH-cytochrome P450 reductase (CPR). Heme 67-71 heme oxygenase 1 Homo sapiens 0-16 15516695-1 2005 Heme oxygenase-1 (HO-1) catalyzes the physiological degradation of heme at the expense of molecular oxygen using electrons donated by NADPH-cytochrome P450 reductase (CPR). Heme 67-71 heme oxygenase 1 Homo sapiens 18-22 15516695-4 2005 The HO-1 mutants, K149A, K149A/K153A, and R185A, showed almost no heme degradation activity with NADPH-CPR, whereas they exhibited activity comparable to that of the wild type when sodium ascorbate was used. Heme 66-70 heme oxygenase 1 Homo sapiens 4-8 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). Heme 86-90 heme oxygenase 1 Homo sapiens 18-22 15933765-4 2005 Induction of HO-1 occurs as an adaptive and beneficial response to several injurious stimuli including heme and this inducible nature of HO-1 signifies its importance in several pathophysiological disease states. Heme 103-107 heme oxygenase 1 Homo sapiens 13-17 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. Heme 79-83 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. Heme 79-83 heme oxygenase 1 Homo sapiens 18-22 16291246-3 2005 The NO-derived induction of HO-1 caused (a) rapid elimination of toxic heme to inhibit lipid peroxidation and to prevent further induction of iNOS, (b) rapid production of bile pigment antioxidants to scavenge reactive oxygen (O2-) and nitrogen (NO) metabolites, and (c) rapid production of carbon monoxide (CO) to inhibit further production of O2- and NO by blocking the activities of NADPH-oxidase and iNOS, respectively. Heme 71-75 heme oxygenase 1 Homo sapiens 28-32 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. Heme 110-114 heme oxygenase 1 Homo sapiens 0-30 15899048-1 2005 Heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, is expressed by macrophages and endothelial cells in response to various stresses. Heme 38-42 heme oxygenase 1 Homo sapiens 0-16 15899048-1 2005 Heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, is expressed by macrophages and endothelial cells in response to various stresses. Heme 38-42 heme oxygenase 1 Homo sapiens 18-22 15547665-3 2004 Heme oxygenase-1 (HO-1) is known to be induced not only by its substrate, heme, but also by various oxidative stresses, and thought to play an important role in the protection of the host from oxidative tissue injuries. Heme 74-78 heme oxygenase 1 Homo sapiens 0-16 15308469-4 2004 After it enters the cell, heme is degraded by heme oxygenase-1 (HO-1), and iron is released. Heme 26-30 heme oxygenase 1 Homo sapiens 46-62 15465821-1 2004 Heme oxygenase-1 is an antioxidant defense enzyme that converts heme to biliverdin, iron, and carbon monoxide. Heme 64-68 heme oxygenase 1 Homo sapiens 0-16 15465821-7 2004 The effect of increasing concentrations of heme to up-regulate levels of heme oxygenase-1 was more pronounced when Bach-1 siRNA was present. Heme 43-47 heme oxygenase 1 Homo sapiens 73-89 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. Heme 72-76 heme oxygenase 1 Homo sapiens 90-94 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. Heme 175-179 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. Heme 175-179 heme oxygenase 1 Homo sapiens 183-187 15547665-3 2004 Heme oxygenase-1 (HO-1) is known to be induced not only by its substrate, heme, but also by various oxidative stresses, and thought to play an important role in the protection of the host from oxidative tissue injuries. Heme 74-78 heme oxygenase 1 Homo sapiens 18-22 15547665-8 2004 These findings suggest that, in the liver of ALF patients, there may be an increase in free heme concentration which up-regulates HO-1 gene expression, while down-regulating ALAS1 gene expression, resulting in markedly altered heme metabolism and liver function. Heme 92-96 heme oxygenase 1 Homo sapiens 130-134 15522396-0 2004 Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage. Heme 59-63 heme oxygenase 1 Homo sapiens 88-104 15560792-5 2004 PCC 6803 (Syn HO-1), in complex with heme at 2.5 A resolution. Heme 37-41 heme oxygenase 1 Homo sapiens 14-18 15560792-7 2004 Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity. Heme 13-17 heme oxygenase 1 Homo sapiens 37-41 15560792-7 2004 Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity. Heme 28-32 heme oxygenase 1 Homo sapiens 37-41 15560792-7 2004 Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity. Heme 28-32 heme oxygenase 1 Homo sapiens 94-98 15560792-10 2004 The surfaces of the heme binding sides are both positively charged, but this patch of Syn HO-1 is narrow compared to that of mammalian HO-1. Heme 20-24 heme oxygenase 1 Homo sapiens 90-94 15560792-10 2004 The surfaces of the heme binding sides are both positively charged, but this patch of Syn HO-1 is narrow compared to that of mammalian HO-1. Heme 20-24 heme oxygenase 1 Homo sapiens 135-139 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. Heme 19-23 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. Heme 19-23 heme oxygenase 1 Homo sapiens 155-159 15474356-9 2004 These results support the hypothesis that HO-1 protects astrocytes from heme-mediated oxidative injury. Heme 72-76 heme oxygenase 1 Homo sapiens 42-46 15451438-1 2004 Previous studies show that expression of heme oxygenase-1 (HO-1) in endothelial cells results in decreased cyclooxygenase expression and prostaglandin (PG) levels through limiting heme availability. Heme 41-45 heme oxygenase 1 Homo sapiens 59-63 15636365-1 2004 Human Heme Oxygenase-1 (hHO-1) is the rate-limiting enzyme in the catabolism reaction of heme, which directly regulates the concentration of bilirubin in human body. Heme 89-93 heme oxygenase 1 Homo sapiens 6-22 15345141-4 2004 Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1). Heme 5-9 heme oxygenase 1 Homo sapiens 232-248 15345141-4 2004 Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1). Heme 5-9 heme oxygenase 1 Homo sapiens 250-254 15345141-4 2004 Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1). Heme 35-39 heme oxygenase 1 Homo sapiens 232-248 15345141-4 2004 Free heme, i.e., a protein-unbound heme, exists in cells at a very minute concentration and exerts regulatory functions such as the repression of nonspecific delta-aminolevulinate synthase expression and the induction of microsomal heme oxygenase-1 (HO-1). Heme 35-39 heme oxygenase 1 Homo sapiens 250-254 15345141-5 2004 The latter gene expression occurs by way of free heme-mediated derepression of Bach1, a mammalian heme-responsive transcription factor that suppresses the activation of the HO-1 gene. Heme 49-53 heme oxygenase 1 Homo sapiens 173-177 15345143-3 2004 Free heme, an entity that can be generated by UVA irradiation of cells, also appears to be a critical intermediate that can directly influence both the transcriptional activation and repression of the HO-1 gene. Heme 5-9 heme oxygenase 1 Homo sapiens 201-205 15242350-8 2004 These results demonstrate for the first time that USF proteins bind to the human HO-1 promoter in vivo and are required for high-level expression of HO-1 by haem and cadmium in human renal epithelial cells. Heme 157-161 heme oxygenase 1 Homo sapiens 81-85 15242350-8 2004 These results demonstrate for the first time that USF proteins bind to the human HO-1 promoter in vivo and are required for high-level expression of HO-1 by haem and cadmium in human renal epithelial cells. Heme 157-161 heme oxygenase 1 Homo sapiens 149-153 15297453-1 2004 Human heme oxygenase-1 (hHO-1) catalyzes the O2-dependent oxidation of heme to biliverdin, CO, and free iron. Heme 6-10 heme oxygenase 1 Homo sapiens 24-29 15297453-10 2004 In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon. Heme 15-19 heme oxygenase 1 Homo sapiens 20-25 15297453-10 2004 In the 5-phenylheme-hHO-1 structure, the phenyl-substituted heme occupies the same position as heme in the heme-HO-1 complex but the 5-phenyl substituent disrupts the rigid hydrophobic wall of residues Met34, Phe214, and residues 26-42 near the alpha-meso carbon. Heme 15-19 heme oxygenase 1 Homo sapiens 21-25 15345147-2 2004 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress. Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 15345147-2 2004 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 15345147-2 2004 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress. Heme 109-113 heme oxygenase 1 Homo sapiens 0-16 15345147-2 2004 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, is induced not only by its substrate, heme, but also by oxidative stress. Heme 109-113 heme oxygenase 1 Homo sapiens 18-22 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. Heme 148-152 heme oxygenase 1 Homo sapiens 65-69 15345152-3 2004 As a further complication, heme and cadmium, two potent inducers of the hmox-1 gene, inhibit Bach1 function by different mechanisms-by inhibition of DNA binding or promotion of nuclear export, respectively. Heme 27-31 heme oxygenase 1 Homo sapiens 72-78 15636365-1 2004 Human Heme Oxygenase-1 (hHO-1) is the rate-limiting enzyme in the catabolism reaction of heme, which directly regulates the concentration of bilirubin in human body. Heme 89-93 heme oxygenase 1 Homo sapiens 24-29 15339982-8 2004 Heme catabolism is regulated by (inducible) heme oxygenase-1 (HO-1). Heme 0-4 heme oxygenase 1 Homo sapiens 44-60 15339982-8 2004 Heme catabolism is regulated by (inducible) heme oxygenase-1 (HO-1). Heme 0-4 heme oxygenase 1 Homo sapiens 62-66 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. Heme 95-99 heme oxygenase 1 Homo sapiens 107-123 15271722-2 2004 HO-1 catalyzes the conversion of the heme moiety of hemeproteins, such as hemoglobin, myoglobin, and cytochrome P450, to biliverdin, liberating carbon monoxide (CO) in the process. Heme 37-41 heme oxygenase 1 Homo sapiens 0-4 15271722-7 2004 These results suggest that oxidative stress caused by anesthesia and/or surgery may induce HO-1, which catalyzes heme to produce CO, leading to increased exhaled CO concentration. Heme 113-117 heme oxygenase 1 Homo sapiens 91-95 15219989-0 2004 Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex. Heme 49-53 heme oxygenase 1 Homo sapiens 71-87 14726403-8 2004 Increased HO-1 enzymatic activity in vitro enhanced proliferation of KSHV-infected DMVECs in the presence of free heme. Heme 114-118 heme oxygenase 1 Homo sapiens 10-14 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. Heme 40-44 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. Heme 40-44 heme oxygenase 1 Homo sapiens 18-22 15180563-3 2004 Exposure of mammalian cells to oxidative stimuli induces heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, as well as a 33-kDa heat shock protein. Heme 57-61 heme oxygenase 1 Homo sapiens 75-79 15126353-2 2004 Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the degradation of heme and has recently been implicated in the regulation of growth and survival of various neoplastic cells. Heme 89-93 heme oxygenase 1 Homo sapiens 0-16 15126353-2 2004 Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the degradation of heme and has recently been implicated in the regulation of growth and survival of various neoplastic cells. Heme 89-93 heme oxygenase 1 Homo sapiens 18-22 14726403-9 2004 Treatment with the HO-1 inhibitor chromium mesoporphyrin IX abolished heme-induced proliferation. Heme 70-74 heme oxygenase 1 Homo sapiens 19-23 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. Heme 36-40 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. Heme 64-68 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. Heme 64-68 heme oxygenase 1 Homo sapiens 30-34 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. Heme 159-163 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. Heme 159-163 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. Heme 36-40 heme oxygenase 1 Homo sapiens 18-22 15004156-1 2004 Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin. Heme 54-58 heme oxygenase 1 Homo sapiens 0-16 14977880-1 2004 Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO). Heme 33-37 heme oxygenase 1 Homo sapiens 0-16 14977880-1 2004 Heme oxygenase-1 (HO-1) degrades heme into iron, biliverdin, and carbon monoxide (CO). Heme 33-37 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. Heme 23-27 heme oxygenase 1 Homo sapiens 41-45 15004156-1 2004 Heme oxygenase-1 (HO-1) cleaves the porphyrin ring of heme into carbon monoxide, Fe2+, and biliverdin, which is then converted into bilirubin. Heme 54-58 heme oxygenase 1 Homo sapiens 18-22 14761930-5 2004 Several stimuli implicated in the pathogenesis of renal injury, such as heme, nitric oxide, growth factors, angiotensin II, cytokines, and nephrotoxins, induce HO-1. Heme 72-76 heme oxygenase 1 Homo sapiens 160-164 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. Heme 85-89 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. Heme 65-69 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. Heme 65-69 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. Heme 85-89 heme oxygenase 1 Homo sapiens 18-22 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). Heme 178-182 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). Heme 178-182 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. Heme 100-104 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. Heme 100-104 heme oxygenase 1 Homo sapiens 32-36 14635185-1 2003 The purpose of the present study was to examine the role of human heme oxygenase (human HO-1) in cell cycle progression following exposure to heme or human HO-1 gene transfer and to identify target genes associated with human HO-1-meditated increases in cell cycle progression using cDNA microarray technology. Heme 66-70 heme oxygenase 1 Homo sapiens 88-92 14523007-1 2003 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, protects against oxidative stress, and shows potent anti-inflammatory effects. Heme 60-64 heme oxygenase 1 Homo sapiens 0-16 14523007-1 2003 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, protects against oxidative stress, and shows potent anti-inflammatory effects. Heme 60-64 heme oxygenase 1 Homo sapiens 18-22 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). Heme 59-63 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). Heme 59-63 heme oxygenase 1 Homo sapiens 24-28 14635185-1 2003 The purpose of the present study was to examine the role of human heme oxygenase (human HO-1) in cell cycle progression following exposure to heme or human HO-1 gene transfer and to identify target genes associated with human HO-1-meditated increases in cell cycle progression using cDNA microarray technology. Heme 66-70 heme oxygenase 1 Homo sapiens 156-160 14635185-1 2003 The purpose of the present study was to examine the role of human heme oxygenase (human HO-1) in cell cycle progression following exposure to heme or human HO-1 gene transfer and to identify target genes associated with human HO-1-meditated increases in cell cycle progression using cDNA microarray technology. Heme 66-70 heme oxygenase 1 Homo sapiens 156-160 14635185-2 2003 Heme-induced robust human HO-1 expression in quiescent human microvessel endothelial cells cultured in 1% FBS and the levels of human HO-1 expression progressively declined without a change in the cell cyclin. Heme 0-4 heme oxygenase 1 Homo sapiens 26-30 14635185-2 2003 Heme-induced robust human HO-1 expression in quiescent human microvessel endothelial cells cultured in 1% FBS and the levels of human HO-1 expression progressively declined without a change in the cell cyclin. Heme 0-4 heme oxygenase 1 Homo sapiens 134-138 12933701-1 2003 Heme oxygenase-1 (HO-1) is a stress protein that has been suggested to participate in defense mechanisms against agents that may induce oxidative injury, such as heme and inflammatory molecules. Heme 162-166 heme oxygenase 1 Homo sapiens 0-16 14562166-1 2003 INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). Heme 80-84 heme oxygenase 1 Homo sapiens 44-48 12933701-1 2003 Heme oxygenase-1 (HO-1) is a stress protein that has been suggested to participate in defense mechanisms against agents that may induce oxidative injury, such as heme and inflammatory molecules. Heme 162-166 heme oxygenase 1 Homo sapiens 18-22 12933701-3 2003 Overexpression of HO-1 was coupled with an increase in HO activity and carbon monoxide synthesis, decreased cellular heme, and acceleration in all phases of the cell cycle (P<0.001). Heme 117-121 heme oxygenase 1 Homo sapiens 18-22 12933701-8 2003 These findings identify a novel effect of HO-1 on endothelial cell growth and indicate that heme metabolism and HO-1 expression regulate signaling systems in cells exposed to high glucose, which controls cell-cycle progression. Heme 92-96 heme oxygenase 1 Homo sapiens 42-46 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. Heme 77-81 heme oxygenase 1 Homo sapiens 192-196 12958189-2 2003 HO-1 cleaves the heme porphyrin ring releasing Fe2+, which induces the expression of the Fe2+ sequestering protein ferritin. Heme 17-21 heme oxygenase 1 Homo sapiens 0-4 12783778-0 2003 An internal enhancer regulates heme- and cadmium-mediated induction of human heme oxygenase-1. Heme 31-35 heme oxygenase 1 Homo sapiens 77-93 12783778-1 2003 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Heme 60-64 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. Heme 60-64 heme oxygenase 1 Homo sapiens 18-22 12783778-3 2003 The purpose of this study was to characterize the regulation of the human HO-1 gene in renal proximal tubule and aortic endothelial cells in response to heme and cadmium. Heme 153-157 heme oxygenase 1 Homo sapiens 74-78 12783778-4 2003 Evaluation of multiple human HO-1 promoter-reporter constructs up to -9.1 kb demonstrated only a partial response to heme and cadmium. Heme 117-121 heme oxygenase 1 Homo sapiens 29-33 12783778-7 2003 Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene. Heme 131-135 heme oxygenase 1 Homo sapiens 62-66 12783778-7 2003 Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene. Heme 131-135 heme oxygenase 1 Homo sapiens 102-106 12783778-7 2003 Our studies identified a novel enhancer internal to the human HO-1 gene that, in conjunction with the HO-1 promoter, recapitulates heme- and cadmium-mediated induction of the endogenous HO-1 gene. Heme 131-135 heme oxygenase 1 Homo sapiens 102-106 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. Heme 0-4 heme oxygenase 1 Homo sapiens 69-85 12891549-10 2003 These effects were ascribed to bilirubin, one of the products of HO-1-mediated heme degradation. Heme 79-83 heme oxygenase 1 Homo sapiens 65-69 12909459-0 2003 Heme oxygenase-1: unleashing the protective properties of heme. Heme 58-62 heme oxygenase 1 Homo sapiens 0-16 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). Heme 34-38 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. Heme 0-4 heme oxygenase 1 Homo sapiens 87-91 14580148-7 2003 Notably, HO-1 expression is induced by heme in all mammalian cells examined, but is repressed by hypoxia in certain types of cultured human cells. Heme 39-43 heme oxygenase 1 Homo sapiens 9-13 14580148-8 2003 The recent discovery of Bach1 as a heme-regulated and hypoxia-inducible repressor for transcription of the HO-1 gene has provided a missing link in the feedback control of heme catabolism. Heme 35-39 heme oxygenase 1 Homo sapiens 107-111 14592553-6 2003 Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene attenuated heme and Ang II-induced prostaglandin synthesis. Heme 103-107 heme oxygenase 1 Homo sapiens 16-20 14592553-6 2003 Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene attenuated heme and Ang II-induced prostaglandin synthesis. Heme 103-107 heme oxygenase 1 Homo sapiens 82-86 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. Heme 6-10 heme oxygenase 1 Homo sapiens 24-29 12704646-1 2003 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme to carbon monoxide (CO), iron, and biliverdin. Heme 53-57 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. