PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34737578-6 2021 Hydrogen sulfide (H2S) likewise opposes mast cell activation; H2S can boost AMPK activity, up-regulate cGMP production, and trigger Nrf2-mediated induction of Phase 2 enzymes - including heme oxygenase-1, whose generation of bilirubin suppresses NADPH oxidase activity. Bilirubin 225-234 heme oxygenase 1 Homo sapiens 187-203 34293961-10 2021 Meanwhile, administration of antioxidants or heme oxygenase-1 induction to elevate the hepatocellular levels of the endogenous scavenger bilirubin are promising alternatives that need to be re-evaluated and implemented. Bilirubin 137-146 heme oxygenase 1 Homo sapiens 45-61 34483918-11 2021 Moreover, the end products of HO-1, namely, CO, Fe2+, and biliverdin (will converted to bilirubin), also decreases the expression of matrix metalloproteinase-9. Bilirubin 88-97 heme oxygenase 1 Homo sapiens 30-34 34499923-5 2022 Recent reports indicate that HO-1 with its antioxidants via the effect of bilirubin increases formation of biologically active lipid metabolites such as epoxyeicosatrienoic acid (EET), omega-3 and other polyunsaturated fatty acids (PUFAs). Bilirubin 74-83 heme oxygenase 1 Homo sapiens 29-33 34573035-0 2021 Bilirubin Links HO-1 and UGT1A1*28 Gene Polymorphisms to Predict Cardiovascular Outcome in Patients Receiving Maintenance Hemodialysis. Bilirubin 0-9 heme oxygenase 1 Homo sapiens 16-20 34573035-1 2021 Serum bilirubin levels, which are determined by a complex interplay of various enzymes, including heme oxygenase-1 (HO-1) and uridine diphosphate-glucuronosyl transferase (UGT1A1), may be protective against progression of cardiovascular disease (CVD) in hemodialysis patients. Bilirubin 6-15 heme oxygenase 1 Homo sapiens 98-114 34573035-1 2021 Serum bilirubin levels, which are determined by a complex interplay of various enzymes, including heme oxygenase-1 (HO-1) and uridine diphosphate-glucuronosyl transferase (UGT1A1), may be protective against progression of cardiovascular disease (CVD) in hemodialysis patients. Bilirubin 6-15 heme oxygenase 1 Homo sapiens 116-120 34573035-3 2021 This retrospective study enrolled 1080 prevalent hemodialysis patients and the combined genetic polymorphisms of HO-1 and UGT1A1 on serum bilirubin were analyzed. Bilirubin 138-147 heme oxygenase 1 Homo sapiens 113-117 34573035-5 2021 Mean serum bilirubin was highest in patients with S/S + S/L of the HO-1 promoter and UGT1A1 7/7 genotypes (Group 1), intermediate in those with S/S + S/L of the HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 2), and lowest in the carriers with the L/L HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 3) (p < 0.001). Bilirubin 11-20 heme oxygenase 1 Homo sapiens 67-71 34573035-5 2021 Mean serum bilirubin was highest in patients with S/S + S/L of the HO-1 promoter and UGT1A1 7/7 genotypes (Group 1), intermediate in those with S/S + S/L of the HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 2), and lowest in the carriers with the L/L HO-1 promoter and UGT1A1 7/6 + 6/6 genotypes (Group 3) (p < 0.001). Bilirubin 11-20 heme oxygenase 1 Homo sapiens 161-165 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. Bilirubin 230-239 heme oxygenase 1 Homo sapiens 0-16 35480872-0 2022 Biliverdin/Bilirubin Redox Pair Protects Lens Epithelial Cells against Oxidative Stress in Age-Related Cataract by Regulating NF-kappaB/iNOS and Nrf2/HO-1 Pathways. Bilirubin 11-20 heme oxygenase 1 Homo sapiens 150-154 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. Bilirubin 176-185 heme oxygenase 1 Homo sapiens 18-22 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. Bilirubin 187-189 heme oxygenase 1 Homo sapiens 18-22 35204062-3 2022 Exercise elevates heme oxygenase-1 (HO-1) and biliverdin reductase A (BVRA) expression as built-in protective mechanisms, which produce the most potent antioxidant, bilirubin. Bilirubin 165-174 heme oxygenase 1 Homo sapiens 18-34 35204062-3 2022 Exercise elevates heme oxygenase-1 (HO-1) and biliverdin reductase A (BVRA) expression as built-in protective mechanisms, which produce the most potent antioxidant, bilirubin. Bilirubin 165-174 heme oxygenase 1 Homo sapiens 36-40 35204062-7 2022 The main objective of this review is to describe the function of bilirubin as an antioxidant and metabolic hormone and how the HO-1-BVRA-bilirubin-PPARalpha axis influences inflammation, metabolic function and interacts with exercise to improve outcomes of weight management. Bilirubin 137-146 heme oxygenase 1 Homo sapiens 127-131 33394027-9 2021 This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KmPOR HO-1 without affecting the Vmaxapp. Bilirubin 118-127 heme oxygenase 1 Homo sapiens 36-40 33394027-9 2021 This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KmPOR HO-1 without affecting the Vmaxapp. Bilirubin 118-127 heme oxygenase 1 Homo sapiens 104-108 33394027-9 2021 This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KmPOR HO-1 without affecting the Vmaxapp. Bilirubin 118-127 heme oxygenase 1 Homo sapiens 104-108 35419301-3 2022 The upregulation of HO-1 under pathological conditions associated with cellular stress represents an important cytoprotective defense mechanism by virtue of the anti-oxidant properties of the bilirubin and the anti-inflammatory effect of the CO produced. Bilirubin 192-201 heme oxygenase 1 Homo sapiens 20-24 33484436-14 2021 CONCLUSION: The precise mechanism accountable for the anti-inflammatory features of HO-1 is not completely understood; nevertheless, the CO signaling function associated with the antioxidant property shown by bilirubin possibly will play an act in the improvement of inflammation. Bilirubin 209-218 heme oxygenase 1 Homo sapiens 84-88 