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 12704646-3 2003 Although interest in HO-1 originally centered on its heme-degrading function, recent findings indicate that HO-1 exerts other biologically important actions. Heme 53-57 heme oxygenase 1 Homo sapiens 21-25 12500973-0 2003 Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1. Heme 18-22 heme oxygenase 1 Homo sapiens 67-83 12709568-2 2003 We examined the effect of delivery of the human HO-1 gene on cellular heme in renal tissue using a retroviral vector. Heme 70-74 heme oxygenase 1 Homo sapiens 48-52 12709571-1 2003 Heme oxygenase-1 (HO-1) is an essential enzyme in heme catabolism and is characterized by its inducibility in response to various environmental factors, including its substrate heme. Heme 50-54 heme oxygenase 1 Homo sapiens 0-16 12709571-1 2003 Heme oxygenase-1 (HO-1) is an essential enzyme in heme catabolism and is characterized by its inducibility in response to various environmental factors, including its substrate heme. Heme 50-54 heme oxygenase 1 Homo sapiens 18-22 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. Heme 168-172 heme oxygenase 1 Homo sapiens 22-26 12511571-2 2003 HO-1 is induced by its substrate heme and various environmental factors, which represents a protective response against oxidative stresses. Heme 33-37 heme oxygenase 1 Homo sapiens 0-4 12709582-3 2003 Culture of PMEC with low serum heme decreased cGMP and the detection of peroxide with 10 microM 2",7"-dichlorofluorescin diacetate and increased HO-1 further decreased cGMP without altering the peroxide detection under these conditions. Heme 31-35 heme oxygenase 1 Homo sapiens 145-149 12709585-2 2003 Although most of the monocyte-derived cytokines exhibit proinflammatory functions in vivo, heme oxygenase-1 (HO-1), an inducible heme-degrading enzyme, exerts potent anti-inflammatory effect through production of carbon monoxide and bilirubin. Heme 91-95 heme oxygenase 1 Homo sapiens 109-113 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. Heme 27-31 heme oxygenase 1 Homo sapiens 0-3 12678694-7 2003 Perhaps one or more of the products of HO1 heme metabolism is involved in induced adaptive resistance or perhaps a heme-independent mechanism is involved. Heme 43-47 heme oxygenase 1 Homo sapiens 39-42 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. Heme 61-65 heme oxygenase 1 Homo sapiens 0-16 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. Heme 145-149 heme oxygenase 1 Homo sapiens 0-16 12623985-6 2003 Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene also attenuated heme and Ang II-induced prostaglandin synthesis. Heme 108-112 heme oxygenase 1 Homo sapiens 16-20 12623985-6 2003 Upregulation of HO-1 gene expression by retrovirus-mediated delivery of the human HO-1 gene also attenuated heme and Ang II-induced prostaglandin synthesis. Heme 108-112 heme oxygenase 1 Homo sapiens 82-86 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. Heme 76-80 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. Heme 76-80 heme oxygenase 1 Homo sapiens 18-22 12433915-2 2003 We have examined the binding of NO to human heme oxygenase-1 (hHO-1), an enzyme that oxidizes heme to biliverdin, CO, and free iron, to determine whether inhibition of hHO-1 by NO can contribute to the signaling interplay of NO and CO. An Fe(3+)-NO hHO-1-heme complex is formed with NO or the NO donors NOC9 or 2-(N,N-diethylamino)-diazenolate-2-oxide.sodium salt. Heme 44-48 heme oxygenase 1 Homo sapiens 62-67 12964953-2 2003 In addition to its physiological role in heme degradation, HO-1 may influence a number of cellular processes, including growth, inflammation, and apoptosis. Heme 41-45 heme oxygenase 1 Homo sapiens 59-63 14529549-1 2003 The heme oxygenase-1 (HO-1) enzyme catalyzes the rate-limiting reaction in the catabolism of heme yielding products with pleiotropic, but ultimately, cytoprotective activities. Heme 4-8 heme oxygenase 1 Homo sapiens 22-26 14529549-4 2003 Extensive analysis of the mouse gene, and to a lesser extent of the human gene, has identified a common mechanism the stress response element (StRE)/Nrf2 transcription factor pathway for gene regulation in response to a diverse array of HO-1 inducers including the substrate heme, various environmental and industrial toxins, and plant-derived polyphenolic compounds. Heme 275-279 heme oxygenase 1 Homo sapiens 237-241 14529550-9 2003 Human HO-1 gene transfer into endothelial cells has been shown to attenuate Ang II- TNF- and heme-mediated DNA damage. Heme 93-97 heme oxygenase 1 Homo sapiens 6-10 12469218-6 2003 These findings suggest that the overexpression of CYP2E1 results in the up-regulation of ALAS-N in order to meet with an increased demand for heme synthesis for CYP2E1 formation, while it also results in the up-regulation of HO-1 presumably by enzyme induction by free heme released from CYP2E1, which then results in the elimination of toxic excess free heme and ultimately restores the physiologic milieu. Heme 269-273 heme oxygenase 1 Homo sapiens 225-229 12469218-6 2003 These findings suggest that the overexpression of CYP2E1 results in the up-regulation of ALAS-N in order to meet with an increased demand for heme synthesis for CYP2E1 formation, while it also results in the up-regulation of HO-1 presumably by enzyme induction by free heme released from CYP2E1, which then results in the elimination of toxic excess free heme and ultimately restores the physiologic milieu. Heme 269-273 heme oxygenase 1 Homo sapiens 225-229 15115285-1 2003 Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin. Heme 107-111 heme oxygenase 1 Homo sapiens 0-21 15115285-1 2003 Heat shock protein 32 (Hsp32, hemoxygenase-1) is induced by reactive oxygen metabolites (ROM) and degrades heme leading to the formation of antioxidant bilirubin. Heme 107-111 heme oxygenase 1 Homo sapiens 23-28 12498987-1 2003 In many models, a protective role for heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, has been demonstrated. Heme 38-42 heme oxygenase 1 Homo sapiens 56-60 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). Heme 47-51 heme oxygenase 1 Homo sapiens 0-4 12444034-2 2002 Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties. Heme 174-178 heme oxygenase 1 Homo sapiens 33-37 12444034-2 2002 Although the mechanisms by which HO-1 exerts its cytoprotection are not clearly understood, it has been speculated that carbon monoxide (CO), a catalytic byproduct following heme catabolism by HO-1, may mediate cellular cytoprotection via its anti-inflammatory properties. Heme 174-178 heme oxygenase 1 Homo sapiens 193-197 12376366-8 2002 These results indicate that prolonged overexpression of HO-1 ultimately decreases sGC activity by limiting the availability of cellular heme. Heme 136-140 heme oxygenase 1 Homo sapiens 56-60 12699247-0 2002 Interaction of heme with nitroxyl or nitric oxide amplifies heme oxygenase-1 induction: involvement of the transcription factor Nrf2. Heme 15-19 heme oxygenase 1 Homo sapiens 60-76 12699247-1 2002 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme, the expression of which is highly sensitive to induction by pro-oxidant stimuli including the substrate heme and reactive oxygen species. Heme 156-160 heme oxygenase 1 Homo sapiens 0-16 12699247-1 2002 Heme oxygenase-1 (HO-1) is a cytoprotective enzyme, the expression of which is highly sensitive to induction by pro-oxidant stimuli including the substrate heme and reactive oxygen species. Heme 156-160 heme oxygenase 1 Homo sapiens 18-22 12699247-4 2002 The amplification of the heme oxygenase pathway appears to involve a direct interaction between heme and the NO groups, as the ability of both NO(-)- and NO-releasing agents to induce HO-1 is totally lost by their pre-incubation for 1 hr in complete medium prior to cell treatment but is highly preserved by addition of hemin during the preincubation step. Heme 25-29 heme oxygenase 1 Homo sapiens 184-188 12699247-8 2002 We propose that modification of the iron protoporphyrin centers by NO groups to modulate HO-1 expression might be regarded as a molecular switch to maximize heme oxygenase enzymatic activity and consequently mitigate the redox imbalance imposed by oxidative and nitrosative stress. Heme 36-55 heme oxygenase 1 Homo sapiens 89-93 12376366-3 2002 Pulmonary cells that expressed hHO-1 exhibited a fourfold increase in HO activity associated with decreases in the steady-state levels of heme and cGMP without changes in soluble GC (sGC) and endothelial nitric oxide synthase (NOS) proteins or basal nitrite production. Heme 138-142 heme oxygenase 1 Homo sapiens 31-36 12376366-4 2002 Heme elicited significant increases in CO production and intracellular cGMP levels in both pulmonary endothelial and pulmonary hHO-1-expressing cells. Heme 0-4 heme oxygenase 1 Homo sapiens 127-132 12376366-5 2002 N(omega)-nitro-L-arginine methyl ester (L-NAME), an inhibitor of NOS, significantly decreased cGMP levels in heme-treated pulmonary endothelial cells but not heme-treated hHO-1-expressing cells. Heme 109-113 heme oxygenase 1 Homo sapiens 171-176 12376366-6 2002 In the presence of exogenous heme, CO and cGMP levels in hHO-1-expressing cells exceeded the corresponding levels in pulmonary endothelial cells. Heme 29-33 heme oxygenase 1 Homo sapiens 57-62 12382200-12 2002 Heme oxygenase 1 is essential for the catabolism of heme and in the recycling of hemoglobin iron in macrophages. Heme 52-56 heme oxygenase 1 Homo sapiens 0-16 12394829-1 2002 The heme oxygenase-1 (HO-1) system, the rate-limiting step in the conversion of heme, is among the most critical of cytoprotective mechanisms activated during cellular stress. Heme 4-8 heme oxygenase 1 Homo sapiens 22-26 12230869-1 2002 Heme oxygenase-1 (HO-1) is an inducible enzyme that degrades heme to carbon monoxide, iron ions, and biliverdin. Heme 61-65 heme oxygenase 1 Homo sapiens 18-22 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. Heme 46-50 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. Heme 61-65 heme oxygenase 1 Homo sapiens 0-16 12230871-3 2002 Here we present an overview of the heme degradation processes and relevant disorders by focusing on heme oxygenase-1 (HO-1), a key enzyme in heme catabolism. Heme 35-39 heme oxygenase 1 Homo sapiens 100-116 12230871-3 2002 Here we present an overview of the heme degradation processes and relevant disorders by focusing on heme oxygenase-1 (HO-1), a key enzyme in heme catabolism. Heme 35-39 heme oxygenase 1 Homo sapiens 118-122 12006183-3 2002 We have also shown that the antiapoptotic effect of HO-1 is mediated through heme catabolism into the gas carbon monoxide (CO). Heme 77-81 heme oxygenase 1 Homo sapiens 52-56 12130498-2 2002 Deficiency of the heme-catabolizing enzyme, heme oxygenase-1 (HO-1), in both a human patient and transgenic knockout mice leads to an abundance of circulating heme and damage to vascular endothelium. Heme 18-22 heme oxygenase 1 Homo sapiens 44-60 12130498-2 2002 Deficiency of the heme-catabolizing enzyme, heme oxygenase-1 (HO-1), in both a human patient and transgenic knockout mice leads to an abundance of circulating heme and damage to vascular endothelium. Heme 18-22 heme oxygenase 1 Homo sapiens 62-66 12130498-2 2002 Deficiency of the heme-catabolizing enzyme, heme oxygenase-1 (HO-1), in both a human patient and transgenic knockout mice leads to an abundance of circulating heme and damage to vascular endothelium. Heme 44-48 heme oxygenase 1 Homo sapiens 62-66 12042071-9 2002 Okadaic acid and phorbol 12-myristate 13-acetate significantly decreased heme-mediated induction of heme oxygenase-1 mRNA in both Huh-7 and HepG2 cells. Heme 73-77 heme oxygenase 1 Homo sapiens 100-116 12042071-10 2002 Wortmannin diminished the heme-mediated induction of heme oxygenase-1 mRNA in HepG2 cells, but not Huh-7 cells. Heme 26-30 heme oxygenase 1 Homo sapiens 53-69 12042074-1 2002 Heme-hemopexin coordinately regulates genes encoding protective proteins including metallothionein-I (MT-I) and heme oxygenase 1 (HO-1). Heme 0-4 heme oxygenase 1 Homo sapiens 112-128 12042074-1 2002 Heme-hemopexin coordinately regulates genes encoding protective proteins including metallothionein-I (MT-I) and heme oxygenase 1 (HO-1). Heme 0-4 heme oxygenase 1 Homo sapiens 130-134 12042074-2 2002 Hexamethylene-bisacetamide (HMBA), which induces differentiation and activates protein kinase C (PKC), synergistically augments the induction of both MT-I and MT-II mRNAs in response to heme-hemopexin, but attenuates the induction of HO-1. Heme 186-190 heme oxygenase 1 Homo sapiens 234-238 11773068-10 2002 The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected. Heme 271-275 heme oxygenase 1 Homo sapiens 96-100 11592943-1 2001 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Heme 60-64 heme oxygenase 1 Homo sapiens 0-16 11930234-1 2002 The heme oxygenase-1 (HO-1), a rate-limiting enzyme in heme metabolism, has been recently defined as a novel stress-stimulated protein, since the intracellular expression of HO-1 in response to various stimuli as oxidation, ischemia and endotoxin injury has been proved to be able to protect the cells from damage. Heme 4-8 heme oxygenase 1 Homo sapiens 174-178 11928711-3 2002 Exposure of mammalian cells to oxidative stimuli induces heme oxygenase-1 (HO-1), the rate-limiting enzyme in heme degradation, as well as the 32-kDa heat shock protein. Heme 57-61 heme oxygenase 1 Homo sapiens 75-79 11707454-2 2002 Depletion of nutrients results in cellular stress, which evokes adaptive and protective responses, one of which is the induction of heme oxygenase-1 (HO-1), a 32-kDa endoplasmic reticulum enzyme that catalyzes the rate-limiting step in heme degradation. Heme 132-136 heme oxygenase 1 Homo sapiens 150-154 11948696-5 2002 The degree of HO-1 expression and, consequently, the levels of cellular heme were directly related to COX activity. Heme 72-76 heme oxygenase 1 Homo sapiens 14-18 11752115-9 2002 The degree of HO-1 expression and, consequently, the level of cellular heme, were directly related to COX activity. Heme 71-75 heme oxygenase 1 Homo sapiens 14-18 11668058-1 2001 Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron. Heme 63-67 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. Heme 63-67 heme oxygenase 1 Homo sapiens 18-22 11668058-9 2001 These results indicate that the HO-1-bilirubin pathway can effectively defend hypoxic cardiomyocytes against reoxygenation injury and highlight the issue of heme availability in the cytoprotective action afforded by HO-1. Heme 157-161 heme oxygenase 1 Homo sapiens 216-220 11930234-1 2002 The heme oxygenase-1 (HO-1), a rate-limiting enzyme in heme metabolism, has been recently defined as a novel stress-stimulated protein, since the intracellular expression of HO-1 in response to various stimuli as oxidation, ischemia and endotoxin injury has been proved to be able to protect the cells from damage. Heme 4-8 heme oxygenase 1 Homo sapiens 22-26 15499991-3 2002 Three isoforms of heme oxygenase (HO) have been described: two constitutively expressed isoforms, HO-2 and HO-3, and an inducible isoform, HO-1 that is increased as an