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. Bilirubin 382-391 heme oxygenase 1 Homo sapiens 208-212 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. Bilirubin 230-239 heme oxygenase 1 Homo sapiens 18-22 33238962-7 2020 Serum HO-1 correlated with serum total bilirubin (R = 0.454, P < 0.001) and serum LDH (R = 0.500, P < 0.001). Bilirubin 39-48 heme oxygenase 1 Homo sapiens 6-10 32128811-5 2020 We found that BRUP-1 up-regulated the expression level of heme oxygenase-1 (HO-1), one of the rate-limiting enzyme of bilirubin production via nuclear factor erythroid 2-related factor 2 (Nrf2) activation. Bilirubin 118-127 heme oxygenase 1 Homo sapiens 58-74 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. Bilirubin 191-200 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. Bilirubin 191-200 heme oxygenase 1 Homo sapiens 18-22 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. Bilirubin 135-144 heme oxygenase 1 Homo sapiens 21-25 32128811-5 2020 We found that BRUP-1 up-regulated the expression level of heme oxygenase-1 (HO-1), one of the rate-limiting enzyme of bilirubin production via nuclear factor erythroid 2-related factor 2 (Nrf2) activation. Bilirubin 118-127 heme oxygenase 1 Homo sapiens 76-80 32278282-8 2020 Finally, silencing HO-1 expression partially rescued the proliferative and migratory response of canagliflozin-treated SMCs, and this was reversed by carbon monoxide and bilirubin. Bilirubin 170-179 heme oxygenase 1 Homo sapiens 19-23 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. Bilirubin 123-132 heme oxygenase 1 Homo sapiens 0-16 32899732-1 2020 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin. Bilirubin 139-148 heme oxygenase 1 Homo sapiens 0-16 32899732-1 2020 Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into carbon monoxide (CO), iron, and biliverdin, which is rapidly metabolized to bilirubin. Bilirubin 139-148 heme oxygenase 1 Homo sapiens 18-22 32899732-4 2020 The vasoprotection evoked by HO-1 is largely ascribed to the generation of CO and/or the bile pigments, biliverdin and bilirubin, which exert potent antioxidant and anti-inflammatory effects. Bilirubin 119-128 heme oxygenase 1 Homo sapiens 29-33 32899732-6 2020 Several therapeutic strategies are currently being pursued that may allow for the targeting of HO-1 in arterial remodeling in various pathologies, including the use of gene delivery approaches, the development of novel inducers of the enzyme, and the administration of unique formulations of CO and bilirubin. Bilirubin 299-308 heme oxygenase 1 Homo sapiens 95-99 31830562-4 2020 Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin. Bilirubin 160-169 heme oxygenase 1 Homo sapiens 47-63 31830562-4 2020 Activation of Nrf2 results in the synthesis of heme oxygenase-1 (HO-1) leading to the formation of a number of bioactive metabolites, mainly CO, biliverdin and bilirubin. Bilirubin 160-169 heme oxygenase 1 Homo sapiens 65-69 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. Bilirubin 161-170 heme oxygenase 1 Homo sapiens 0-4 32347305-11 2020 OUTCOMES: HO-1 exerts some protective effects on the placentation, probably by a combination of factors, including its interrelation with the PGC-1alpha/PPAR pathway and the sFlt1/PlGF balance, and through its primary metabolites, notably carbon monoxide and bilirubin. Bilirubin 259-268 heme oxygenase 1 Homo sapiens 10-14 32908636-6 2020 HO-1 activity leads to production of carbon monoxide (CO), free iron ion, and biliverdin; the latter is promptly reduced to bilirubin. Bilirubin 124-133 heme oxygenase 1 Homo sapiens 0-4 32006543-1 2020 OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin. Bilirubin 77-86 heme oxygenase 1 Homo sapiens 11-27 32006543-1 2020 OBJECTIVE: Heme oxygenase-1 (HO-1) degrades heme to CO, iron, and biliverdin/bilirubin. Bilirubin 77-86 heme oxygenase 1 Homo sapiens 29-33 32006543-2 2020 Although serum bilirubin levels were often reported in patients with coronary artery disease (CAD), HO-1 levels in patients with CAD and the association between HO-1 and bilirubin levels have not been clarified. Bilirubin 170-179 heme oxygenase 1 Homo sapiens 161-165 31425676-2 2019 In a few instances e.g., neonatal jaundice, overproduction of HO-1 and increased HO activity results in elevated levels of bilirubin requiring clinical intervention with inhibitors of HO activity. Bilirubin 123-132 heme oxygenase 1 Homo sapiens 62-66 32082188-3 2020 This review aims to provide an up-to-date and critical overview of the molecular mechanisms by which bilirubin derived from plasma or from HMOX1 activation in vascular cells affects endothelial function. Bilirubin 101-110 heme oxygenase 1 Homo sapiens 139-144 32082188-5 2020 In this context, therapeutic interventions aimed at mildly increasing serum bilirubin as well as bilirubin generated endogenously by endothelial HMOX1 should be considered. Bilirubin 97-106 heme oxygenase 1 Homo sapiens 145-150 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. Bilirubin 142-151 heme oxygenase 1 Homo sapiens 24-28 31771519-20 2019 Bilirubin levels may become elevated as a result of heme oxygenase-1 activation, occurring in exercise-induced acute kidney injury in patients with RHUC; this phenomenon suggests renal ischemia-reperfusion injury. Bilirubin 0-9 heme oxygenase 1 Homo sapiens 52-68 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. Bilirubin 123-125 heme oxygenase 1 Homo sapiens 0-22 31425676-3 2019 In contrast HO-1 levels and HO activity are low in obesity and the HO system responds to mitigate the deleterious effects of oxidative stress through increased levels of bilirubin (anti-inflammatory) and CO (anti-apoptotic) and decreased levels of heme (pro-oxidant). Bilirubin 170-179 heme oxygenase 1 Homo sapiens 12-16 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. Bilirubin 187-196 heme oxygenase 1 Homo sapiens 0-16 31396090-3 2019 Heme oxygenase (HO) -1 can catabolize free heme into carbon monoxide (CO), ferrous iron, and biliverdin (BV)/bilirubin (BR). Bilirubin 109-118 heme oxygenase 1 Homo sapiens 0-22 31344980-1 2019 Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme to generate ferrous iron, carbon monoxide (CO), and biliverdin, which is subsequently converted to bilirubin. Bilirubin 187-196 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. Bilirubin 194-203 heme oxygenase 1 Homo sapiens 20-24 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. Bilirubin 101-110 heme oxygenase 1 Homo sapiens 30-34 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). Bilirubin 229-238 heme oxygenase 1 Homo sapiens 24-28 30605610-3 2019 As one of antioxidant defense systems, heme oxygenase-1 (HO-1) acts as an essential role in tumor development by offering antioxidant bilirubin to protect cancer cells under stress conditions. Bilirubin 134-143 heme oxygenase 1 Homo sapiens 39-55 30605610-3 2019 As one of antioxidant defense systems, heme oxygenase-1 (HO-1) acts as an essential role in tumor development by offering antioxidant bilirubin to protect cancer cells under stress conditions. Bilirubin 134-143 heme oxygenase 1 Homo sapiens 57-61 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). Bilirubin 108-117 heme oxygenase 1 Homo sapiens 0-16 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. Bilirubin 67-76 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. Bilirubin 66-75 heme oxygenase 1 Homo sapiens 0-21 29974998-6 2018 Moreover, the expression of HO-1, a functional modulator of Tregs, was decreased in vitiligo Tregs, and the concentrations of HO-1 metabolites, including bilirubin, CoHb and iron, were correspondingly decreased in serum of vitiligo patients. Bilirubin 154-163 heme oxygenase 1 Homo sapiens 126-130 30153269-7 2018 These data suggest that the HO-1-derived metabolites, CO and bilirubin, elevate astrocytic mitochondrial function via a HIF-1alpha/ERRalpha circuit coupled with L-type Ca2+ channel activation and PGC-1alpha-mediated oxygen consumption. Bilirubin 61-70 heme oxygenase 1 Homo sapiens 28-32 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. Bilirubin 197-206 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. Bilirubin 197-206 heme oxygenase 1 Homo sapiens 18-22 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. Bilirubin 119-128 heme oxygenase 1 Homo sapiens 11-27 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. Bilirubin 109-118 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. Bilirubin 109-118 heme oxygenase 1 Homo sapiens 18-22 28206992-3 2017 Polymorphisms of the HO-1 gene promoter may modulate transcriptional activity, thereby augmenting or attenuating HO-1 expression with resultant modulation of the production of bilirubin. Bilirubin 176-185 heme oxygenase 1 Homo sapiens 21-25 28206992-5 2017 In this clinical review, we surveyed the role of HO-1 gene promoter polymorphisms in the control of bilirubin production and further considered their role, if any, in the pathophysiology of neonatal hyperbilirubinemia. Bilirubin 100-109 heme oxygenase 1 Homo sapiens 49-53 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. Bilirubin 119-128 heme oxygenase 1 Homo sapiens 29-33 27662012-0 2016 Mutating heme oxygenase-1 into a peroxidase causes a defect in bilirubin synthesis associated with microcytic anemia and severe hyperinflammation. Bilirubin 63-72 heme oxygenase 1 Homo sapiens 9-25 28978042-1 2017 Heme oxygenase-1 (HO-1) degrades heme to bilirubin. Bilirubin 41-50 heme oxygenase 1 Homo sapiens 0-16 28978042-1 2017 Heme oxygenase-1 (HO-1) degrades heme to bilirubin. Bilirubin 41-50 heme oxygenase 1 Homo sapiens 18-22 27943244-1 2017 OBJECTIVE: The present study was undertaken to investigate the genotype and allele frequencies of the variants in the four bilirubin metabolism genes (UGT1A1, OATP2, HMOX1, and BLVRA) and their association with hyperbilirubinemia. Bilirubin 123-132 heme oxygenase 1 Homo sapiens 166-171 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. Bilirubin 113-122 heme oxygenase 1 Homo sapiens 11-15 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. Bilirubin 73-82 heme oxygenase 1 Homo sapiens 16-20 26270345-8 2015 Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity. Bilirubin 53-62 heme oxygenase 1 Homo sapiens 31-35 27411481-8 2016 RESULTS: SSc patients have lower plasma levels of bilirubin, suggestive of an aberrant HO-1 function. Bilirubin 50-59 heme oxygenase 1 Homo sapiens 87-91 27381978-7 2016 In the human endothelial Ea.hy926 cell line, we demonstrated that intracellular bilirubin (3-5 pmol mg(-1) protein) could be modulated by either extracellular bilirubin uptake, or by up-regulation of heme oxygenase-1, a cellular enzyme related to endogenous bilirubin synthesis. Bilirubin 80-89 heme oxygenase 1 Homo sapiens 200-216 26968795-0 2016 Heme oxygenase-1-derived bilirubin counteracts HIV protease inhibitor-mediated endothelial cell dysfunction. Bilirubin 25-34 heme oxygenase 1 Homo sapiens 0-16 26968795-9 2016 Inhibition of HO-1 activity or expression potentiated the anti-proliferative and inflammatory actions of PIs which was reversed by bilirubin but not carbon monoxide. Bilirubin 131-140 heme oxygenase 1 Homo sapiens 14-18 26968795-12 2016 Thus, induction of HO-1 via the ROS-Nrf2 pathway in human ECs counteracts the anti-proliferative and inflammatory actions of PIs by generating bilirubin. Bilirubin 143-152 heme oxygenase 1 Homo sapiens 19-23 26166253-2 2016 HO-1, a cellular stress protein, serves a vital metabolic function as the rate-limiting