adaptive response to several injurious stimuli including heme, hyperoxia, hypoxia, endotoxin and heavy metals. Heme 18-22 heme oxygenase 1 Homo sapiens 139-143 11592943-1 2001 Heme oxygenase-1 (HO-1) catalyzes the rate-limiting step in heme degradation, releasing iron, carbon monoxide, and biliverdin. Heme 60-64 heme oxygenase 1 Homo sapiens 18-22 11950143-2 2001 Heme oxygenase isozymes, HO-1, HO-2 and HO-3, are HSP32 protein cognates, with a known function of catalyzing the isomer specific oxidation of the heme molecule, including that of NO synthase. Heme 147-151 heme oxygenase 1 Homo sapiens 25-44 11593038-5 2001 Overexpression of HO-1 AS was associated with a long-term decrease (45%) of endogenous HO-1 protein and an increase (167%) in unmetabolized exogenous heme in HMEC-1 cells. Heme 150-154 heme oxygenase 1 Homo sapiens 18-22 11593038-6 2001 Carbon monoxide (CO) production in HO-1 S- or AS-transduced HMEC-1 cells after heme treatment was increased (159%) or decreased (50%), respectively, compared with nontransduced cells. Heme 79-83 heme oxygenase 1 Homo sapiens 35-39 11768235-2 2001 Heme oxygenase-1, the major inducible isoform of heme oxygenase (HO), can be induced by heme and numerous other physical and chemical factors, many of which cause cellular "stress". Heme 49-53 heme oxygenase 1 Homo sapiens 0-16 11768235-12 2001 Our results are consistent with the proposition that induction of HO-1 by PAO involves inhibition of specific PTP(s), and that the mechanisms of induction of HO-1 by PAO and by heme may share some common pathways. Heme 177-181 heme oxygenase 1 Homo sapiens 66-70 11768235-12 2001 Our results are consistent with the proposition that induction of HO-1 by PAO involves inhibition of specific PTP(s), and that the mechanisms of induction of HO-1 by PAO and by heme may share some common pathways. Heme 177-181 heme oxygenase 1 Homo sapiens 158-162 11435909-3 2001 HO-1 metabolizes heme to the antioxidant bilirubin and carbon monoxide, and represents a powerful endogenous defensive mechanism against free radicals in many diseases. Heme 17-21 heme oxygenase 1 Homo sapiens 0-4 23045067-1 2001 Heme oxygenase 1 and 2 activities are responsible for initiating most of the degradation of heme, although other enzyme pathways play a role as well. Heme 92-96 heme oxygenase 1 Homo sapiens 0-22 11194943-4 2001 Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant. Heme 57-61 heme oxygenase 1 Homo sapiens 0-16 11194943-4 2001 Heme oxygenase-1 (HO-1) is an inducible enzyme degrading heme into the gaseous mediator carbon monoxide (CO) and biliverdin, a local antioxidant. Heme 57-61 heme oxygenase 1 Homo sapiens 18-22 11247059-1 2001 STUDY OBJECTIVES: In the absence of heme oxygenase-1 (HO-1), which catalyzes the oxidation of heme to generate carbon monoxide and indirect bilirubin, hypoxia induces severe right ventricular dilation and infarction. Heme 36-40 heme oxygenase 1 Homo sapiens 54-58 11950143-2 2001 Heme oxygenase isozymes, HO-1, HO-2 and HO-3, are HSP32 protein cognates, with a known function of catalyzing the isomer specific oxidation of the heme molecule, including that of NO synthase. Heme 147-151 heme oxygenase 1 Homo sapiens 50-55 11007950-1 2000 Heme oxygenase (HO)-1 is the inducible isoform of the rate-limiting enzyme of heme degradation. Heme 78-82 heme oxygenase 1 Homo sapiens 0-21 11135063-10 2001 CONCLUSION: We conclude that up-regulation of HO-1 occurs in the kidney in humans and rats repetitively exposed to heme proteins. Heme 115-119 heme oxygenase 1 Homo sapiens 46-50 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. Heme 63-67 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. Heme 14-18 heme oxygenase 1 Homo sapiens 119-141 11015442-3 2000 Overexpression of HO-1, or induction of HO-1 expression by heme, protects endothelial cells (ECs) from apoptosis. Heme 59-63 heme oxygenase 1 Homo sapiens 40-44 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. Heme 14-18 heme oxygenase 1 Homo sapiens 143-149 11053673-2 2000 Heme oxygenase-1 (HO-1) is a 32kDa stress protein that degrades heme to biliverdin, free iron and carbon monoxide. Heme 64-68 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. Heme 64-68 heme oxygenase 1 Homo sapiens 18-22 10733947-1 2000 Heme oxygenase-1 is the heme catabolic enzyme induced in human dermal fibroblasts by environmental stress. Heme 24-28 heme oxygenase 1 Homo sapiens 0-16 10773020-9 2000 The increase in HO activity after adenoviral-mediated human HO-1 transfer was associated with a decrease in microsomal heme-CYP and CYP activity. Heme 119-123 heme oxygenase 1 Homo sapiens 60-64 10653390-9 2000 To explore the hypothesis that these peptides exert their immunosuppressive effect by altering HO-1 activity, animals were treated with iron protoporphyrin, an inducer of HO-1 activity, or tin protoporphyrin, an inhibitor of HO-1. Heme 136-155 heme oxygenase 1 Homo sapiens 171-175 10746601-1 2000 BACKGROUND: Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that catalyzes the degradation of heme to biliverdin. Heme 97-101 heme oxygenase 1 Homo sapiens 12-28 10746601-1 2000 BACKGROUND: Heme oxygenase-1 (HO-1) is a 32-kDa stress protein that catalyzes the degradation of heme to biliverdin. Heme 97-101 heme oxygenase 1 Homo sapiens 30-34 10681502-0 2000 Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1. Heme 79-83 heme oxygenase 1 Homo sapiens 93-109 10681514-4 2000 In transfected cells overexpressing HO-1, the activity of heme oxygenase was increased, and conversely, the level of tau protein was dramatically decreased when compared with antisense HO-1 or CEP transfected cells. Heme 58-62 heme oxygenase 1 Homo sapiens 36-40 10653390-9 2000 To explore the hypothesis that these peptides exert their immunosuppressive effect by altering HO-1 activity, animals were treated with iron protoporphyrin, an inducer of HO-1 activity, or tin protoporphyrin, an inhibitor of HO-1. Heme 136-155 heme oxygenase 1 Homo sapiens 171-175 10490932-17 1999 It is possible that amelioration of the heme-induced oxidative stress and expression of ICAM-I is due, in part, to the induction of HO-1 activity. Heme 40-44 heme oxygenase 1 Homo sapiens 132-136 10517538-3 1999 We have observed that heme is released from microsomal heme-containing proteins by UVA and other oxidants and that activation of HO-1 expression by UVA correlates with levels of heme release. Heme 22-26 heme oxygenase 1 Homo sapiens 129-133 10629191-4 2000 The product of the hemO gene is homologous to enzymes that degrade heme; 21% of its amino acid residues are identical, and 44% are similar, to those of the human heme oxygenase-1. Heme 67-71 heme oxygenase 1 Homo sapiens 162-178 10630670-3 1999 However, as attempts are made to unravel the mechanisms by which HO-1 is induced and as we discover that CO, iron and bilirubin may be important effector molecules, we are learning to appreciate that heme oxygenases may be central to the regulation of many physiological and pathophysiological processes besides their established function in heme catabolism. Heme 200-204 heme oxygenase 1 Homo sapiens 65-69 10564544-4 1999 Endothelial cells treated with heme (10 microM) and IL-6 (25 ng/ml), increased HO-1 mRNA 15- and 60-fold, respectively. Heme 31-35 heme oxygenase 1 Homo sapiens 79-83 10490932-4 1999 Additionally, we studied HO-1 expression in experimental models of adhesion molecule expression produced by heme in endothelial cells, and the relationship of HO-1 expression to the induced adhesion molecules. Heme 108-112 heme oxygenase 1 Homo sapiens 25-29 10490932-9 1999 Endothelial cells exposed to heme elicited increased HO activity, which was prevented (70%) by HO-1 antisense ODNs. Heme 29-33 heme oxygenase 1 Homo sapiens 95-99 10490932-11 1999 Addition of HO-1 antisense ODNs prevented heme degradation and resulted in elevation of microsomal heme. Heme 42-46 heme oxygenase 1 Homo sapiens 12-16 10490932-11 1999 Addition of HO-1 antisense ODNs prevented heme degradation and resulted in elevation of microsomal heme. Heme 99-103 heme oxygenase 1 Homo sapiens 12-16 10490932-13 1999 Incubation of endothelial cells with HO-1 antisense enhanced heme-dependent increase of ICAM-1. Heme 61-65 heme oxygenase 1 Homo sapiens 37-41 10491455-3 1999 Exhaled carbon monoxide (CO), a product of heme degradation by heme oxygenase 1 (HO-1) which is induced by inflammatory cytokines and oxidants, was therefore tested as a non-invasive marker of airway inflammation and oxidative stress. Heme 43-47 heme oxygenase 1 Homo sapiens 81-85 10193374-3 1998 HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO). Heme 17-21 heme oxygenase 1 Homo sapiens 0-4 10409239-2 1999 Overexpression of HO-1 in cells might, therefore, protect against oxidative stress produced by certain agents, specifically heme, by catalyzing its degradation to bilirubin, which by itself has antioxidant properties. Heme 124-128 heme oxygenase 1 Homo sapiens 18-22 10409239-6 1999 Moreover, human HO-1 gene-transduced endothelial cells acquired substantial resistance to toxicity produced by exposure to heme and H(2)O(2) compared with that in nontransduced cells. Heme 123-127 heme oxygenase 1 Homo sapiens 16-20 10409239-7 1999 The protective effect of enhancement of HO-1 activity against heme and H(2)O(2) was reversed by pretreatment with stannic mesoporphyrin, a competitive inhibitor of HO. Heme 62-66 heme oxygenase 1 Homo sapiens 40-44 10101013-3 1999 Recently, heme oxygenase 1 (HO-1), the rate-limiting enzyme in the metabolism of heme, has been found to have a protective role in oxidant injury. Heme 10-14 heme oxygenase 1 Homo sapiens 28-32 10101013-11 1999 We also evaluated 4.5 kb of the human HO-1 promoter region and demonstrated that this region has promoter activity to the stimulus heme; however, there was no evidence of promoter activity to either iron or hyperoxia. Heme 131-135 heme oxygenase 1 Homo sapiens 38-42 10101013-12 1999 This diversity of promoter activity to heme, heavy metals, and hyperoxia is unique to the human HO-1 gene. Heme 39-43 heme oxygenase 1 Homo sapiens 96-100 10218639-0 1999 Cyclooxygenase dependent release of heme from microsomal hemeproteins correlates with induction of heme oxygenase 1 transcription in human fibroblasts. Heme 36-40 heme oxygenase 1 Homo sapiens 99-115 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. Heme 85-89 heme oxygenase 1 Homo sapiens 71-75 10218639-4 1999 We also demonstrate a high degree of correlation between the amount of heme released and the degree of subsequent induction of heme oxygenase 1 transcription following UVA and hydrogen peroxide treatment. Heme 71-75 heme oxygenase 1 Homo sapiens 127-143 10218639-5 1999 We propose that release of heme from microsomal hemeproteins determines the degree of induction of heme oxygenase 1 transcription in human fibroblasts after oxidative stress. Heme 27-31 heme oxygenase 1 Homo sapiens 99-115 9402154-3 1997 Indirect immunofluorescence double labeling studies demonstrated a simultaneous increase of ICAM-1 and HO-1 after exposure of cells to heme for 24 hr. Heme 135-139 heme oxygenase 1 Homo sapiens 103-107 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. Heme 42-46 heme oxygenase 1 Homo sapiens 100-104 9828853-3 1998 HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO). Heme 17-21 heme oxygenase 1 Homo sapiens 0-4 9402154-9 1997 These results suggest that upregulation of ICAM-1, VCAM-1, and E selectin expression is associated with oxidative stress induced by hemoglobin/heme and that HO-1 may play a modulating role via its ability to degrade heme to a substance with antioxidant properties. Heme 216-220 heme oxygenase 1 Homo sapiens 157-161 9225984-2 1997 Heme oxygenase-1 (HO-1), a key enzyme in heme catabolism, also functions as an antioxidant enzyme. Heme 41-45 heme oxygenase 1 Homo sapiens 0-16 9337616-8 1997 Because either hemin alone or UVA radiation are able to lead to a refractoriness of the heme oxygenase-1 gene to reinduction by a second exposure to one or the other agent in human fibroblasts, we conclude that heme, or an as yet unidentified heme derivative, is involved in the refractoriness response. Heme 211-215 heme oxygenase 1 Homo sapiens 88-104 9295197-7 1997 Heme oxygenase-1 (HO-1) markedly reduced the activity of both the endogenous AD inhibitor and hemin, indicating that the endogenous inhibitor contains heme. Heme 151-155 heme oxygenase 1 Homo sapiens 0-16 9295197-7 1997 Heme oxygenase-1 (HO-1) markedly reduced the activity of both the endogenous AD inhibitor and hemin, indicating that the endogenous inhibitor contains heme. Heme 151-155 heme oxygenase 1 Homo sapiens 18-22 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. Heme 37-41 heme oxygenase 1 Homo sapiens 55-60 9225984-2 1997 Heme oxygenase-1 (HO-1), a key enzyme in heme catabolism, also functions as an antioxidant enzyme. Heme 41-45 heme oxygenase 1 Homo sapiens 18-22 8816811-2 1996 Heme oxygenase-1 (HO-1) is inducible not only by its heme substrate, but also by a variety of agents causing oxidative stress. Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 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. Heme 130-134 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. Heme 130-134 heme oxygenase 1 Homo sapiens 94-99 8816811-2 1996 Heme oxygenase-1 (HO-1) is inducible not only by its heme substrate, but also by a variety of agents causing oxidative stress. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 8816811-11 1996 Taken together, our data suggest that overexpression of HO-1 results in cell growth arrest, which may facilitate cellular protection against non-heme-mediated oxidant insult such as hyperoxia. Heme 145-149 heme oxygenase 1 Homo sapiens 56-60 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). Heme 63-67 heme oxygenase 1 Homo sapiens 83-107 8679227-8 1996 Since the identification of HO-1 in 1968, many of the studies involving this enzyme were understandably focused on the regulation and function of HO-1 in heme metabolism. Heme 154-158 heme oxygenase 1 Homo sapiens 28-32 8679227-8 1996 Since the identification of HO-1 in 1968, many of the studies involving this enzyme were understandably focused on the regulation and function of HO-1 in heme metabolism. Heme 154-158 heme oxygenase 1 Homo sapiens 146-150 8679227-9 1996 This emphasis is self-evident as HO-1 catalyzes the first and rate-limiting step in heme degradation. Heme 84-88 heme oxygenase 1 Homo sapiens 33-37 8679227-10 1996 Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins. Heme 128-132 heme oxygenase 1 Homo sapiens 86-90 8679227-10 1996 Interestingly, however, evidence accumulated over the past 25 years demonstrates that HO-1 is induced not only by the substrate heme but also by a variety of non-heme inducers such as heavy metals, endotoxin, heat shock, inflammatory cytokines, and prostaglandins. Heme 162-166 heme oxygenase 1 Homo sapiens 86-90 8679227-11 1996 The chemical diversity of HO-1 inducers led to the speculation that HO-1, besides its role in heme degradation, may also play a vital function in maintaining cellular homeostasis. Heme 94-98 heme oxygenase 1 Homo sapiens 26-30 8679227-11 1996 The chemical diversity of HO-1 inducers led to the speculation that HO-1, besides its role in heme degradation, may also play a vital function in maintaining cellular homeostasis. Heme 94-98 heme oxygenase 1 Homo sapiens 68-72 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. Heme 155-159 heme oxygenase 1 Homo sapiens 37-50 8650873-8 1996 HO-1 in the prostate tissue was found catalytically active and oxidatively cleaved the heme molecule (Fe-protoporphyrin IX) to biliverdin. Heme 87-91 heme oxygenase 1 Homo sapiens 0-4 8654390-1 1996 Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide. Heme 43-47 heme oxygenase 1 Homo sapiens 0-16 8654390-1 1996 Heme oxygenase 1 is an essential enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide. Heme 72-76 heme oxygenase 1 Homo sapiens 0-16 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). Heme 63-67 heme oxygenase 1 Homo sapiens 109-113 8547275-7 1996 These results place His-132 close to the iron on the distal side of the heme pocket and indicate that His-132 facilitates, but is not absolutely required for, the catalytic turnover of HO-1. Heme 72-76 heme oxygenase 1 Homo sapiens 185-189 8030754-1 1994 Heme oxygenase-1 is an important enzyme that degrades heme, a pro-oxidant, leading to the formation of antioxidant molecules. Heme 54-58 heme oxygenase 1 Homo sapiens 0-16 7703255-3 1995 The purified, truncated hHO-1/heme complex is spectroscopically indistinguishable from that of the rat enzyme and converts heme to biliverdin when reconstituted with rat liver cytochrome P450 reductase. Heme 30-34 heme oxygenase 1 Homo sapiens 24-29 7703255-3 1995 The purified, truncated hHO-1/heme complex is spectroscopically indistinguishable from that of the rat enzyme and converts heme to biliverdin when reconstituted with rat liver cytochrome P450 reductase. Heme 123-127 heme oxygenase 1 Homo sapiens 24-29 8146161-1 1994 Oxidative stress of human skin fibroblasts by treatment with ultraviolet A (UVA) radiation has been shown to lead to an increase in levels of the heme catabolizing enzyme heme oxygenase 1 [heme, hydrogen-donor:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating), EC 1.14.99.3] and the iron storage protein ferritin. Heme 146-150 heme oxygenase 1 Homo sapiens 171-187 8016102-3 1994 Heme treatment increased both HO activity and HO-1 mRNA in the human erythroleukemic