step in the degradation of heme to generate carbon monoxide (CO), iron, and biliverdin-IXalpha (BV), the latter which is converted to bilirubin-IXalpha (BR). Bilirubin 222-239 heme oxygenase 1 Homo sapiens 0-4 25922869-1 2015 BACKGROUND: In vitro and animal studies indicate that statins increase heme oxygenase-1 gene (HMOX1) expression, which then, presumably, increases plasma bilirubin concentration. Bilirubin 154-163 heme oxygenase 1 Homo sapiens 94-99 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. Bilirubin 205-214 heme oxygenase 1 Homo sapiens 46-51 26779023-9 2015 All together, these results corroborate the neuroprotective effect of FA through the up-regulation of the HO-1/BVR system, via carbon monoxide and BR formation, and provide the first evidence on the role of HO-1/Nrf2 axis in FA-related enhancement of cell stress response in human neurons. Bilirubin 147-149 heme oxygenase 1 Homo sapiens 106-114 26779023-9 2015 All together, these results corroborate the neuroprotective effect of FA through the up-regulation of the HO-1/BVR system, via carbon monoxide and BR formation, and provide the first evidence on the role of HO-1/Nrf2 axis in FA-related enhancement of cell stress response in human neurons. Bilirubin 147-149 heme oxygenase 1 Homo sapiens 106-110 26631587-9 2016 Key messages Bilirubin levels are inversely related to cardiovascular disease, and overexpression of heme oxygenase-1 (the enzyme that determines bilirubin production) has prevented post-infarction ventricular remodeling in experimental animals, but the association between bilirubin levels and the progression of ventricular volumes and function in patients with acute myocardial infarction remained unexplored. Bilirubin 146-155 heme oxygenase 1 Homo sapiens 101-117 26631587-9 2016 Key messages Bilirubin levels are inversely related to cardiovascular disease, and overexpression of heme oxygenase-1 (the enzyme that determines bilirubin production) has prevented post-infarction ventricular remodeling in experimental animals, but the association between bilirubin levels and the progression of ventricular volumes and function in patients with acute myocardial infarction remained unexplored. Bilirubin 274-283 heme oxygenase 1 Homo sapiens 101-117 26270345-8 2015 Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity. Bilirubin 53-62 heme oxygenase 1 Homo sapiens 93-97 26270345-8 2015 Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity. Bilirubin 53-62 heme oxygenase 1 Homo sapiens 93-97 26270345-8 2015 Although two other products of HO-1 activity--CO and bilirubin--have been invoked to explain HO-1-mediated cytoprotection, we conclude that, at least in this experimental system, HO-1 activity triggers the induction of ferritin and the latter is actually responsible for the cytoprotective effects of HO-1 activity. Bilirubin 53-62 heme oxygenase 1 Homo sapiens 93-97 25820186-7 2015 CO and Fe were implicated in the HMOX1 effects, whereas bilirubin was inert or counteracted the HMOX1-related changes. Bilirubin 56-65 heme oxygenase 1 Homo sapiens 96-101 26146841-3 2015 Eleven common mutations and polymorphisms across five bilirubin metabolism genes, namely those encoding UGT1A1, HMOX1, BLVRA, SLCO1B1 and SLCO1B3, were determined using the high resolution melt (HRM) assay or PCR-capillary electrophoresis analysis. Bilirubin 54-63 heme oxygenase 1 Homo sapiens 112-117 24690955-2 2014 Bilirubin is produced by heme oxygenase-1 (HO-1), catalyzed by UDP-glucuronosyltransferase (UGT1A1), and has potential as an antioxidant. Bilirubin 0-9 heme oxygenase 1 Homo sapiens 25-41 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. Bilirubin 57-66 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. Bilirubin 65-74 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. Bilirubin 65-74 heme oxygenase 1 Homo sapiens 18-22 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. Bilirubin 158-167 heme oxygenase 1 Homo sapiens 54-70 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. Bilirubin 158-167 heme oxygenase 1 Homo sapiens 72-76 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. Bilirubin 179-188 heme oxygenase 1 Homo sapiens 31-35 24131232-5 2014 Moreover, therapeutic delivery of HO-1 products CO, biliverdin, and bilirubin has been shown to have favorable effects, notably on endothelial cells and in animal models of vascular disease. Bilirubin 68-77 heme oxygenase 1 Homo sapiens 34-38 25371888-6 2014 In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide. Bilirubin 93-102 heme oxygenase 1 Homo sapiens 88-92 25371888-6 2014 In addition, the HO-1 inducer cobalt protoporphyrin (CoPP) and the metabolic product of HO-1 bilirubin mimicked diazoxide to inhibit sFlt-1 release and reactive oxygen species (ROS) production under hypoxia, whereas the HO-1 inhibitor zinc protoporphyrin IX (ZnPP IX) antagonized the effect of diazoxide. Bilirubin 93-102 heme oxygenase 1 Homo sapiens 88-92 26159150-7 2015 Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin. Bilirubin 229-238 heme oxygenase 1 Homo sapiens 46-50 26159150-7 2015 Intriguingly, pharmacological inactivation of HO-1 with zinc protoporphyrin IX reversed anti-inflammatory effect of ZY- 1A4, but the anti-inflammatory effect of ZY-1A4 was largely mimicked by HO-1 by-products carbon monoxide and bilirubin. Bilirubin 229-238 heme oxygenase 1 Homo sapiens 192-196 25262300-1 2014 OBJECTIVE: To explore the effects of variants in Uridine Diphosphate Glucuronosyl Transferase 1A1 (UGT1A1) and Heme Oxygenase-1 (HMOX1) on daily physiological bilirubin levels and bilirubin changes during the first week after birth in Chinese newborns. Bilirubin 159-168 heme oxygenase 1 Homo sapiens 111-127 25262300-1 2014 OBJECTIVE: To explore the effects of variants in Uridine Diphosphate Glucuronosyl Transferase 1A1 (UGT1A1) and Heme Oxygenase-1 (HMOX1) on daily physiological bilirubin levels and bilirubin changes during the first week after birth in Chinese newborns. Bilirubin 159-168 heme oxygenase 1 Homo sapiens 129-134 25262300-2 2014 Both UGT1A1 and HMOX1 code rate-limiting enzymes in the bilirubin metabolism pathway. Bilirubin 56-65 heme oxygenase 1 Homo sapiens 16-21 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. Bilirubin 146-155 heme oxygenase 1 Homo sapiens 99-115 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. Bilirubin 146-155 heme oxygenase 1 Homo sapiens 117-121 24690955-2 2014 Bilirubin is produced by heme oxygenase-1 (HO-1), catalyzed by UDP-glucuronosyltransferase (UGT1A1), and has potential as an antioxidant. Bilirubin 0-9 heme oxygenase 1 Homo sapiens 43-47 25344086-4 2014 HO-1 along with its reaction products bilirubin and CO are protective against ischemia-induced injury (myocardial infarction, ischemia-reperfusion (IR)-injury and post-infarct structural remodelling). Bilirubin 38-47 heme oxygenase 1 Homo sapiens 0-4 24323422-8 2013 CO activates cGMP to promote vasodilation, and biliverdin is converted to bilirubin which can serve as an anti-oxidant, both of which may contribute to the reported protective role of HO-1 in cerebral ischemia and subarachnoid hemorrhage. Bilirubin 74-83 heme oxygenase 1 Homo sapiens 184-188 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). Bilirubin 106-115 heme oxygenase 1 Homo sapiens 0-21 23877636-1 2013 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in bilirubin metabolism, and its genetic variant may modulate hyperbilirubinemia risk in neonates. Bilirubin 53-62 heme oxygenase 1 Homo sapiens 0-16 23877636-1 2013 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in bilirubin metabolism, and its genetic variant may modulate hyperbilirubinemia risk in neonates. Bilirubin 53-62 heme oxygenase 1 Homo sapiens 18-22 22147556-2 2012 The production of nitric oxide by the conversion of l-(2,3,4,5)-[3H] arginine to l-(3H) citrulline, the activity of haem oxygenase 1 (HO-1) through bilirubin synthesis and the expression of inducible nitric oxide synthase (iNOS), HO-1 proteins and messenger RNA by Western blot and reverse-transcribed polymerase chain reaction were also tested. Bilirubin 148-157 heme oxygenase 1 Homo sapiens 116-132 22444871-6 2012 This effect is suppressed by the pharmacological inhibition of HO-1 and mimicked by the end-products of HO activity, i.e., bilirubin and carbon monoxide. Bilirubin 123-132 heme oxygenase 1 Homo sapiens 63-67 22212955-0 2012 Association of serum bilirubin and promoter variations in HMOX1 and UGT1A1 genes with sporadic colorectal cancer. Bilirubin 21-30 heme oxygenase 1 Homo sapiens 58-63 23932761-6 2013 Consistent with this view, high expression alleles of the major enzymatic source of bilirubin, heme oxygenase-1 (HO-1), do associate with decreased vascular risk in the majority of studies that have addressed this issue, and increased plasma bilirubin has been reported in carriers of these alleles. Bilirubin 84-93 heme oxygenase 1 Homo sapiens 95-111 23932761-6 2013 Consistent with this view, high expression alleles of the major enzymatic source of bilirubin, heme oxygenase-1 (HO-1), do associate with decreased vascular risk in the majority of studies that have addressed this issue, and increased plasma bilirubin has been reported in carriers of these alleles. Bilirubin 242-251 heme oxygenase 1 Homo sapiens 95-111 23615401-8 2013 HO-1 end products, such as carbon monoxide, free iron and bilirubin, suppressed the TPA-induced MMP-9 mRNA and protein expression, enzyme activity, migration and invasion in MCF-7 cells. Bilirubin 58-67 heme oxygenase 1 Homo sapiens 0-4 23403148-5 2013 CO and bilirubin (a downstream product of biliverdin processing) account for the angiogenic, vasodilatory and anti-oxidant properties of HO-1. Bilirubin 7-16 heme oxygenase 1 Homo sapiens 137-141 23092328-6 2013 HO-1 is a heme-degrading enzyme generating carbon monoxide, iron, and biliverdin/bilirubin, while BCRP is a heme efflux transporter. Bilirubin 81-90 heme oxygenase 1 Homo sapiens 0-4 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. Bilirubin 83-92 heme oxygenase 1 Homo sapiens 179-183 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. Bilirubin 81-90 heme oxygenase 1 Homo sapiens 20-24 22683349-11 2012 Moreover, bilirubin, an antioxidant and physiologic product of HO-1, is protective against mitochondrial oxidative stress. Bilirubin 10-19 heme oxygenase 1 Homo sapiens 63-67 22147556-2 2012 The production of nitric oxide by the conversion of l-(2,3,4,5)-[3H] arginine to l-(3H) citrulline, the activity of haem oxygenase 1 (HO-1) through bilirubin synthesis and the expression of inducible nitric oxide synthase (iNOS), HO-1 proteins and messenger RNA by Western blot and reverse-transcribed polymerase chain reaction were also tested. Bilirubin 148-157 heme oxygenase 1 Homo sapiens 134-138 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. Bilirubin 142-151 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. Bilirubin 142-151 heme oxygenase 1 Homo sapiens 18-22 22095827-2 2012 Niacin is a pleiotropic drug that slows the progression of coronary artery disease and increases serum levels of the HO-1 enzymatic product bilirubin. Bilirubin 140-149 heme oxygenase 1 Homo sapiens 117-121 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. Bilirubin 85-94 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. Bilirubin 85-94 heme oxygenase 1 Homo sapiens 96-100 21917385-4 2011 These considerations suggest that bilirubin, generated within lymphocytes by HO-1 activation, may play a physiological role