cell line K562. Heme 0-4 heme oxygenase 1 Homo sapiens 46-50 8455037-1 1993 In mammalian systems, the heme oxygenase (HO) isozymes HO-1 (HSP32) and HO-2 oxidatively cleave the heme molecule to produce bile pigments and carbon monoxide. Heme 26-30 heme oxygenase 1 Homo sapiens 61-66 19912946-2 1993 The sole source of CO in mammalian systems is the alpha-meso carbon bridge of the heme molecule cleaved by heme oxygenase isozymes, HO-1 and HO-2. Heme 82-86 heme oxygenase 1 Homo sapiens 132-145 29628790-1 2018 Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties. Heme 77-81 heme oxygenase 1 Homo sapiens 0-22 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. Heme 64-68 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. Heme 64-68 heme oxygenase 1 Homo sapiens 18-22 33804563-1 2021 Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin. Heme 79-83 heme oxygenase 1 Homo sapiens 0-16 33804563-1 2021 Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin. Heme 79-83 heme oxygenase 1 Homo sapiens 18-22 33804563-1 2021 Heme oxygenase-1 (HO-1, encoded by HMOX1) is a cytoprotective enzyme degrading heme into CO, Fe2+, and biliverdin. Heme 79-83 heme oxygenase 1 Homo sapiens 35-40 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. Heme 15-19 heme oxygenase 1 Homo sapiens 33-37 29628790-1 2018 Heme oxygenase-1 (HO-1, encoded by HMOX1) through degradation of pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin, exhibits cytoprotective, anti-apoptotic and anti-inflammatory properties. Heme 77-81 heme oxygenase 1 Homo sapiens 35-40 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. Heme 76-80 heme oxygenase 1 Homo sapiens 0-16 25493608-10 2015 This could reflect decreases in cellular heme caused by the massive induction by arsenite of heme oxygenase mRNA (HMOX1; 68-fold increase), the rate-limiting enzyme in heme catabolism. Heme 41-45 heme oxygenase 1 Homo sapiens 114-119 34863556-7 2022 Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin. Heme 139-143 heme oxygenase 1 Homo sapiens 106-122 34863556-7 2022 Moreover, TinPPIX further augments the free heme level along with amplifies the CDT efficacy by disabling heme oxygenase-1 (HO-1)-mediated heme conversion into antioxidative bilirubin. Heme 139-143 heme oxygenase 1 Homo sapiens 124-128 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. Heme 76-80 heme oxygenase 1 Homo sapiens 18-22 34800278-2 2022 HO-1 catalyzes heme breakdown, reducing the levels of this important oxidant molecule and generating antioxidant, anti-inflammatory, and anti-apoptotic byproducts. Heme 15-19 heme oxygenase 1 Homo sapiens 0-4 34927515-8 2022 Furthermore, 5-ALA is a metabolic precursor of heme, which is a potent inducer of the enzyme heme oxygenase-1, the levels of which are decreased in patients with severe COVID-19. Heme 47-51 heme oxygenase 1 Homo sapiens 93-109 34917622-3 2021 Studies have demonstrated that heme oxygenase 1 (HO-1), an inducible enzyme catalyzing heme degradation, exhibits anti-inflammatory, anti-oxidative stress and anti-apoptosis properties. Heme 87-91 heme oxygenase 1 Homo sapiens 31-47 34917622-3 2021 Studies have demonstrated that heme oxygenase 1 (HO-1), an inducible enzyme catalyzing heme degradation, exhibits anti-inflammatory, anti-oxidative stress and anti-apoptosis properties. Heme 87-91 heme oxygenase 1 Homo sapiens 49-53 34973332-2 2022 Humans express two isoforms of HO: the inducible HO-1, which is up-regulated in response to various stressors, including excess heme, and the constitutive HO-2. Heme 128-132 heme oxygenase 1 Homo sapiens 49-53 34973332-8 2022 When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation. Heme 5-9 heme oxygenase 1 Homo sapiens 24-28 34973332-8 2022 When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation. Heme 5-9 heme oxygenase 1 Homo sapiens 58-62 34973332-8 2022 When heme is in excess, HO-1 is induced and both HO-2 and HO-1 can provide protection from heme toxicity via enzymatic degradation. Heme 91-95 heme oxygenase 1 Homo sapiens 58-62 34874275-0 2021 HIF1A-induced heme oxygenase 1 promotes the survival of decidual stromal cells against excess heme-mediated oxidative stress. Heme 94-98 heme oxygenase 1 Homo sapiens 14-30 34874275-1 2021 Heme oxygenase 1 (HO-1, encoded by the HMOX1 gene), is the rate-limiting enzyme that catalyzes heme degradation, and it has been reported to exert antioxidative effects. Heme 95-99 heme oxygenase 1 Homo sapiens 0-16 34874275-1 2021 Heme oxygenase 1 (HO-1, encoded by the HMOX1 gene), is the rate-limiting enzyme that catalyzes heme degradation, and it has been reported to exert antioxidative effects. Heme 95-99 heme oxygenase 1 Homo sapiens 18-22 34874275-1 2021 Heme oxygenase 1 (HO-1, encoded by the HMOX1 gene), is the rate-limiting enzyme that catalyzes heme degradation, and it has been reported to exert antioxidative effects. Heme 95-99 heme oxygenase 1 Homo sapiens 39-44 34874275-10 2021 This study suggests that the upregulation of HO-1 expression via HIF1A protects DSCs against excessive heme-mediated oxidative stress. Heme 103-107 heme oxygenase 1 Homo sapiens 45-49 34866353-14 2022 Heme was the most abundant metabolite in degenerated regions, whereas Heme oxygenase-1 (HO-1), which catabolizes heme, was found in intact regions. Heme 113-117 heme oxygenase 1 Homo sapiens 70-86 34866353-14 2022 Heme was the most abundant metabolite in degenerated regions, whereas Heme oxygenase-1 (HO-1), which catabolizes heme, was found in intact regions. Heme 113-117 heme oxygenase 1 Homo sapiens 88-92 34866353-15 2022 Higher HO-1 levels correlated with lower heme accumulation. Heme 41-45 heme oxygenase 1 Homo sapiens 7-11 34943041-2 2021 The parasite regulates the host immune system by inducing a strong Th2 and regulatory T (Treg) cell immune response through mechanisms that might involve the expression or activity of heme-oxygenase-1 (HO-1), the rate-limiting enzyme in the catabolism of free heme that also has immunoregulatory and antioxidant properties. Heme 260-264 heme oxygenase 1 Homo sapiens 202-206 34634993-1 2021 BACKGROUND: Heme oxygenase (HO)-1 is a rate-limiting enzyme for degrading heme into carbon monoxide. Heme 74-78 heme oxygenase 1 Homo sapiens 12-33 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. Heme 152-156 heme oxygenase 1 Homo sapiens 63-79 34688156-2 2021 With the continuous deepening of research, in addition to directly regulating redox by catalyzing the degradation of heme, HO-1 protein also participates in the gene expression level in a great diversity of methods, thereby initiating cell defense. Heme 117-121 heme oxygenase 1 Homo sapiens 123-127 34728736-8 2021 Free iron and biliverdin, which are metabolic byproducts of heme catalysis by HO-1, also suppressed the viral infection. Heme 60-64 heme oxygenase 1 Homo sapiens 78-82 34453944-1 2021 AIM: Biliverdin reductase-A (BVR-A) other than its canonical role in the degradation pathway of heme as partner of heme oxygenase-1 (HO1), has recently drawn attention as a protein with pleiotropic functions involved in insulin-glucose homeostasis. Heme 96-100 heme oxygenase 1 Homo sapiens 115-131 34453944-1 2021 AIM: Biliverdin reductase-A (BVR-A) other than its canonical role in the degradation pathway of heme as partner of heme oxygenase-1 (HO1), has recently drawn attention as a protein with pleiotropic functions involved in insulin-glucose homeostasis. Heme 96-100 heme oxygenase 1 Homo sapiens 133-136 34241977-2 2021 The inhibition of HO-1 through imidazole-based drugs, which is non-competitive with heme, is a focus of anticancer drug research. Heme 84-88 heme oxygenase 1 Homo sapiens 18-22 34089821-1 2021 The intracellular enzyme heme oxygenase-1 (HO-1) is responsible for the degradation of cell-free (cf) heme. Heme 102-106 heme oxygenase 1 Homo sapiens 25-41 34089821-1 2021 The intracellular enzyme heme oxygenase-1 (HO-1) is responsible for the degradation of cell-free (cf) heme. Heme 102-106 heme oxygenase 1 Homo sapiens 43-47 34583348-3 2021 Erythrocyte destruction results in increased release of cytotoxic free heme that is scavenged by haptoglobin (Hp), hemopexin (Hx) and heme oxygenase-1 (HO-1). Heme 71-75 heme oxygenase 1 Homo sapiens 134-150 34583348-3 2021 Erythrocyte destruction results in increased release of cytotoxic free heme that is scavenged by haptoglobin (Hp), hemopexin (Hx) and heme oxygenase-1 (HO-1). Heme 71-75 heme oxygenase 1 Homo sapiens 152-156 34472337-1 2021 Heme oxygenase-1 (HO-1) promotes heme catabolism exercising cytoprotective roles in normal and cancer cells. Heme 33-37 heme oxygenase 1 Homo sapiens 0-16 34472337-1 2021 Heme oxygenase-1 (HO-1) promotes heme catabolism exercising cytoprotective roles in normal and cancer cells. Heme 33-37 heme oxygenase 1 Homo sapiens 18-22 34321570-2 2021 Quantifying circadian disruption by analyzing expression of the circadian gene period circadian regulator 2 (PER2) and heme oxygenase 1 (HO1), which determines heme turnover, may prove to be potential diagnostic tools. Heme 160-164 heme oxygenase 1 Homo sapiens 119-135 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. Heme 114-118 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. Heme 114-118 heme oxygenase 1 Homo sapiens 18-22 34504854-4 2021 Heme oxygenase-1 (HO-1), an enzyme involved in the process of heme degradation, has attracted widespread attention in recent years due to its cytoprotective properties. Heme 62-66 heme oxygenase 1 Homo sapiens 0-16 34504854-4 2021 Heme oxygenase-1 (HO-1), an enzyme involved in the process of heme degradation, has attracted widespread attention in recent years due to its cytoprotective properties. Heme 62-66 heme oxygenase 1 Homo sapiens 18-22 34321570-2 2021 Quantifying circadian disruption by analyzing expression of the circadian gene period circadian regulator 2 (PER2) and heme oxygenase 1 (HO1), which determines heme turnover, may prove to be potential diagnostic tools. Heme 160-164 heme oxygenase 1 Homo sapiens 137-140 34290541-3 2021 In 2018, we reported that heme oxygenase-1 (HO-1), an inducible stress response protein important for heme catabolism and implicated in PD pathology, was higher in PD saliva relative to healthy controls, suggesting that salivary HO-1 may serve as a potential biomarker of PD. Heme 102-106 heme oxygenase 1 Homo sapiens 26-42 34290541-3 2021 In 2018, we reported that heme oxygenase-1 (HO-1), an inducible stress response protein important for heme catabolism and implicated in PD pathology, was higher in PD saliva relative to healthy controls, suggesting that salivary HO-1 may serve as a potential biomarker of PD. Heme 102-106 heme oxygenase 1 Homo sapiens 44-48 35565370-3 2022 We quantified the heme-degrading enzyme, heme oxygenase-1 (HO-1, encoded by Hmox1) in normal peritoneum, endometriotic lesions and endometriosis-associated ovarian cancer (EAOC) of clear cell type (OCCC). Heme 18-22 heme oxygenase 1 Homo sapiens 41-57 34073678-7 2021 Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Heme 0-4 heme oxygenase 1 Homo sapiens 20-36 34073678-7 2021 Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Heme 0-4 heme oxygenase 1 Homo sapiens 38-42 34073678-7 2021 Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Heme 76-80 heme oxygenase 1 Homo sapiens 20-36 34073678-7 2021 Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Heme 76-80 heme oxygenase 1 Homo sapiens 38-42 34073678-8 2021 Therapeutic strategies targeting the heme/HO-1 pathway, including therapeutic modulation of heme levels, elevation (or inhibition) of HO-1 protein and activity, and application of CO donor compounds or gas show potential in inflammatory conditions including sepsis and pulmonary diseases. Heme 37-41 heme oxygenase 1 Homo sapiens 42-46 35551540-1 2022 INTRODUCTION: Heme-oxygenase 1 (HMOX1) is a critical stress response gene that catalyzes the multistep oxidation of heme. Heme 116-120 heme oxygenase 1 Homo sapiens 14-30 35551540-1 2022 INTRODUCTION: Heme-oxygenase 1 (HMOX1) is a critical stress response gene that catalyzes the multistep oxidation of heme. Heme 116-120 heme oxygenase 1 Homo sapiens 32-37 35428017-2 2022 The aim of this study was to investigate the role of heme in HO-1 and HO-2 induced colorectal carcinogenesis and the clinicopathological significance of their expressions in patients with colorectal carcinoma (CRC). Heme 53-57 heme oxygenase 1 Homo sapiens 61-65 35565370-3 2022 We quantified the heme-degrading enzyme, heme oxygenase-1 (HO-1, encoded by Hmox1) in normal peritoneum, endometriotic lesions and endometriosis-associated ovarian cancer (EAOC) of clear cell type (OCCC). Heme 18-22 heme oxygenase 1 Homo sapiens 59-63 35565370-3 2022 We quantified the heme-degrading enzyme, heme oxygenase-1 (HO-1, encoded by Hmox1) in normal peritoneum, endometriotic lesions and endometriosis-associated ovarian cancer (EAOC) of clear cell type (OCCC). Heme 18-22 heme oxygenase 1 Homo sapiens 76-81 35631320-0 2022 Activation of Nrf2/HO-1 Antioxidant Pathway by Heme Attenuates Calcification of Human Lens Epithelial Cells. Heme 47-51 heme oxygenase 1 Homo sapiens 19-23 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. Heme 71-75 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. Heme 71-75 heme oxygenase 1 Homo sapiens 18-22 35631320-8 2022 We used heme to activate Nrf2, which strongly upregulated the expression of Nrf2 and heme oxygenase-1 (HO-1). Heme 8-12 heme oxygenase 1 Homo sapiens 85-101 35631320-8 2022 We used heme to activate Nrf2, which strongly upregulated the expression of Nrf2 and heme oxygenase-1 (HO-1). Heme 8-12 heme oxygenase 1 Homo sapiens 103-107 35631320-11 2022 Anti-calcification effect of heme was lost when the transcriptional activity of Nrf2 or the enzyme activity of HO-1 was blocked with pharmacological inhibitors. Heme 29-33 heme oxygenase 1 Homo sapiens 111-115 35631320-12 2022 Among products of HO-1 catalyzed heme degradation iron mimicked the anti-calcification effect of heme. Heme 33-37 heme oxygenase 1 Homo sapiens 18-22 35631320-12 2022 Among products of HO-1 catalyzed heme degradation iron mimicked the anti-calcification effect of heme. Heme 97-101 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. Heme 18-22 heme oxygenase 1 Homo sapiens 56-60 35631320-13 2022 We concluded that heme-induced upregulation of the Nrf2/HO-1 system inhibits HuLECs calcification through the liberation of heme iron. Heme 124-128 heme oxygenase 1 Homo sapiens 56-60 35281042-2 2022 Heme oxygenase-1 (HO-1) is an essential stress-response enzyme highly expressed in the lungs, and catabolizes heme into ferrous iron, carbon monoxide (CO), and biliverdin (BV)/bilirubin (BR), especially in pathological conditions which cause oxidative stress and inflammation. Heme 110-114 heme oxygenase 1 Homo sapiens 18-22 35396005-3 2022 Heme oxygenase 1 (HO 1) is a key rate limiting enzyme in the process of heme metabolism, which has the functions of anti inflammation, anti oxidation, anti apoptosis, anti aging, reducing cell damage and promoting angiogenesis. Heme 72-76 heme oxygenase 1 Homo sapiens 0-16 35396005-3 2022 Heme oxygenase 1 (HO 1) is a key rate limiting enzyme in the process of heme metabolism, which has the functions of anti inflammation, anti oxidation, anti apoptosis, anti aging, reducing cell damage and promoting angiogenesis. Heme 72-76 heme oxygenase 1 Homo sapiens 18-22 35419301-2 2022 HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron. Heme 15-19 heme oxygenase 1 Homo sapiens 0-4 34999313-5 2022 In non-transfected cells, we also observed TNF-alpha-induced VCAM1 overexpression as well as heme-induced overexpression of HMOX1 in both cell models. Heme 93-97 heme oxygenase 1 Homo sapiens 124-129 33903766-2 2021 Here we show that a distinct subset of TAMs (F4/80hiCD115hiC3aRhiCD88hi), endowed with high rates of heme catabolism by the stress-responsive enzyme heme oxygenase-1 (HO-1), plays a critical role in shaping a prometastatic tumor microenvironment favoring immunosuppression, angiogenesis and epithelial-to-mesenchymal transition. Heme 101-105 heme oxygenase 1 Homo sapiens 149-165 3290025-1 1988 In biological systems oxidation of heme is carried out by two isozymes of the microsomal heme oxygenase, HO-1 and HO-2. Heme 35-39 heme oxygenase 1 Homo sapiens 105-118 3290025-9 1988 In vivo induction of HO-1 activity in the liver is accompanied by decreases in the total P-450 levels and, in a reconstituted system, cytochrome P-450b heme can be quantitatively converted to biliverdin by HO-1 and HO-2. Heme 152-156 heme oxygenase 1 Homo sapiens 21-25 33388910-1 2021 Heme oxygenase (HO)-1 is a rate-limiting enzyme for degrading heme into carbon monoxide. Heme 62-66 heme oxygenase 1 Homo sapiens 0-21 35204159-1 2022 Heme oxygenase 1 (HO-1), the rate-limiting enzyme in heme degradation, is involved in the maintenance of cellular homeostasis, exerting a cytoprotective role by its antioxidative and anti-inflammatory functions. Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 35204159-1 2022 Heme oxygenase 1 (HO-1), the rate-limiting enzyme in heme degradation, is involved in the maintenance of cellular homeostasis, exerting a cytoprotective role by its antioxidative and anti-inflammatory functions. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 33905708-6 2021 RESULTS: Heme supports carcinogenesis via modulation of immune cell function, promoting inflammation and gut dysbiosis, impeding tumour suppressive potential of P53 gene, promoting cellular cytotoxicity and reactive oxygen species generation and modulating Nfr2 /HO-1 axis. Heme 9-13 heme oxygenase 1 Homo sapiens 263-267 33845576-1 2021 Heme oxygenase-1 (HO-1) is a vital enzyme in humans that primarily regulates free heme concentrations. Heme 82-86 heme oxygenase 1 Homo sapiens 0-16 33845576-1 2021 Heme oxygenase-1 (HO-1) is a vital enzyme in humans that primarily regulates free heme concentrations. Heme 82-86 heme oxygenase 1 Homo sapiens 18-22 33845576-8 2021 Finally, through the analysis of Fe-L2, we have shown that close structural analogues of heme are required to maintain HO-1 activity. Heme 89-93 heme oxygenase 1 Homo sapiens 119-123 33903766-2 2021 Here we show that a distinct subset of TAMs (F4/80hiCD115hiC3aRhiCD88hi), endowed with high rates of heme catabolism by the stress-responsive enzyme heme oxygenase-1 (HO-1), plays a critical role in shaping a prometastatic tumor microenvironment favoring immunosuppression, angiogenesis and epithelial-to-mesenchymal transition. Heme 101-105 heme oxygenase 1 Homo sapiens 167-171 33537805-2 2021 HO-1 can be induced by a variety of stimuli, including heavy metals, heat shock, inflammatory stimuli, heme and its derivatives, stress, hypoxia, and biological hormones. Heme 103-107 heme oxygenase 1 Homo sapiens 0-4 33920891-0 2021 Heme-Mediated Activation of the Nrf2/HO-1 Axis Attenuates Calcification of Valve Interstitial Cells. Heme 0-4 heme oxygenase 1 Homo sapiens 37-41 33920891-7 2021 Heme induced Nrf2 and HO-1 expression in VICs. Heme 0-4 heme oxygenase 1 Homo sapiens 22-26 33920891-8 2021 Heme lost its anti-calcification potential when we blocked transcriptional activity Nrf2 or enzyme activity of HO-1. Heme 0-4 heme oxygenase 1 Homo sapiens 111-115 33920891-10 2021 This study suggests that heme-mediated activation of the Nrf2/HO-1 pathway inhibits the calcification of VICs. Heme 25-29 heme oxygenase 1 Homo sapiens 62-66 33754715-1 2021 Human heme oxygenase (hHO-1) is a physiologically important enzyme responsible for free heme catabolism. Heme 6-10 heme oxygenase 1 Homo sapiens 22-27 33923744-3 2021 The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body"s antioxidant response to oxidative stress. Heme 325-329 heme oxygenase 1 Homo sapiens 20-24 33537805-3 2021 HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron. Heme 36-40 heme oxygenase 1 Homo sapiens 0-4 33537805-3 2021 HO-1 is the rate-limiting enzyme of heme catabolism, which splits heme into biliverdin, carbon monoxide (CO) and iron. Heme 66-70 heme oxygenase 1 Homo sapiens 0-4 33787980-3 2021 In this review, we summarize how this complex system is regulated by the heme oxygenase-1 (HO-1)-an enzyme, which degrades heme to biliverdin, ferrous ion and carbon monoxide. Heme 73-77 heme oxygenase 1 Homo sapiens 91-95 33716792-6 2021 Heme oxygenase-1 (HO-1), a phase II detoxification enzyme responsible for heme catabolism, is induced by oxidative stress, among others. Heme 74-78 heme oxygenase 1 Homo sapiens 0-16 33868304-1 2021 Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+). Heme 126-130 heme oxygenase 1 Homo sapiens 0-16 33868304-1 2021 Heme oxygenase-1 (HO-1) is an inducible intracellular enzyme that is expressed in response to a variety of stimuli to degrade heme, which generates the biologically active catabolites carbon monoxide (CO), biliverdin and ferrous iron (Fe2+). Heme 126-130 heme oxygenase 1 Homo sapiens 18-22 33868304-4 2021 Intrinsically to the cell, HO-1 activity provides antioxidant, anti-apoptotic and cytoprotective effects via its catabolites as well as clearing toxic intracellular heme. Heme 165-169 heme oxygenase 1 Homo sapiens 27-31 33716792-6 2021 Heme oxygenase-1 (HO-1), a phase II detoxification enzyme responsible for heme catabolism, is induced by oxidative stress, among others. Heme 74-78 heme oxygenase 1 Homo sapiens 18-22 33716792-8 2021 The regulatory role of heme availability for the synthesis of enzymes involved in hypertension development, such as cyclooxygenase or nitric oxide synthase, seems to be responsible for many of the beneficial HO-1 effects; additionally, the antioxidant, anti-inflammatory, antiapoptotic, and antiproliferative effects of the end products of its reaction, carbon monoxide, biliverdin/bilirubin, and Fe2+, would also contribute. Heme 23-27 heme oxygenase 1 Homo sapiens 208-212 33643023-2 2021 Biliverdin is derived from heme through a reaction mediated by HO-1 and protects cells from oxidative stress. Heme 27-31 heme oxygenase 1 Homo sapiens 63-67 33152749-3 2021 Here, we found that cell-free heme suppresses human B cell plasmablast/plasma cell differentiation by inhibiting the DOCK8/STAT3 signaling pathway, which is critical for B cell activation, as well as by upregulating heme oxygenase 1 (HO-1) through its enzymatic byproducts, carbon monoxide and biliverdin. Heme 30-34 heme oxygenase 1 Homo sapiens 216-232 33176981-0 2021 Desaturation and heme elevation during COVID-19 infection: A potential prognostic factor of heme oxygenase-1. Heme 17-21 heme oxygenase 1 Homo sapiens 92-108 33152749-3 2021 Here, we found that cell-free heme suppresses human B cell plasmablast/plasma cell differentiation by inhibiting the DOCK8/STAT3 signaling pathway, which is critical for B cell activation, as well as by upregulating heme oxygenase 1 (HO-1) through its enzymatic byproducts, carbon monoxide and biliverdin. Heme 30-34 heme oxygenase 1 Homo sapiens 234-238 33228202-8 2020 HO-1 degrades the prooxidant heme and generates molecules with antioxidative and anti-inflammatory properties, resulting in decreased oxidative stress and inflammation. Heme 29-33 heme oxygenase 1 Homo sapiens 0-4 33184238-4 2020 Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis. Heme 87-91 heme oxygenase 1 Homo sapiens 0-16 33184238-4 2020 Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis. Heme 87-91 heme oxygenase 1 Homo sapiens 18-22 33184238-4 2020 Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis. Heme 119-123 heme oxygenase 1 Homo sapiens 0-16 33184238-4 2020 Heme oxygenase-1 (HO-1) is a cytoprotective, inducible enzyme that degrades toxic free heme released from destabilized heme proteins and, during this process, releases beneficial by-products such as carbon monoxide and biliverdin/bilirubin and promotes ferritin synthesis. Heme 119-123 heme oxygenase 1 Homo sapiens 18-22 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. Heme 97-101 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. Heme 97-101 heme oxygenase 1 Homo sapiens 18-22 33414780-6 2020 Plasma levels of heme and its scavenger hemopexin and degrading enzyme heme-oxygenase-1 (HO-1) were measured in 48 STEC-HUS patients. Heme 17-21 heme oxygenase 1 Homo sapiens 89-93 33414780-10 2020 Interestingly, especially patients with high heme levels (n = 12, heme levels above 75 quartile range) had high plasma HO-1 levels with median of 332.5 (86-720) ng/ml (p = 0.008). Heme 45-49 heme oxygenase 1 Homo sapiens 119-123 33414780-10 2020 Interestingly, especially patients with high heme levels (n = 12, heme levels above 75 quartile range) had high plasma HO-1 levels with median of 332.5 (86-720) ng/ml (p = 0.008). Heme 66-70 heme oxygenase 1 Homo sapiens 119-123 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. Heme 45-49 heme oxygenase 1 Homo sapiens 31-34 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. Heme 124-128 heme oxygenase 1 Homo sapiens 31-34 33051205-2 2020 Tight regulation of the cellular levels and catalytic activities of HO1 and HO2 is important for maintaining heme homeostasis. Heme 109-113 heme oxygenase 1 Homo sapiens 68-71 33327226-8 2020 The increase in heme in vivo induces HO-1 production, a heme-degrading enzyme. Heme 16-20 heme oxygenase 1 Homo sapiens 37-41 33327226-8 2020 The increase in heme in vivo induces HO-1 production, a heme-degrading enzyme. Heme 56-60 heme oxygenase 1 Homo sapiens 37-41 33157356-7 2020 Furthermore, we found that ferric ion (Fe3+) but not biliverdin and carbon monoxide, products of heme degradation by HO-1, mediated the HO-1-induced anti-DTMUV effect. Heme 97-101 heme oxygenase 1 Homo sapiens 136-140 33260980-1 2020 Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that catalyzes heme group degradation. Heme 74-78 heme oxygenase 1 Homo sapiens 0-16 33260980-1 2020 Heme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that catalyzes heme group degradation. Heme 74-78 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. Heme 98-102 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. Heme 98-102 heme oxygenase 1 Homo sapiens 18-22 33228260-4 2020 HO-1 may function as a pleiotropic modulator of inflammatory signaling, via the removal of heme, and generation of its enzymatic degradation-products. Heme 91-95 heme oxygenase 1 Homo sapiens 0-4 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. Heme 186-190 heme oxygenase 1 Homo sapiens 13-17 33148696-12 2021 In contrast, HO-1-mediated heme metabolism was inhibited at subsaturating POR. Heme 27-31 heme oxygenase 1 Homo sapiens 13-17 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). Heme 47-51 heme oxygenase 1 Homo sapiens 77-93 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). Heme 47-51 heme oxygenase 1 Homo sapiens 95-99 33066778-1 2020 BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin. Heme 65-69 heme oxygenase 1 Homo sapiens 12-28 33066778-1 2020 BACKGROUND: Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin. Heme 65-69 heme oxygenase 1 Homo sapiens 30-35 32860873-3 2020 Endogenously, CO is synthesized upon degradation of heme by heme oxygenases (HOs) of which two enzymatically active isoenzymes are known in mammals; the stress-inducible HO-1 and the constitutively expressed HO-2. Heme 52-56 heme oxygenase 1 Homo sapiens 170-174 32860873-5 2020 In context with ROS, HO-1 expression has been associated with antioxidant defense related to the heme-metabolite redox pair biliverdin/bilirubin. Heme 97-101 heme oxygenase 1 Homo sapiens 21-25 32993497-3 2020 H2S release is triggered by carbon monoxide (CO) from the catabolism of heme by inducible heme oxygenase (HO-1) and heme proteins possess catalytic activity necessary for the H2S signalling by protein persulfidation. Heme 72-76 heme oxygenase 1 Homo sapiens 106-110 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. Heme 116-120 heme oxygenase 1 Homo sapiens 0-16 32971746-1 2020 Heme oxygenase-1 is induced by many cellular stressors and catalyzes the breakdown of heme to generate carbon monoxide and bilirubin, which confer cytoprotection. Heme 86-90 heme oxygenase 1 Homo sapiens 0-16 32971746-8 2020 Our results suggest that regulation of heme may be an equally significant role of HO-1. Heme 39-43 heme oxygenase 1 Homo sapiens 82-86 32558263-4 2020 Two closely related enzymes, heme oxygenase-1 (HMOX1) and heme oxygenase-2 (HMOX2), degrade free heme to produce carbon monoxide, Fe2+ and biliverdin. Heme 29-33 heme oxygenase 1 Homo sapiens 47-52 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. Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 32611235-2 2020 In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes. Heme 31-35 heme oxygenase 1 Homo sapiens 208-224 32611235-2 2020 In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes. Heme 31-35 heme oxygenase 1 Homo sapiens 226-231 32611235-2 2020 In human macrophages in vitro, heme activates an adenosine monophosphate activated protein kinase / activating transcription factor 1 (AMPK/ATF1) pathway that directs Mhem macrophages through coregulation of heme oxygenase 1 (HMOX1, HO-1) and lipid homeostasis genes. Heme 31-35 heme oxygenase 1 Homo sapiens 233-237 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. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 32717801-1 2020 Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO). Heme 17-21 heme oxygenase 1 Homo sapiens 35-39 32880973-1 2021 Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders. Heme 73-77 heme oxygenase 1 Homo sapiens 0-16 32880973-1 2021 Heme oxygenase-1 (HO-1), a highly inducible stress protein that degrades heme to biliverdin, carbon monoxide and free ferrous iron, is increased in blood and other biofluids of subjects with various systemic and neurological disorders. Heme 73-77 heme oxygenase 1 Homo sapiens 18-22 32500379-3 2020 Additionally, COVID-19"s heme reduction may contribute to even lower HO-1. Heme 25-29 heme oxygenase 1 Homo sapiens 69-73 32615411-3 2020 Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant. Heme 34-38 heme oxygenase 1 Homo sapiens 78-94 32615411-3 2020 Carbon monoxide (CO) arising from heme degradation, catalyzed particularly by heme oxygenase-1 (HO-1), has been shown to own cytoprotective effects including anti-inflammation and antioxidant. Heme 34-38 heme oxygenase 1 Homo sapiens 96-100 32982786-5 2020 HO-1 and HO-2 catalyze the rate-limiting step of cellular heme degradation and, similar to SirT1, HO-1 exerts beneficial effects in the vasculature through the activation of anti-oxidant, anti-inflammatory, anti-apoptotic, and anti-proliferative signaling pathways. Heme 58-62 heme oxygenase 1 Homo sapiens 0-4 32828015-6 2020 In addition, the leukocytes from people with HIV with CWP had attenuated levels of the heme metabolizing enzyme, heme oxygenase-1, which metabolizes free heme to carbon-monoxide and biliverdin. Heme 87-91 heme oxygenase 1 Homo sapiens 113-129 32695110-4 2020 Heme is a chemoattractant, activates the complement system, modulates host defense mechanisms through the activation of innate immune receptors and the heme oxygenase-1/ferritin system, and induces innate immune memory. Heme 0-4 heme oxygenase 1 Homo sapiens 152-168 32692767-1 2020 Heme oxygenase (HO-1) mediates the enzymatic cleavage of heme, a molecule with proinflammatory and prooxidant properties. Heme 57-61 heme oxygenase 1 Homo sapiens 16-20 32760278-7 2020 HO-1 is an enzyme that degrades heme groups, leading to the production of potent antioxidant, anti-inflammatory, and bactericidal mediators, such as biliverdin, bilirubin, and CO. Heme 32-36 heme oxygenase 1 Homo sapiens 0-4 32156661-2 2020 As a response, heme induces its metabolic degradation via heme oxygenase-1 (HO-1), activated by NF-E2-related factor 2 (NRF2), the master stress response transcription factor. Heme 15-19 heme oxygenase 1 Homo sapiens 58-74 32369450-3 2020 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme that catabolizes free heme. Heme 74-78 heme oxygenase 1 Homo sapiens 0-16 32369450-3 2020 Heme oxygenase-1 (HO-1) is the rate-limiting enzyme that catabolizes free heme. Heme 74-78 heme oxygenase 1 Homo sapiens 18-22 32006543-1 2020 OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin. Heme 44-48 heme oxygenase 1 Homo sapiens 11-27 32006543-1 2020 OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin. Heme 44-48 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. Heme 52-56 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. Heme 52-56 heme oxygenase 1 Homo sapiens 18-22 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. Heme 83-87 heme oxygenase 1 Homo sapiens 0-16 32035862-2 2020 In living organisms, it is produced endogenously during the degradation of heme by oxygenase, which occurs in three isoforms: HO-1, HO-2 and HO-3. Heme 75-79 heme oxygenase 1 Homo sapiens 126-130 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. Heme 83-87 heme oxygenase 1 Homo sapiens 18-22 33016915-4 2020 Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions. Heme 88-92 heme oxygenase 1 Homo sapiens 0-16 32082323-6 2020 Heme oxygenase-1 (HO-1, encoded by HMOX1) produces BV by heme degradation, while biliverdin reductase-A (BLVR-A) generates BR by the subsequent conversion of BV. Heme 57-61 heme oxygenase 1 Homo sapiens 0-22 32082323-6 2020 Heme oxygenase-1 (HO-1, encoded by HMOX1) produces BV by heme degradation, while biliverdin reductase-A (BLVR-A) generates BR by the subsequent conversion of BV. Heme 57-61 heme oxygenase 1 Homo sapiens 35-40 33016915-4 2020 Heme oxygenase 1 (HO-1) is a 32 kDa enzyme, which catalyzes the degradation of cellular heme to free ferrous iron, biliverdin, and carbon monoxide under stressful conditions. Heme 88-92 heme oxygenase 1 Homo sapiens 18-22 33016915-6 2020 The beneficial roles of HO-1 overexpression in AD brains are widely accepted due to its ability to convert pro-oxidant heme to biliverdin and bilirubin (antioxidants), which promote restoration of a suitable tissue redox microenvironment. Heme 119-123 heme oxygenase 1 Homo sapiens 24-28 31704095-1 2019 Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron. Heme 34-38 heme oxygenase 1 Homo sapiens 0-16 31704097-4 2019 BVR-deficiency induces the activity of Nrf2 transcription factor and increases heme oxygenase-1 (HO-1) level, which is accompanied by the reduction of cellular heme content, increase in a free iron fraction and oxidative stress. Heme 79-83 heme oxygenase 1 Homo sapiens 97-101 31704095-1 2019 Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXalpha, carbon monoxide (CO), and iron. Heme 34-38 heme oxygenase 1 Homo sapiens 18-22 31571584-6 2019 Complete heme tolerance requires a fully-operational heme degradation pathway as haplo insufficiency of HMOX1 combined with SLC48A1 inactivation causes perinatal lethality demonstrating synthetic lethal interactions between heme transport and degradation. Heme 9-13 heme oxygenase 1 Homo sapiens 104-109 31921135-2 2019 Based on studies showing the potential role of heme oxygenase-1 (HO-1), an enzyme that catalyzes the degradation of heme and has anti-inflammatory properties in SLE development, we decided to explore HO-1 in LN. Heme 47-51 