in the promotion of Treg immunomodulation. Bilirubin 34-43 heme oxygenase 1 Homo sapiens 77-81 22195275-0 2012 Heme Oxygenase-1 Attenuates Hypoxia-Induced sFlt-1 and Oxidative Stress in Placental Villi through Its Metabolic Products CO and Bilirubin. Bilirubin 129-138 heme oxygenase 1 Homo sapiens 0-16 21840000-2 2011 As statins can stimulate heme oxygenase-1 (HO-1), which increases bilirubin production, we investigated whether statins in routine use increase total bilirubin levels in subjects at high cardiovascular risk. Bilirubin 66-75 heme oxygenase 1 Homo sapiens 25-41 21917385-5 2011 This effect of bilirubin is likely to be independent of NADPH oxidase inhibition, since the NAPDH oxidase activity of macrophages is necessary for Treg induction, possibly because it contributes to HO-1 induction in lymphocytes. Bilirubin 15-24 heme oxygenase 1 Homo sapiens 198-202 21593686-8 2011 HO-1 activity was determined in microsomal fractions from HUVECs by monitoring the conversion of heme into bilirubin. Bilirubin 107-116 heme oxygenase 1 Homo sapiens 0-4 21552291-11 2011 Finally, H(2)O(2)-mediated cell death was rescued significantly in p53-deficient cells by antioxidant treatment, as well as by bilirubin, a by-product of HO-1 metabolism. Bilirubin 127-136 heme oxygenase 1 Homo sapiens 154-158 22090784-1 2011 Heme oxygenase-1 (HO-1) system catalyzes heme to biologically active products: carbon monoxide, biliverdin/bilirubin and free iron. Bilirubin 107-116 heme oxygenase 1 Homo sapiens 0-16 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. Bilirubin 61-70 heme oxygenase 1 Homo sapiens 119-123 21635873-5 2011 Interestingly, the glutathione donor N-acetyl-l-cysteine or the NADPH oxidase inhibitor apocynin blocked the induction of HO-1 by compound C. Finally, compound C stimulated EC death and this was potentiated by silencing HO-1 expression and reversed by the administration of CO, biliverdin, or bilirubin. Bilirubin 293-302 heme oxygenase 1 Homo sapiens 122-126 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. Bilirubin 134-143 heme oxygenase 1 Homo sapiens 0-4 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. Bilirubin 205-214 heme oxygenase 1 Homo sapiens 56-60 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. Bilirubin 131-140 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. Bilirubin 131-140 heme oxygenase 1 Homo sapiens 18-22 21198350-0 2011 Association of (GT)n repeats promoter polymorphism of heme oxygenase-1 gene with serum bilirubin levels in healthy Indian adults. Bilirubin 87-96 heme oxygenase 1 Homo sapiens 54-70 21198350-1 2011 AIM: The present study was undertaken to investigate a length polymorphism of (GT)n repeats of the heme oxygenase-1 (HMOX-1) gene and its association with serum bilirubin levels in apparently healthy adults. Bilirubin 161-170 heme oxygenase 1 Homo sapiens 99-115 21198350-1 2011 AIM: The present study was undertaken to investigate a length polymorphism of (GT)n repeats of the heme oxygenase-1 (HMOX-1) gene and its association with serum bilirubin levels in apparently healthy adults. Bilirubin 161-170 heme oxygenase 1 Homo sapiens 117-123 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. Bilirubin 191-200 heme oxygenase 1 Homo sapiens 33-37 20704550-5 2010 The vasoprotection afforded by HO-1 is largely attributable to its end products: CO and the bile pigments, biliverdin and bilirubin. Bilirubin 122-131 heme oxygenase 1 Homo sapiens 31-35 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. Bilirubin 182-191 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. Bilirubin 182-191 heme oxygenase 1 Homo sapiens 18-22 20704544-2 2010 BVR is the sole catalyst for the conversion of biliverdin-IXalpha the activity product of the stress-inducible HO-1 and the constitutive HO-2, to bilirubin-IXalpha. Bilirubin 146-155 heme oxygenase 1 Homo sapiens 111-115 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. Bilirubin 131-140 heme oxygenase 1 Homo sapiens 0-4 20679134-2 2010 Enzymatic studies with the purified 30-kDa form of HO-1 routinely use a coupled assay containing biliverdin reductase (BVR), which converts BV to bilirubin (BR). Bilirubin 146-155 heme oxygenase 1 Homo sapiens 51-55 20430037-0 2010 Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin. Bilirubin 28-37 heme oxygenase 1 Homo sapiens 108-124 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). Bilirubin 115-124 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). Bilirubin 115-124 heme oxygenase 1 Homo sapiens 30-34 20689484-4 2010 METHODS: Changes in the HO-1 activity after AMI were analyzed by measuring serum levels of bilirubin and Fe. Bilirubin 91-100 heme oxygenase 1 Homo sapiens 24-28 20689484-9 2010 Furthermore, the serum HO-1 protein level was elevated, and its change was significantly correlated with the change in bilirubin level (r = 0.82, P < 0.005). Bilirubin 119-128 heme oxygenase 1 Homo sapiens 23-27 20430037-0 2010 Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1-evidence for direct and indirect antioxidant actions of bilirubin. Bilirubin 181-190 heme oxygenase 1 Homo sapiens 108-124 20430037-2 2010 HO-1-derived bilirubin is an efficient scavenger of reactive oxygen and nitrogen species (RONS). Bilirubin 13-22 heme oxygenase 1 Homo sapiens 0-4 20430037-3 2010 It remains to determine whether conversion of biliverdin to bilirubin is an essential step for HO-1-conferred protection of endothelial cells. Bilirubin 60-69 heme oxygenase 1 Homo sapiens 95-99 20430037-7 2010 HO-1- and BVR-silenced cells have increased levels of oxidative stress and bilirubin but not biliverdin increased expression of the protective protein GTP-cyclohydrolase. Bilirubin 75-84 heme oxygenase 1 Homo sapiens 0-4 20430037-8 2010 