heme oxygenase 1 Homo sapiens 65-69 31571584-6 2019 Complete heme tolerance requires a fully-operational heme degradation pathway as haplo insufficiency of HMOX1 combined with SLC48A1 inactivation causes perinatal lethality demonstrating synthetic lethal interactions between heme transport and degradation. Heme 53-57 heme oxygenase 1 Homo sapiens 104-109 31571584-6 2019 Complete heme tolerance requires a fully-operational heme degradation pathway as haplo insufficiency of HMOX1 combined with SLC48A1 inactivation causes perinatal lethality demonstrating synthetic lethal interactions between heme transport and degradation. Heme 53-57 heme oxygenase 1 Homo sapiens 104-109 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. Heme 114-118 heme oxygenase 1 Homo sapiens 9-12 32587840-1 2019 Heme oxygenase-1 (HO-1) is an inducible enzyme involved in the catalysis of heme conversion into biliverdin. Heme 76-80 heme oxygenase 1 Homo sapiens 0-16 32587840-1 2019 Heme oxygenase-1 (HO-1) is an inducible enzyme involved in the catalysis of heme conversion into biliverdin. Heme 76-80 heme oxygenase 1 Homo sapiens 18-22 31396090-3 2019 Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR). Heme 43-47 heme oxygenase 1 Homo sapiens 0-22 31276659-1 2019 Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin. Heme 52-56 heme oxygenase 1 Homo sapiens 0-16 31276659-1 2019 Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin. Heme 52-56 heme oxygenase 1 Homo sapiens 18-22 31276659-1 2019 Heme oxygenase-1 (HO-1, HMOX1) degrades pro-oxidant heme into carbon monoxide (CO), ferrous ions (Fe2+) and biliverdin. Heme 52-56 heme oxygenase 1 Homo sapiens 24-29 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. Heme 83-87 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. Heme 83-87 heme oxygenase 1 Homo sapiens 18-22 31344980-5 2019 In atherosclerosis, HO-1 may play a protective role against the progression of atherosclerosis, mainly due to the degradation of pro-oxidant heme, the generation of anti-oxidants biliverdin and bilirubin and the production of vasodilator CO. Heme 141-145 heme oxygenase 1 Homo sapiens 20-24 31251786-4 2019 In this study we found that HBZ activates expression of Heme Oxygenase 1 (HMOX-1), a component of the oxidative stress response that functions to detoxify free heme. Heme 160-164 heme oxygenase 1 Homo sapiens 56-72 31396016-4 2019 Both conditions can be accompanied by decreased levels of heme oxygenase-1 (HMOX1), cytoprotective, heme-degrading enzyme. Heme 58-62 heme oxygenase 1 Homo sapiens 76-81 31257023-3 2019 Nrf2 accumulation in lung cancers causes the stabilization of Bach1 by inducing Ho1, the enzyme catabolizing heme. Heme 109-113 heme oxygenase 1 Homo sapiens 80-83 31251786-4 2019 In this study we found that HBZ activates expression of Heme Oxygenase 1 (HMOX-1), a component of the oxidative stress response that functions to detoxify free heme. Heme 160-164 heme oxygenase 1 Homo sapiens 74-80 31251786-8 2019 Consistent with this model, we found that HMOX-1 is upregulated in HTLV-1-transformed T-cell lines and confers these cells with resistance to heme-induced cytotoxicity. Heme 142-146 heme oxygenase 1 Homo sapiens 42-48 31261522-1 2019 Heme oxygenase-1 (HO-1) is an important catalytic enzyme in heme degradation, which increases during stressful conditions. Heme 60-64 heme oxygenase 1 Homo sapiens 0-16 31163581-1 2019 (1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects. Heme 49-53 heme oxygenase 1 Homo sapiens 16-32 31163581-1 2019 (1) Background: Heme oxygenase-1 (HO-1) degrades heme and generates carbon monoxide (CO), producing various anti-inflammatory, anti-oxidative, and anti-apoptotic effects. Heme 49-53 heme oxygenase 1 Homo sapiens 34-38 31261522-1 2019 Heme oxygenase-1 (HO-1) is an important catalytic enzyme in heme degradation, which increases during stressful conditions. Heme 60-64 heme oxygenase 1 Homo sapiens 18-22 31288720-4 2019 Recent studies revealed that heme oxygenase 1 (HO-1), an enzyme that participates in heme degradation, plays a critical role in the pathogenesis and may regulate autoimmunity. Heme 29-33 heme oxygenase 1 Homo sapiens 47-51 30944174-6 2019 Here, using hydrogen-deuterium exchange MS, size-exclusion chromatography, and sedimentation velocity, we investigated how these divergent regions impact the dynamics and structure of the apo and heme-bound forms of HO1 and HO2. Heme 196-200 heme oxygenase 1 Homo sapiens 216-219 30944174-7 2019 Our results reveal that heme binding to the catalytic cores of HO1 and HO2 causes similar dynamic and structural changes in regions (proximal, distal, and A6 helices) within and linked to the heme pocket. Heme 24-28 heme oxygenase 1 Homo sapiens 63-66 30944174-7 2019 Our results reveal that heme binding to the catalytic cores of HO1 and HO2 causes similar dynamic and structural changes in regions (proximal, distal, and A6 helices) within and linked to the heme pocket. Heme 192-196 heme oxygenase 1 Homo sapiens 63-66 30898432-3 2019 Patrolling monocytes, which normally scavenge damaged cells and debris from the vasculature, express higher levels of anti-inflammatory heme oxygenase 1 (HO-1), a heme degrading enzyme with anti-cytotoxic and anti-inflammatory properties. Heme 136-140 heme oxygenase 1 Homo sapiens 154-158 30995787-2 2019 HO-1 protects cells against oxidative injury, degrading free heme and inhibiting ROS production. Heme 61-65 heme oxygenase 1 Homo sapiens 0-4 30784878-3 2019 Under these conditions, HO-1 exerts its strong cytoprotective activities and plays a crucial role in stimulating cell survival by removing the pro-oxidant heme and by producing carbon monoxide and biliverdin (promptly reduced to bilirubin). Heme 155-159 heme oxygenase 1 Homo sapiens 24-28 30883732-1 2019 Heme oxygenase-1 (HMOX1) catalyzes heme degradation utilizing reducing equivalents supplied from NADPH-cytochrome P450 reductase (CYPOR). Heme 35-39 heme oxygenase 1 Homo sapiens 0-16 30883732-1 2019 Heme oxygenase-1 (HMOX1) catalyzes heme degradation utilizing reducing equivalents supplied from NADPH-cytochrome P450 reductase (CYPOR). Heme 35-39 heme oxygenase 1 Homo sapiens 18-23 30883732-6 2019 As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP+ binding to enhance the electron-transfer efficiency from FMN to heme. Heme 71-75 heme oxygenase 1 Homo sapiens 82-87 30883732-6 2019 As a result of this change, the FMN-binding domain of CYPOR approaches heme-bound HMOX1 upon NADP+ binding to enhance the electron-transfer efficiency from FMN to heme. Heme 163-167 heme oxygenase 1 Homo sapiens 82-87 30759842-3 2019 Imidazole scaffold is normally present in most of the classical HO-1 inhibitors and seems indispensable to the inhibitory activity due to its strong interaction with the Fe(II) of the heme group. Heme 184-188 heme oxygenase 1 Homo sapiens 64-68 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. Heme 162-166 heme oxygenase 1 Homo sapiens 30-34 30683864-7 2019 Collectively, our data indicate that HO-1, by detoxifying heme, blocks p16INK4a expression in macrophages, preventing DNA damage and cellular senescence. Heme 58-62 heme oxygenase 1 Homo sapiens 37-41 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). Heme 148-152 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). Heme 148-152 heme oxygenase 1 Homo sapiens 30-34 30213580-5 2019 Consequently, biological actions of HO-1 are not limited to degradation of a toxic heme released from hemoproteins, but also provide an adaptive cellular response against chronic inflammation and oxidative injury. Heme 83-87 heme oxygenase 1 Homo sapiens 36-40 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). Heme 37-41 heme oxygenase 1 Homo sapiens 127-143 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). Heme 37-41 heme oxygenase 1 Homo sapiens 145-149 30009872-4 2019 By converting pro-oxidant heme to the antioxidants, biliverdin and bilirubin, HO-1/biliverdin reductase may help restore a more favorable tissue redox microenvironment. Heme 26-30 heme oxygenase 1 Homo sapiens 78-82 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. Heme 45-49 heme oxygenase 1 Homo sapiens 0-21 30583467-5 2018 The critical role of HO-1 in heme metabolism makes it an important candidate to mediate protective or detrimental effects via ferroptosis induction. Heme 29-33 heme oxygenase 1 Homo sapiens 21-25 30619356-0 2018 Heme Drives Susceptibility of Glomerular Endothelium to Complement Overactivation Due to Inefficient Upregulation of Heme Oxygenase-1. Heme 0-4 heme oxygenase 1 Homo sapiens 117-133 30619356-8 2018 Only HUVEC (Human Umbilical Vein EC) developed adaptation to heme, which was lost after inhibition of HO-1 activity. Heme 61-65 heme oxygenase 1 Homo sapiens 102-106 30577437-1 2018 Heme oxygenase-1 (HO-1), a rate-limiting enzyme involved in the degradation of heme, is induced in response to a wide range of stress conditions. Heme 79-83 heme oxygenase 1 Homo sapiens 0-16 30577437-1 2018 Heme oxygenase-1 (HO-1), a rate-limiting enzyme involved in the degradation of heme, is induced in response to a wide range of stress conditions. Heme 79-83 heme oxygenase 1 Homo sapiens 18-22 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. Heme 78-82 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. Heme 78-82 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. Heme 56-60 heme oxygenase 1 Homo sapiens 0-16 30354231-11 2018 Surgery and heme arginate infusion significantly increased HO-1 mRNA concentration in peripheral blood mononuclear cells ( P<0.001). Heme 12-16 heme oxygenase 1 Homo sapiens 59-63 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. Heme 69-73 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. Heme 69-73 heme oxygenase 1 Homo sapiens 18-22 30105448-13 2018 The induction of HO-1 might have be a promising approach for the treatment of psoriasis through antioxidant ability, immunomodulatory role as well as its role in heme synthesis. Heme 162-166 heme oxygenase 1 Homo sapiens 17-21 29530745-1 2018 OBJECTIVE: The aim of this study was to investigate how maternal cell-free fetal hemoglobin and heme impact the scavenger enzyme systems Hemopexin and Heme Oxygenase-1 in patients with preeclampsia (PE). Heme 96-100 heme oxygenase 1 Homo sapiens 151-167 29530745-10 2018 CONCLUSIONS: Increased maternal plasma levels of heme and HbF in PE are associated with decreased HO-1 and hemopexin protein levels as well as reduced hemopexin activity. Heme 49-53 heme oxygenase 1 Homo sapiens 98-102 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. Heme 56-60 heme oxygenase 1 Homo sapiens 18-23 29278009-1 2018 BACKGROUND: Heme oxygenase (HO)-1 is a heme-degrading enzyme highly expressed in monocyte/macrophage, serum levels of which may be promising biomarker for adult-onset Still"s disease (AOSD). Heme 39-43 heme oxygenase 1 Homo sapiens 12-33 30258436-1 2018 Heme Oxygenase 1 (HMOX1) is an enzyme that catalyzes the reaction that degrades the heme group contained in several important proteins, such as hemoglobin, myoglobin, and cytochrome p450. Heme 84-88 heme oxygenase 1 Homo sapiens 0-16 30258436-1 2018 Heme Oxygenase 1 (HMOX1) is an enzyme that catalyzes the reaction that degrades the heme group contained in several important proteins, such as hemoglobin, myoglobin, and cytochrome p450. Heme 84-88 heme oxygenase 1 Homo sapiens 18-23 29761622-4 2018 HMOX1 is a cytoprotective enzyme that degrades heme to generate carbon monoxide (CO), biliverdin, and molecular iron. Heme 47-51 heme oxygenase 1 Homo sapiens 0-5 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. Heme 96-100 heme oxygenase 1 Homo sapiens 0-16 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. Heme 40-44 heme oxygenase 1 Homo sapiens 58-62 30354985-1 2018 Background and Purpose- Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to generate carbon monoxide, biliverdin, and iron. Heme 75-79 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. Heme 75-79 heme oxygenase 1 Homo sapiens 42-46 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. Heme 89-93 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. Heme 89-93 heme oxygenase 1 Homo sapiens 24-28 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. Heme 69-73 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. Heme 69-73 heme oxygenase 1 Homo sapiens 18-22 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. Heme 52-56 heme oxygenase 1 Homo sapiens 0-21 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. Heme 96-100 heme oxygenase 1 Homo sapiens 18-22 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. Heme 128-132 heme oxygenase 1 Homo sapiens 218-222 29525432-1 2018 Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin. Heme 63-67 heme oxygenase 1 Homo sapiens 0-16 29461260-5 2018 Heme may increase host susceptibility to infections by inducing heme oxygenase 1 (HO-1) in immature neutrophils, thereby inhibiting oxidative burst required for clearance of engulfed bacteria. Heme 0-4 heme oxygenase 1 Homo sapiens 64-80 29461260-5 2018 Heme may increase host susceptibility to infections by inducing heme oxygenase 1 (HO-1) in immature neutrophils, thereby inhibiting oxidative burst required for clearance of engulfed bacteria. Heme 0-4 heme oxygenase 1 Homo sapiens 82-86 29525432-1 2018 Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to produce three anti-oxidant molecules: carbon monoxide (CO), ferrous ion (Fe2+), and biliverdin. Heme 63-67 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). Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 29437594-2 2018 Patrolling monocytes, which normally scavenge damaged cells and debris from the vasculature, express higher levels of anti-inflammatory heme oxygenase 1 (HO-1), a heme degrading enzyme. Heme 136-140 heme oxygenase 1 Homo sapiens 154-158 29437594-4 2018 We found that a mean 37% of patrolling monocytes from SCD patients express very high levels of HO-1 (HO-1hi) vs 6% in healthy controls and demonstrated that HO-1hi expression was dependent on uptake of heme-exposed endothelium. Heme 202-206 heme oxygenase 1 Homo sapiens 95-99 29437594-4 2018 We found that a mean 37% of patrolling monocytes from SCD patients express very high levels of HO-1 (HO-1hi) vs 6% in healthy controls and demonstrated that HO-1hi expression was dependent on uptake of heme-exposed endothelium. Heme 202-206 heme oxygenase 1 Homo sapiens 101-107 29437594-4 2018 We found that a mean 37% of patrolling monocytes from SCD patients express very high levels of HO-1 (HO-1hi) vs 6% in healthy controls and demonstrated that HO-1hi expression was dependent on uptake of heme-exposed endothelium. Heme 202-206 heme oxygenase 1 Homo sapiens 157-163 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. Heme 101-105 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. Heme 101-105 heme oxygenase 1 Homo sapiens 18-22 28756878-2 2017 By means of these catabolic end-products and by removal of pro-oxidant heme, HO-1 exerts antioxidant, antiapoptotic, and immune-modulating effects, leading to overall cytoprotective and beneficial functions in mammalian cells. Heme 71-75 heme oxygenase 1 Homo sapiens 77-81 28276576-2 2017 Our group reported decreased risk for ET in carriers of the minor alleles of the rs2071746 and rs1051308 SNPs in the haem-oxygenases 1 and 2 (HMOX1 and HMOX2), respectively, involved in haem metabolism. Heme 117-121 heme oxygenase 1 Homo sapiens 142-147 29122256-7 2017 Macrophages phagocytize the erythrocytes in the extravascular space which stimulates the production of Heme Oxygenase-1 (HO-1) to metabolize the heme. Heme 145-149 heme oxygenase 1 Homo sapiens 103-119 29122256-7 2017 Macrophages phagocytize the erythrocytes in the extravascular space which stimulates the production of Heme Oxygenase-1 (HO-1) to metabolize the heme. Heme 145-149 heme oxygenase 1 Homo sapiens 121-125 29163402-3 2017 Once induced, HO-1 degrades iron-containing heme into ferrous iron (Fe2+), carbon monoxide (CO) and biliverdin. Heme 44-48 heme oxygenase 1 Homo sapiens 14-18 28655775-8 2017 In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Heme 3-7 heme oxygenase 1 Homo sapiens 36-39 28655775-8 2017 In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Heme 3-7 heme oxygenase 1 Homo sapiens 80-83 28655775-8 2017 In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Heme 22-26 heme oxygenase 1 Homo sapiens 36-39 28655775-8 2017 In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction. Heme 22-26 heme oxygenase 1 Homo sapiens 80-83 28655775-9 2017 Furthermore, in vitro reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1. Heme 142-146 heme oxygenase 1 Homo sapiens 99-102 28978042-1 2017 Heme oxygenase-1 (HO-1) degrades heme to bilirubin. Heme 33-37 heme oxygenase 1 Homo sapiens 0-16 28978042-1 2017 Heme oxygenase-1 (HO-1) degrades heme to bilirubin. Heme 33-37 heme oxygenase 1 Homo sapiens 18-22 28978042-7 2017 Since translocation of HO-1 disrupts the association with cytochrome P450 reductase, heme degrading activity was higher for ER anchored versus anchorless HO-1. Heme 85-89 heme oxygenase 1 Homo sapiens 23-27 28978042-7 2017 Since translocation of HO-1 disrupts the association with cytochrome P450 reductase, heme degrading activity was higher for ER anchored versus anchorless HO-1. Heme 85-89 heme oxygenase 1 Homo sapiens 154-158 28978042-11 2017 In contrast, an increase in ER anchored HO-1 with high heme degrading activity does not contribute to imatinib resistance. Heme 55-59 heme oxygenase 1 Homo sapiens 40-44 29070980-3 2017 The haptoglobin-CD163-heme oxygenase-1 (HO-1) pathway circumvents heme toxicity through enzymatic degradation of heme and transcription of antioxidant genes. Heme 22-26 heme oxygenase 1 Homo sapiens 40-44 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. Heme 59-63 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. Heme 59-63 heme oxygenase 1 Homo sapiens 111-114 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. Heme 61-65 heme oxygenase 1 Homo sapiens 0-16 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. Heme 61-65 heme oxygenase 1 Homo sapiens 18-22 28955775-4 2017 The enhanced heme synthesis in Caco-2 cells was more pronounced under the effect of the combination of ALA and SFC than under the effect of ALA alone, as reflected by the induced expression of heme oxygenase 1 (HO-1), as well as a reduced protein level of the transcriptional corepressor Bach1. Heme 13-17 heme oxygenase 1 Homo sapiens 193-209 28955775-4 2017 The enhanced heme synthesis in Caco-2 cells was more pronounced under the effect of the combination of ALA and SFC than under the effect of ALA alone, as reflected by the induced expression of heme oxygenase 1 (HO-1), as well as a reduced protein level of the transcriptional corepressor Bach1. Heme 13-17 heme oxygenase 1 Homo sapiens 211-215 28347842-0 2017 Potential role of heme metabolism in the inducible expression of heme oxygenase-1. Heme 18-22 heme oxygenase 1 Homo sapiens 65-81 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. Heme 11-15 heme oxygenase 1 Homo sapiens 29-33 28347842-3 2017 We examined the involvement of heme metabolism in the induction of HO-1 by the inducers sulforaphane and sodium arsenite. Heme 31-35 heme oxygenase 1 Homo sapiens 67-71 28347842-5 2017 RESULTS: The blockade of heme biosynthesis by succinylacetone and N-methyl protoporphyrin, which are inhibitors of heme biosynthesis, markedly decreased the induction of HO-1. Heme 25-29 heme oxygenase 1 Homo sapiens 170-174 28347842-5 2017 RESULTS: The blockade of heme biosynthesis by succinylacetone and N-methyl protoporphyrin, which are inhibitors of heme biosynthesis, markedly decreased the induction of HO-1. Heme 115-119 heme oxygenase 1 Homo sapiens 170-174 28347842-7 2017 The cessation of HO-1 induction occurred at the transcriptional and translational levels, and was mediated by the activation of the heme-binding transcriptional repressor Bach1 and translational factor HRI. Heme 132-136 heme oxygenase 1 Homo sapiens 17-21 28347842-9 2017 CONCLUSIONS: We demonstrated the importance of heme metabolism in the stress-inducible expression of HO-1, and also that heme and its degradation products are protective factors for self-defense responses. Heme 47-51 heme oxygenase 1 Homo sapiens 101-105 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. Heme 38-42 heme oxygenase 1 Homo sapiens 92-96 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. Heme 128-132 heme oxygenase 1 Homo sapiens 92-96 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. Heme 59-63 heme oxygenase 1 Homo sapiens 0-4 28420988-8 2017 Second, heme oxygenases (HOs), in particular the inducible HO isozyme, HO-1, can provide antioxidant cytoprotection via enzymatic degradation of intracellular heme. Heme 8-12 heme oxygenase 1 Homo sapiens 71-75 28186648-1 2017 Heme oxygenase-1 (HO-1) catalyses the degradation of heme to biliverdin, free iron, and carbon monoxide. Heme 53-57 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. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 28412905-3 2017 The enzyme HO-1 catalyzes the degradation of heme into three biologically active end products, namely biliverdin/bilirubin, CO and ferrous ion. Heme 45-49 heme oxygenase 1 Homo sapiens 11-15 28480030-1 2017 Carbon monoxide (CO) formed endogenously is considered to be cytoprotective, and the vast majority of CO formation is attributed to the degradation of heme by heme oxygenases-1 and -2 (HO-1, HO-2). Heme 151-155 heme oxygenase 1 Homo sapiens 159-183 28480030-1 2017 Carbon monoxide (CO) formed endogenously is considered to be cytoprotective, and the vast majority of CO formation is attributed to the degradation of heme by heme oxygenases-1 and -2 (HO-1, HO-2). Heme 151-155 heme oxygenase 1 Homo sapiens 185-189 28055290-6 2017 In addition, we have demonstrated that heme degradation by HMOX1/HO-1 (heme oxygenase 1) is required and that Fe is essential for the formation of ALIS, as heme analogs lacking the central atom of Fe are not able to induce these structures. Heme 39-43 heme oxygenase 1 Homo sapiens 59-64 28055290-6 2017 In addition, we have demonstrated that heme degradation by HMOX1/HO-1 (heme oxygenase 1) is required and that Fe is essential for the formation of ALIS, as heme analogs lacking the central atom of Fe are not able to induce these structures. Heme 39-43 heme oxygenase 1 Homo sapiens 65-87 28055290-6 2017 In addition, we have demonstrated that heme degradation by HMOX1/HO-1 (heme oxygenase 1) is required and that Fe is essential for the formation of ALIS, as heme analogs lacking the central atom of Fe are not able to induce these structures. Heme 71-75 heme oxygenase 1 Homo sapiens 59-64 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. Heme 32-36 heme oxygenase 1 Homo sapiens 16-20 27397680-7 2016 Alternatively, GGT5 overexpression induces heme oxygenase 1 (HO-1) expression, which, as a key catalyst responsible for the oxidative degradation of heme, may inhibit the activities of the cytochrome P450 monooxygenases, thus substantially impairing testicular steroidogenesis. Heme 43-47 heme oxygenase 1 Homo sapiens 61-65 27997582-2 2016 The cytoprotective enzyme heme oxygenase-1 (HO-1) is a rate-limiting enzyme in heme degradation and it has been shown to exert anti-inflammatory functions. Heme 26-30 heme oxygenase 1 Homo sapiens 44-48 27257045-1 2016 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme, which may be involved in the pathogenesis of AKI. Heme 53-57 heme oxygenase 1 Homo sapiens 0-16 27257045-1 2016 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme, which may be involved in the pathogenesis of AKI. Heme 53-57 heme oxygenase 1 Homo sapiens 18-22 27795400-1 2016 Heme oxygenase-1 (HO-1) is a stress response antioxidant enzyme which catalyzes the degradation of heme released during inflammation. Heme 99-103 heme oxygenase 1 Homo sapiens 18-22 27795400-13 2016 Here, we describe a potential strategy for treating TB based on pharmacological inhibition of the host heme-degrading enzyme HO-1. Heme 103-107 heme oxygenase 1 Homo sapiens 125-129 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. Heme 96-100 heme oxygenase 1 Homo sapiens 46-51 27642551-0 2016 Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase-1. Heme 13-17 heme oxygenase 1 Homo sapiens 96-112 27490825-6 2016 X-ray crystallographic structures of human HO1 H25R with bound heme and additional functional studies suggest that HO mutant activity inside these cells does not involve heme ligation by a proximal amino acid. Heme 63-67 heme oxygenase 1 Homo sapiens 43-46 26483091-1 2016 BACKGROUND: Heme-oxygenase 1 (HO-1), an inducible heme-degrading enzyme, has antiatherogenic effects through its enzymatic end products. Heme 50-54 heme oxygenase 1 Homo sapiens 12-28 27244263-4 2016 Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin. Heme 84-88 heme oxygenase 1 Homo sapiens 106-122 27244263-4 2016 Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin. Heme 84-88 heme oxygenase 1 Homo sapiens 124-128 27244263-4 2016 Our study was based on previous findings that demonstrated that Br2 upregulates the heme-degrading enzyme heme oxygenase-1 (HO-1), which converts toxic heme into bilverdin. Heme 106-110 heme oxygenase 1 Homo sapiens 124-128 27244263-7 2016 However, therapeutic reduction of heme levels, by either scavenging with hemopexin or degradation by HO-1, improved lung function and survival. Heme 34-38 heme oxygenase 1 Homo sapiens 101-105 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. Heme 170-174 heme oxygenase 1 Homo sapiens 188-192 26595750-1 2016 Heme oxygenase (HO)-1 catalyzes the degradation of cytotoxic heme into biliverdin and blocks antitumor immune responses, thus protecting cancer against host defense. Heme 61-65 heme oxygenase 1 Homo sapiens 0-21 26483091-1 2016 BACKGROUND: Heme-oxygenase 1 (HO-1), an inducible heme-degrading enzyme, has antiatherogenic effects through its enzymatic end products. Heme 50-54 heme oxygenase 1 Homo sapiens 30-34 27412411-1 2016 Heme oxygenase 1 (HO-1) is an inducible stress-response enzyme that not only catalyzes the degradation of heme (e.g., released from erythrocytes) but also has an important function in various physiological and pathophysiological states associated with cellular stress, such as ischemic/reperfusion injury. Heme 106-110 heme oxygenase 1 Homo sapiens 0-16 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+)). Heme 79-83 heme oxygenase 1 Homo sapiens 18-22 26652036-0 2016 Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction Studies. Heme 32-36 heme oxygenase 1 Homo sapiens 54-78 26652036-1 2016 The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Heme 26-30 heme oxygenase 1 Homo sapiens 42-45 27412411-1 2016 Heme oxygenase 1 (HO-1) is an inducible stress-response enzyme that not only catalyzes the degradation of heme (e.g., released from erythrocytes) but also has an important function in various physiological and pathophysiological states associated with cellular stress, such as ischemic/reperfusion injury. Heme 106-110 heme oxygenase 1 Homo sapiens 18-22 26680374-1 2016 BACKGROUND: The enzyme heme oxygenase-1 (HO-1) degrades heme and protects against ischemia-reperfusion injury. Heme 23-27 heme oxygenase 1 Homo sapiens 41-45 26315932-2 2015 We have previously shown that the liberation of heme in acute hemolysis can induce heme oxygenase-1 during granulopoiesis, impairing the ability of developing neutrophils to mount a bactericidal oxidative burst, and increasing susceptibility to bacterial infection. Heme 48-52 heme oxygenase 1 Homo sapiens 83-99 26507166-4 2015 Heme oxygenase-1 (HO-1) is an enzyme that catalyzes oxidation of heme to biliverdin, and has anti-inflammatory and anti-oxidant properties. Heme 65-69 heme oxygenase 1 Homo sapiens 0-16 26507166-4 2015 Heme oxygenase-1 (HO-1) is an enzyme that catalyzes oxidation of heme to biliverdin, and has anti-inflammatory and anti-oxidant properties. Heme 65-69 heme oxygenase 1 Homo sapiens 18-22 26884897-8 2015 HO-1 and its reaction products of heme degradation has been linked to cytoprotection, and as an inducible form of HO, serves a vital metabolic function as the rate-limiting step in the heme degradation pathway, and affords protection in models of liver I/R injury. Heme 34-38 heme oxygenase 1 Homo sapiens 0-4 26884897-8 2015 HO-1 and its reaction products of heme degradation has been linked to cytoprotection, and as an inducible form of HO, serves a vital metabolic function as the rate-limiting step in the heme degradation pathway, and affords protection in models of liver I/R injury. Heme 185-189 heme oxygenase 1 Homo sapiens 0-4 26392237-1 2015 Heme oxygenase-1 (HO-1, hmox-1) catalyzes the rate-limiting step in the heme degradation processes. Heme 72-76 heme oxygenase 1 Homo sapiens 0-22 26392237-1 2015 Heme oxygenase-1 (HO-1, hmox-1) catalyzes the rate-limiting step in the heme degradation processes. Heme 72-76 heme oxygenase 1 Homo sapiens 24-30 26270345-1 2015 Earlier observations indicate that free heme is selectively toxic to cells lacking heme oxygenase-1 (HO-1) but how this enzyme prevents heme toxicity remains unexplained. Heme 40-44 heme oxygenase 1 Homo sapiens 83-99 26510767-2 2015 Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation. Heme 112-116 heme oxygenase 1 Homo sapiens 0-16 26510767-2 2015 Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation. Heme 112-116 heme oxygenase 1 Homo sapiens 18-22 26493719-3 2015 Heme oxygenase-1 (HO-1; also known as Hsp32) is an inducible enzyme participating in heme degradation and involved in oxidative stress resistance. Heme 85-89 heme oxygenase 1 Homo sapiens 0-16 26493719-3 2015 Heme oxygenase-1 (HO-1; also known as Hsp32) is an inducible enzyme participating in heme degradation and involved in oxidative stress resistance. Heme 85-89 heme oxygenase 1 Homo sapiens 18-22 26493719-3 2015 Heme oxygenase-1 (HO-1; also known as Hsp32) is an inducible enzyme participating in heme degradation and involved in oxidative stress resistance. Heme 85-89 heme oxygenase 1 Homo sapiens 38-43 26339767-5 2015 RECENT FINDINGS: Recent studies demonstrate that Hx-dependent uptake of extracellular heme leads to the deactivation of Bach1 repression leading to the transcriptional activation of antioxidant heme oxygenase-1 gene. Heme 86-90 heme oxygenase 1 Homo sapiens 194-210 26270345-1 2015 Earlier observations indicate that free heme is selectively toxic to cells lacking heme oxygenase-1 (HO-1) but how this enzyme prevents heme toxicity remains unexplained. Heme 40-44 heme oxygenase 1 Homo sapiens 101-105 26270345-2 2015 Here, using A549 (human lung cancer) and immortalized human bronchial epithelial cells incubated with exogenous heme, we find knock-down of HO-1 using siRNA does promote the accumulation of cell-associated heme and heme-induced cell death. Heme 112-116 heme oxygenase 1 Homo sapiens 140-144 26270345-2 2015 Here, using A549 (human lung cancer) and immortalized human bronchial epithelial cells incubated with exogenous heme, we find knock-down of HO-1 using siRNA does promote the accumulation of cell-associated heme and heme-induced cell death. Heme 206-210 heme oxygenase 1 Homo sapiens 140-144 26270345-2 2015 Here, using A549 (human lung cancer) and immortalized human bronchial epithelial cells incubated with exogenous heme, we find knock-down of HO-1 using siRNA does promote the accumulation of cell-associated heme and heme-induced cell death. Heme 206-210 heme oxygenase 1 Homo sapiens 140-144 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). Heme 46-50 heme oxygenase 1 Homo sapiens 173-177 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). Heme 134-138 heme oxygenase 1 Homo sapiens 173-177 26270345-5 2015 Supporting the importance of endogenous oxidant production, both chemical and siRNA inhibition of catalase activity predisposes HO-1 deficient cells to heme-mediated killing. Heme 152-156 heme oxygenase 1 Homo sapiens 128-132 26270345-6 2015 Importantly, it appears that HO-1 deficiency somehow blocks the induction of ferritin; control cells exposed to heme show ~10-fold increases in ferritin heavy chain expression whereas in heme-exposed HO-1 deficient cells ferritin expression is unchanged. Heme 112-116 heme oxygenase 1 Homo sapiens 29-33 26270345-6 2015 Importantly, it appears that HO-1 deficiency somehow blocks the induction of ferritin; control cells exposed to heme show ~10-fold increases in ferritin heavy chain expression whereas in heme-exposed HO-1 deficient cells ferritin expression is unchanged. Heme 187-191 heme oxygenase 1 Homo sapiens 29-33 26270345-7 2015 Finally, overexpression of ferritin H chain in HO-1 deficient cells completely prevents heme-induced cytotoxicity. Heme 88-92 heme oxygenase 1 Homo sapiens 47-51 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. Heme 35-39 heme oxygenase 1 Homo sapiens 0-16 26208625-7 2015 Inhibitors interact with the heme cofactor and a hydrophobic pocket (Met34, Phe37, Val50, Leu147 and Phe214) in the HO-1 binding site. Heme 29-33 heme oxygenase 1 Homo sapiens 116-120 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. Heme 35-39 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. Heme 35-39 heme oxygenase 1 Homo sapiens 76-80 26011640-8 2015 Collectively, we found that microglial HO-1 and the generation of CO are essential for effective elimination of blood and heme after SAH that otherwise leads to neuronal injury and cognitive dysfunction. Heme 122-126 heme oxygenase 1 Homo sapiens 39-43 26045540-3 2015 HO-1 converts the pro-oxidant, proinflammatory heme molecule into metabolites with antioxidant, anti-inflammatory, and proliferative activities. Heme 47-51 heme oxygenase 1 Homo sapiens 0-4 26045540-4 2015 Previously published work has shown that KSHV-infected EC in vitro proliferate in response to free heme in a HO-1-dependent manner, thus implicating virus-enhanced HO-1 activity in KS tumorigenesis. Heme 99-103 heme oxygenase 1 Homo sapiens 109-113 26045540-4 2015 Previously published work has shown that KSHV-infected EC in vitro proliferate in response to free heme in a HO-1-dependent manner, thus implicating virus-enhanced HO-1 activity in KS tumorigenesis. Heme 99-103 heme oxygenase 1 Homo sapiens 164-168 26045540-12 2015 The detoxifying action of HO-1 is critical for the protection of cells exposed to high heme levels. Heme 87-91 heme oxygenase 1 Homo sapiens 26-30 26045540-15 2015 Our previous work showed that KSHV-infected cells proliferate in response to heme and that this occurs in a HO-1-dependent manner. Heme 77-81 heme oxygenase 1 Homo sapiens 108-112 26045540-16 2015 We therefore hypothesize that KSHV induction of HO-1 contributes to KS tumor development via heme metabolism and propose that HO-1 be evaluated as a therapeutic target for KS. Heme 93-97 heme oxygenase 1 Homo sapiens 48-52 25751573-1 2015 BACKGROUND: Heme oxygenase 1 (HO1) catalyzes heme degradation, and offers protection for several organs, including the kidney. Heme 45-49 heme oxygenase 1 Homo sapiens 12-28 25751573-1 2015 BACKGROUND: Heme