Moreover, protection by hemin-induced HO-1 expression or biliverdin-triggered bilirubin formation was impaired upon silencing of the HO-1 or BVR gene, respectively. Bilirubin 78-87 heme oxygenase 1 Homo sapiens 133-137 19890094-5 2010 The protective effect was specific for HO-1 because it was reproduced on administration of the end products of HO-1 activity, carbon monoxide, and bilirubin, and prevented by the pharmacologic inhibition of HO-1 using tin mesoporphyrin IX. Bilirubin 147-156 heme oxygenase 1 Homo sapiens 39-43 20370320-2 2010 Several clinical and epidemiological studies have been carried out on key enzymes generating and eliminating bilirubin (heme oxygenase-1 and UDP-glucuronosyltransferase UGT1A1, respectively) and their regulation by the AhR. Bilirubin 109-118 heme oxygenase 1 Homo sapiens 120-136 20631420-3 2010 As HO-1 can produce endogenous anti-oxidant and anti-inflammatory moieties such as bilirubin and carbon monoxide (CO), these findings suggest a novel mechanism of action for aminosalicylates, acting as anti-colitic agents through the up-regulation of HO-1 enzyme expression and activity. Bilirubin 83-92 heme oxygenase 1 Homo sapiens 3-7 20155807-10 2010 Furthermore, 6-OHDA-induced toxicity was blocked by bilirubin and carbon monoxide, products of the HO-1-catalyzed degradation of heme. Bilirubin 52-61 heme oxygenase 1 Homo sapiens 99-103 20518085-1 2010 Heme oxygenase-1 (HO-1) system catabolizes heme into three products: carbon monoxide, biliverdin/bilirubin and free iron. Bilirubin 97-106 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. Bilirubin 97-106 heme oxygenase 1 Homo sapiens 18-22 20020468-6 2010 Furthermore, downstream products of HO-1, bilirubin, carbon monoxide, and iron, are involved in the inhibitory action of HO-1. Bilirubin 42-51 heme oxygenase 1 Homo sapiens 36-40 20020468-6 2010 Furthermore, downstream products of HO-1, bilirubin, carbon monoxide, and iron, are involved in the inhibitory action of HO-1. Bilirubin 42-51 heme oxygenase 1 Homo sapiens 121-125 19457088-7 2009 Heme-derived free ferrous iron, CO, and biliverdin/bilirubin are biologically active substances that have been shown to either ameliorate or exacerbate neural injury contingent upon specific disease models employed, the intensity and duration of HO-1 expression and the nature of the prevailing redox microenvironment. Bilirubin 51-60 heme oxygenase 1 Homo sapiens 246-250 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. Bilirubin 120-129 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. Bilirubin 120-129 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. Bilirubin 156-165 heme oxygenase 1 Homo sapiens 0-16 19925812-1 2010 Heme oxygenase-1 (HO-1) is up-regulated in response to oxidative stress and catalyzes the degradation of pro-oxidant heme to carbon monoxide (CO), iron and bilirubin. Bilirubin 156-165 heme oxygenase 1 Homo sapiens 18-22 19925812-13 2010 These results indicate that the downstream products of HO-1, i.e. bilirubin and CO, modulate BDNF and GDNF expression in neuron and astrocyte. Bilirubin 66-75 heme oxygenase 1 Homo sapiens 55-59 20184791-5 2010 Over the past decade, compelling evidence has revealed that the induction of HO-1 represents an important defensive mechanism against further oxidative injury in tissues and cells following various insults; this occurs by virtue of the anti-inflammatory and antioxidant capacities of CO, biliverdin, and the subsequent metabolite of biliverdin, bilirubin. Bilirubin 345-354 heme oxygenase 1 Homo sapiens 77-81 20608094-4 2009 Expressions of biopyrrins and heme oxygenase-1 (HO-1), a stress-responsive bilirubin-producing enzyme, in heart, aorta, kidney, liver and lung were immunostained with autopsied specimens. Bilirubin 75-84 heme oxygenase 1 Homo sapiens 30-46 20608094-4 2009 Expressions of biopyrrins and heme oxygenase-1 (HO-1), a stress-responsive bilirubin-producing enzyme, in heart, aorta, kidney, liver and lung were immunostained with autopsied specimens. Bilirubin 75-84 heme oxygenase 1 Homo sapiens 48-52 20608094-12 2009 Induction of anti-oxidative enzyme HO-1 seemed to be involved in the activation of bilirubin/biopyrrin pathway. Bilirubin 83-92 heme oxygenase 1 Homo sapiens 35-39 19625608-7 2009 Finally, treatment of endothelial cells with HOCl stimulated mitochondrial dysfunction, caspase-3 activation, and cell death that was potentiated by the HO inhibitor, tin protoporphyrin-IX, or by the knockdown of HO-1, and reversed by the exogenous administration of biliverdin, bilirubin, or CO. Bilirubin 279-288 heme oxygenase 1 Homo sapiens 213-217 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. Bilirubin 296-305 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. Bilirubin 296-305 heme oxygenase 1 Homo sapiens 18-22 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. Bilirubin 105-114 heme oxygenase 1 Homo sapiens 0-16 19457084-3 2009 Heme oxygenase-1 (HO-1), an enzyme that converts heme to free iron, carbon monoxide (CO) and biliverdin (bilirubin precursor) is expressed in response to various stressors. Bilirubin 105-114 heme oxygenase 1 Homo sapiens 18-22 19063990-0 2009 Heme oxygenase-1 induction prevents neuronal damage triggered during mitochondrial inhibition: role of CO and bilirubin. Bilirubin 110-119 heme oxygenase 1 Homo sapiens 0-16 19243019-8 2009 Among polymorphisms in other genes, only the (GT)n repeat polymorphism in the HMOX1 promoter region showed association with TBIL levels in the Uyghur population, but not in the Han and Kazak populations. Bilirubin 124-128 heme oxygenase 1 Homo sapiens 78-83 19389234-1 2009 BACKGROUND: Heme oxygenase-1 is an inducible cytoprotective enzyme which handles oxidative stress by generating anti-oxidant