oxygenase 1 (HO1) catalyzes heme degradation, and offers protection for several organs, including the kidney. Heme 45-49 heme oxygenase 1 Homo sapiens 30-33 25652453-3 2015 In this study, we investigated whether the heme precursor 5-aminolevulinic acid (5-ALA) with sodium ferrous citrate (SFC) could protect cardiomyocytes from H2O2-induced hypertrophy via modulation of HO-1 expression. Heme 43-47 heme oxygenase 1 Homo sapiens 199-203 25956277-1 2015 HO-1 gene encodes heme oxygenase-1 enzyme that catalyzes the oxidation of heme to carbon monoxide (CO). Heme 18-22 heme oxygenase 1 Homo sapiens 0-4 24931165-1 2015 Heme oxygenase-1 (HO-1) is a heme-degrading enzyme anchored in the endoplasmic reticulum by a carboxyl-terminal transmembrane segment (TMS). Heme 29-33 heme oxygenase 1 Homo sapiens 0-16 24931165-1 2015 Heme oxygenase-1 (HO-1) is a heme-degrading enzyme anchored in the endoplasmic reticulum by a carboxyl-terminal transmembrane segment (TMS). Heme 29-33 heme oxygenase 1 Homo sapiens 18-22 25849895-2 2015 Mammals contain two isoforms of this enzyme, HO2 and HO1, which share the same alpha-helical fold forming the catalytic core and heme binding site, as well as a membrane spanning helix at their C-termini. Heme 129-133 heme oxygenase 1 Homo sapiens 53-56 25595329-3 2015 It has been recently suggested that the heme-catabolizing enzyme heme oxygenase-1 is an essential component of the mesenchymal stromal cell-driven immune suppressive response. Heme 40-44 heme oxygenase 1 Homo sapiens 65-81 25595329-4 2015 Because mesenchymal stromal cells upregulate indoleamine 2,3-dioxygenase expression on interferon-gamma priming and indoleamine 2,3-dioxygenase requires heme as a cofactor for optimal catabolic function, we investigated the potential antagonism of heme oxygenase-1 activity on indoleamine 2, 3-dioxygenase and the impact on mesenchymal stromal cell immune plasticity. Heme 153-157 heme oxygenase 1 Homo sapiens 248-264 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. Heme 95-99 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. Heme 95-99 heme oxygenase 1 Homo sapiens 18-22 25885228-2 2015 In addition to its primary role in heme catabolism, HO-1 exhibits anti-oxidative and anti-inflammatory functions via the actions of biliverdin and CO, respectively. Heme 35-39 heme oxygenase 1 Homo sapiens 52-56 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. Heme 77-81 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. Heme 77-81 heme oxygenase 1 Homo sapiens 18-22 26303493-3 2015 HO-1 degrades heme to generate carbon monoxide (CO) along with Fe(2+) and biliverdin. Heme 14-18 heme oxygenase 1 Homo sapiens 0-4 25610397-1 2014 The heme-degrading enzyme heme oxygenase-1 (HO-1) has cytoprotective, antioxidant, and anti-inflammatory properties. Heme 4-8 heme oxygenase 1 Homo sapiens 26-42 25610397-1 2014 The heme-degrading enzyme heme oxygenase-1 (HO-1) has cytoprotective, antioxidant, and anti-inflammatory properties. Heme 4-8 heme oxygenase 1 Homo sapiens 44-48 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. Heme 83-87 heme oxygenase 1 Homo sapiens 63-68 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. Heme 191-195 heme oxygenase 1 Homo sapiens 63-68 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. Heme 80-84 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. Heme 55-59 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. Heme 55-59 heme oxygenase 1 Homo sapiens 18-22 25744452-3 2015 HO-1 is induced by its substrate heme and environmental factors including oxidative and heat stresses. Heme 33-37 heme oxygenase 1 Homo sapiens 0-4 25463280-1 2015 Heme oxygenase (HO)-1 is the inducible isoform of the heme-degrading enzyme HO, which is upregulated by multiple stress stimuli. Heme 54-58 heme oxygenase 1 Homo sapiens 0-21 26689007-1 2015 Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin. Heme 47-51 heme oxygenase 1 Homo sapiens 0-16 26689007-1 2015 Heme oxygenase-1 (HO-1) is an enzyme degrading heme to three products - ferrous ions, carbon monoxide and biliverdin. Heme 47-51 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. Heme 80-84 heme oxygenase 1 Homo sapiens 18-22 24382006-3 2014 This may be, in part, explained by the high lung content of heme oxygenase-1 (HO-1), the rate-limiting enzyme in the degradation of heme and an important stress protein. Heme 60-64 heme oxygenase 1 Homo sapiens 78-82 25501830-1 2014 Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO). Heme 94-98 heme oxygenase 1 Homo sapiens 0-16 25501830-1 2014 Heme oxygenase-1 (HO-1), an inducible enzyme up-regulated in Alzheimer"s disease, catabolises heme to biliverdin, Fe2+ and carbon monoxide (CO). Heme 94-98 heme oxygenase 1 Homo sapiens 18-22 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). Heme 64-68 heme oxygenase 1 Homo sapiens 109-125 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). Heme 64-68 heme oxygenase 1 Homo sapiens 127-132 25091622-5 2014 As a critical mechanism, we showed that TUS activated heme oxygenase-1 (HO-1), which degrades heme to immunosuppressive products, such as carbon monoxide and bilirubin. Heme 54-58 heme oxygenase 1 Homo sapiens 72-76 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. Heme 94-98 heme oxygenase 1 Homo sapiens 114-130 25213834-4 2014 Knockdown of Nrf2 by siRNA (siNrf2) targeting caused additional refractoriness of HO-1 protein induction to a second UVA or heme treatment and this treatment also further enhanced cell damage by a second dose of UVA radiation. Heme 124-128 heme oxygenase 1 Homo sapiens 82-86 25086213-2 2014 Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation. Heme 112-116 heme oxygenase 1 Homo sapiens 0-16 25086213-2 2014 Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation. Heme 112-116 heme oxygenase 1 Homo sapiens 18-22 24568186-10 2014 Iron released from heme by HO-1 activity is mostly in the Fe(2+) form. Heme 19-23 heme oxygenase 1 Homo sapiens 27-31 24954650-7 2014 HO-1 metabolizes heme to biliverdin, iron and carbon monoxide (CO). Heme 17-21 heme oxygenase 1 Homo sapiens 0-4 24613679-2 2014 Heme also induces the expression of genes such as heme oxygenase-1 (HO-1) by inactivating the transcription repressor Bach1 through direct binding. Heme 0-4 heme oxygenase 1 Homo sapiens 50-66 25072782-3 2014 CO is a byproduct of heme degradation mediated by heme oxygenase (HO-1). Heme 21-25 heme oxygenase 1 Homo sapiens 66-70 25019514-7 2014 Bach1 has an endogenous ligand, heme, that inhibits Bach1 binding to ARE, thus allowing Nrf2-mediated gene expression including that of heme-oxygenase-1 (HMOX1), a well described target of Bach1 repression. Heme 32-36 heme oxygenase 1 Homo sapiens 136-152 25019514-7 2014 Bach1 has an endogenous ligand, heme, that inhibits Bach1 binding to ARE, thus allowing Nrf2-mediated gene expression including that of heme-oxygenase-1 (HMOX1), a well described target of Bach1 repression. Heme 32-36 heme oxygenase 1 Homo sapiens 154-159 24613679-8 2014 RESULTS: rHx-bound heme induced the expression of HO-1 and decreased the level of Bach1 protein. Heme 19-23 heme oxygenase 1 Homo sapiens 50-54 24613679-9 2014 CPZ inhibited the induction of the HO-1 expression by rHx-bound heme. Heme 64-68 heme oxygenase 1 Homo sapiens 35-39 24613679-10 2014 CONCLUSION: rHx-bound heme was internalized into the cells via endocytosis, resulting in HO-1 expression and inactivation of Bach1. Heme 22-26 heme oxygenase 1 Homo sapiens 89-93 24613679-11 2014 GENERAL SIGNIFICANCE: The Bach1-dependent repression of the HO-1 expression is under the control of the Hx-dependent uptake of extracellular heme. Heme 141-145 heme oxygenase 1 Homo sapiens 60-64 24963040-3 2014 Here, we report that subablative bone marrow transplantation (BMT) has a curative effect for disease in Hmox1(-/-) animals as a result of restoration of heme recycling by repopulation of the tissues with wild-type macrophages. Heme 153-157 heme oxygenase 1 Homo sapiens 104-109 24963040-6 2014 These cells, identified as Kupffer cells with high levels of Hmox1 expression, persisted months after transient engraftment of the donor bone marrow and were responsible for the full restoration of heme-recycling ability in Hmox1(-/-) mice and reversing Hmox1-deficient phenotype. Heme 198-202 heme oxygenase 1 Homo sapiens 224-229 24981859-3 2014 NO suppresses the pathogenesis of ECM via a mechanism involving (1) the transcription factor nuclear factor erythroid 2-related factor 2 (NRF-2), (2) induction of heme oxygenase-1 (HO-1), and (3) CO production via heme catabolism by HO-1. Heme 163-167 heme oxygenase 1 Homo sapiens 181-185 24613679-2 2014 Heme also induces the expression of genes such as heme oxygenase-1 (HO-1) by inactivating the transcription repressor Bach1 through direct binding. Heme 0-4 heme oxygenase 1 Homo sapiens 68-72 24613679-3 2014 However, the source of heme for the regulation of the Bach1-HO-1 axis has been unclear. Heme 23-27 heme oxygenase 1 Homo sapiens 60-64 24977002-1 2014 BACKGROUND: There is a reverse relationship between serum bilirubin level and incidence of stroke, heme oxygenase-1 (HO-1) can catalyze heme into bilirubin, it is unknown the association of HO-1 level with risk of stroke. Heme 99-103 heme oxygenase 1 Homo sapiens 117-121 24879794-6 2014 Exogenous hemin induced Treg polarization in purified T cell/monocyte cocultures from healthy volunteers through the monocyte anti-inflammatory heme-degrading enzyme heme oxygenase-1. Heme 144-148 heme oxygenase 1 Homo sapiens 166-182 24958774-4 2014 In a stable isotope labeling by amino acids in cell culture-based proteomics screen, we identified HO-1 (heme oxygenase-1), the rate-limiting enzyme in the degradation of heme to biliverdin, as a novel SPP substrate. Heme 105-109 heme oxygenase 1 Homo sapiens 99-103 24180257-7 2014 Further, heme is an important component of a number of metabolic enzymes, and, therefore, HO-1 plays an important role in the modulation of cellular bioenergetics. Heme 9-13 heme oxygenase 1 Homo sapiens 90-94 24053682-1 2014 SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism. Heme 47-51 heme oxygenase 1 Homo sapiens 14-30 24053682-1 2014 SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism. Heme 47-51 heme oxygenase 1 Homo sapiens 32-36 24053682-1 2014 SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism. Heme 144-148 heme oxygenase 1 Homo sapiens 14-30 24053682-1 2014 SIGNIFICANCE: Heme oxygenase-1 (HO-1) converts heme to biliverdin, carbon monoxide, and ferrous ions, but its cellular functions are far beyond heme metabolism. Heme 144-148 heme oxygenase 1 Homo sapiens 32-36 24053682-2 2014 HO-1 via heme removal and degradation products acts as a cytoprotective, anti-inflammatory, immunomodulatory, and proangiogenic protein, regulating also a cell cycle. Heme 9-13 heme oxygenase 1 Homo sapiens 0-4 24124891-5 2014 While heme catabolism by heme oxygenase-1 (HO-1) prevents programmed cell death, this cytoprotective effect requires the co-expression of ferritin H (heart/heavy) chain (FTH), which controls the pro-oxidant effect of labile Fe released from the protoporphyrin IX ring of heme. Heme 6-10 heme oxygenase 1 Homo sapiens 25-41 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. Heme 90-94 heme oxygenase 1 Homo sapiens 31-35 24147608-6 2014 The importance of HO-1 in MP is emphasized by their expression of specific receptors that primarily function to ingest heme-containing substrate and deliver it to HO-1. Heme 119-123 heme oxygenase 1 Homo sapiens 18-22 24180608-1 2014 SIGNIFICANCE: Heme oxygenase enzymes, which exist as constitutive (HO-2) and inducible (HO-1) isoforms, degrade heme to carbon monoxide (CO) and the bile pigment biliverdin. Heme 112-116 heme oxygenase 1 Homo sapiens 88-92 24341409-1 2014 Not only double, Janus face, but numerous appearances characterize heme oxygenase-1 (HO-1), an inducible enzyme which main role is to degrade heme. Heme 67-71 heme oxygenase 1 Homo sapiens 85-89 24847330-3 2014 HO-1 degrades heme but increases in experimental models of AKI. Heme 14-18 heme oxygenase 1 Homo sapiens 0-4 24700716-2 2014 They focus on a key enzyme involved in heme catabolism, heme oxygenase 1 (HO-1), which, ironically, has been poorly investigated in erythroid cells, the largest pool of heme-containing cells. Heme 39-43 heme oxygenase 1 Homo sapiens 56-72 24700716-2 2014 They focus on a key enzyme involved in heme catabolism, heme oxygenase 1 (HO-1), which, ironically, has been poorly investigated in erythroid cells, the largest pool of heme-containing cells. Heme 39-43 heme oxygenase 1 Homo sapiens 74-78 24681888-5 2014 Heme inhibits the transcriptional repressor activity of Bach1, resulting in the derepression of its target genes, such as globin in erythroid cells and heme oxygenase-1 in diverse cell types. Heme 0-4 heme oxygenase 1 Homo sapiens 152-168 24642709-4 2014 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in the heme metabolism, has been implicated in a various cellular processes, such as inflammatory injury and anti-oxidant/oxidant homeostasis. Heme 57-61 heme oxygenase 1 Homo sapiens 0-16 24659985-2 2014 The expression of the heme catabolizing enzyme encoded by this gene, namely HO-1, is required to successfully support reproductive events. Heme 22-26 heme oxygenase 1 Homo sapiens 76-80 24642709-4 2014 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in the heme metabolism, has been implicated in a various cellular processes, such as inflammatory injury and anti-oxidant/oxidant homeostasis. Heme 57-61 heme oxygenase 1 Homo sapiens 18-22 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. Heme 70-74 heme oxygenase 1 Homo sapiens 88-92 24095978-4 2014 HO-1/BVR-A reduces the intracellular levels of pro-oxidant heme and generates equimolar amounts of the free radical scavengers biliverdin-IX alpha (BV)/bilirubin-IX alpha (BR) as well as the pleiotropic gaseous neuromodulator carbon monoxide (CO) and ferrous iron. Heme 59-63 heme oxygenase 1 Homo sapiens 0-4 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. Heme 156-160 heme oxygenase 1 Homo sapiens 178-194 24323422-7 2013 Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin. Heme 36-40 heme oxygenase 1 Homo sapiens 0-16 24211270-1 2014 Heme oxygenase (HO)-1 is an oxidative stress-response enzyme which catalyzes the degradation of heme into bilirubin, ferric ion, and carbon monoxide (CO). Heme 96-100 heme oxygenase 1 Homo sapiens 0-21 23939757-1 2013 Heme oxygenase-1 (HMOX1) is a ubiquitously expressed inducible enzyme that degrades heme to carbon monoxide, biliverdin, and free iron ions. Heme 84-88 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. Heme 84-88 heme oxygenase 1 Homo sapiens 18-23 24323422-7 2013 Heme oxygenase-1 (HO-1) metabolizes heme to carbon monoxide, ferrous ion, and biliverdin. Heme 36-40 heme oxygenase 1 Homo sapiens 18-22 24201221-3 2013 HMOX1 is the rate-limiting enzyme of heme degradation, and the heme breakdown products, CO, Fe, and bilirubin, are considered to be biologically active metabolites with direct or indirect antioxidant and anti-inflammatory properties. Heme 37-41 heme oxygenase 1 Homo sapiens 0-5 23852701-1 2013 Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin. Heme 99-103 heme oxygenase 1 Homo sapiens 0-16 23852701-1 2013 Heme oxygenase-1 (HO-1) inhibits immune responses and inflammatory reactions via the catabolism of heme into carbon monoxide (CO), Fe(2+) , and biliverdin. Heme 99-103 heme oxygenase 1 Homo sapiens 18-22 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. Heme 50-54 heme oxygenase 1 Homo sapiens 0-4 24179613-5 2013 More specifically, the CO derived from HO-1-mediated heme catabolism has been shown to be involved in the regulation of inflammation; furthermore, administration of low concentrations of exogenous CO has a protective effect against inflammation. Heme 53-57 heme oxygenase 1 Homo sapiens 39-43 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. Heme 111-115 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. Heme 111-115 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. Heme 60-64 heme oxygenase 1 Homo sapiens 0-16 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. Heme 60-64 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. Heme 60-64 heme oxygenase 1 Homo sapiens 207-211 23720344-2 2013 Interestingly, the antioxidant enzyme heme oxygenase-1 (HO-1) is not present in the mitochondria despite the fact that the organelle is the site of heme synthesis and contains multiple heme proteins. Heme 38-42 heme oxygenase 1 Homo sapiens 56-60 23720344-2 2013 Interestingly, the antioxidant enzyme heme oxygenase-1 (HO-1) is not present in the mitochondria despite the fact that the organelle is the site of heme synthesis and contains multiple heme proteins. Heme 148-152 heme oxygenase 1 Homo sapiens 56-60 23720344-10 2013 These data suggest that specific mitochondrially targeted HO-1 under acute pathological conditions may have beneficial effects, but the selective advantage of long-term expression is constrained by a negative impact on the synthesis of heme-containing mitochondrial proteins. Heme 236-240 heme oxygenase 1 Homo sapiens 58-62 23624303-0 2013 Immuno-spin trapping of heme-induced protein radicals: Implications for heme oxygenase-1 induction and heme degradation. Heme 24-28 heme oxygenase 1 Homo sapiens 72-88 23624303-3 2013 Heme is known to induce heme oxygenase-1(HO-1) expression, and the extent of induction depends on the ratio of albumin to heme in plasma. Heme 0-4 heme oxygenase 1 Homo sapiens 24-40