bilirubin and vasodilating carbon monoxide. Bilirubin 125-134 heme oxygenase 1 Homo sapiens 12-28 19131520-4 2009 This allows measurement of bilirubin formation after incorporation of full-length CPR and heme oxygenase-1 (HO-1) into a membrane environment. Bilirubin 27-36 heme oxygenase 1 Homo sapiens 90-106 19131520-4 2009 This allows measurement of bilirubin formation after incorporation of full-length CPR and heme oxygenase-1 (HO-1) into a membrane environment. Bilirubin 27-36 heme oxygenase 1 Homo sapiens 108-112 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). Bilirubin 231-240 heme oxygenase 1 Homo sapiens 0-16 19238116-2 2009 This study investigated the genetic variants of four bilirubin metabolism genes--heme oxygenase-1 (HMOX1), biliverdin reductase A (BLVRA), solute carrier organic anion transporter family member 1B1 (SLCO1B1), and uridine diphosphate glycosyltransferase 1A1 (UGT1A1)--in relation to TBIL levels and CAD. Bilirubin 53-62 heme oxygenase 1 Homo sapiens 99-104 19036700-0 2009 Heme oxygenase-1 expression enhances vascular endothelial resistance to complement-mediated injury through induction of decay-accelerating factor: a role for increased bilirubin and ferritin. Bilirubin 168-177 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). Bilirubin 242-251 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). Bilirubin 231-240 heme oxygenase 1 Homo sapiens 18-22 19162549-2 2009 Over the past few years it has become apparent that these "arms" of the HO-1 system can act protectively in a variety of experimental models of disease; there is also evidence that HO-1 and bilirubin have protective actions in humans. Bilirubin 190-199 heme oxygenase 1 Homo sapiens 72-76 19092646-8 2009 HO-1 and its antioxidant product bilirubin have been reported to be not only involved in vasoprotection, but to have a similar function in gastric tissue. Bilirubin 33-42 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. Bilirubin 157-166 heme oxygenase 1 Homo sapiens 0-16 19046352-3 2009 In the current study, we determined the effects of HO-1 over-expression and its byproducts iron (Fe(2+)), carbon monoxide (CO) and bilirubin on CH biosynthesis, CH efflux and oxysterol formation in cultured astroglia. Bilirubin 131-140 heme oxygenase 1 Homo sapiens 51-55 19120903-2 2008 Two end products of heme degradation, carbon monoxide (CO) and bilirubin, are involved in the protective role of HO-1 against oxidative injury. Bilirubin 63-72 heme oxygenase 1 Homo sapiens 113-117 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. Bilirubin 157-166 heme oxygenase 1 Homo sapiens 18-22 18567745-3 2008 Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health. Bilirubin 202-211 heme oxygenase 1 Homo sapiens 109-125 18443197-0 2008 Serum bilirubin and ferritin levels link heme oxygenase-1 gene promoter polymorphism and susceptibility to coronary artery disease in diabetic patients. Bilirubin 6-15 heme oxygenase 1 Homo sapiens 41-57 18443197-3 2008 The aim of this study was to assess the association of the length of (GT)(n) repeats in the HO-1 gene promoter with serum bilirubin, markers of iron status, and the development of coronary artery disease (CAD). Bilirubin 122-131 heme oxygenase 1 Homo sapiens 92-96 18443197-9 2008 With adjustment for both serum bilirubin and ferritin, the effect of HO-1 promoter polymorphism on susceptibility to CAD disappeared. Bilirubin 31-40 heme oxygenase 1 Homo sapiens 69-73 18443197-10 2008 CONCLUSIONS: Length polymorphism in the HO-1 gene promoter is correlated with susceptibility to CAD in diabetic patients, and this effect might be conveyed through its influence on serum bilirubin and ferritin. Bilirubin 187-196 heme oxygenase 1 Homo sapiens 40-44 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. Bilirubin 201-210 heme oxygenase 1 Homo sapiens 0-19 18567745-3 2008 Moreover, many, but not all, phenolic compounds can have indirect antioxidative effects through induction of heme oxygenase-1 (HO-1), which has antiinflammatory functions via production of antioxidants bilirubin and biliverdin as well as carbon monoxide, thereby contributing to cardiovascular health. Bilirubin 202-211 heme oxygenase 1 Homo sapiens 127-131 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. Bilirubin 140-149 heme oxygenase 1 Homo sapiens 0-16 18205746-8 2008 Treatment with antioxidants (bilirubin, N-acetylcysteine) protected cells against nicotine-induced cytotoxicity and blocked the upregulation of HO-1, the effects of which were more pronounced in IHOK cells than in HN12 cells. Bilirubin 29-38 heme oxygenase 1 Homo sapiens 144-148 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. Bilirubin 140-149 heme oxygenase 1 Homo sapiens 18-22 18289069-3 2008 The precise underlying mechanisms for HO-1-based protection are not yet completely understood, but appear to involve the protective effects of HO-1 by-products, carbon monoxide (CO), biliverdin/bilirubin and free iron. Bilirubin 194-203 heme oxygenase 1 Homo sapiens 38-42 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. Bilirubin 163-172 heme oxygenase 1 Homo sapiens 63-67 18289074-1 2008 Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. Bilirubin 119-128 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. Bilirubin 119-128 heme oxygenase 1 Homo sapiens 18-22 17915953-10 2007 The R254K full-length form had a specific activity of approximately 200-225 nmol of bilirubin h-1 nmol-1 HO-1 as compared to approximately 140-150 nmol of bilirubin h-1 nmol-1 for the WT form, which contains the 30 kDa contaminant. Bilirubin 84-93 heme oxygenase 1 Homo sapiens 105-109 17919067-7 2007 Accumulating evidence indicates that biliverdin/bilirubin can mediate the protective effects of HO-1 in many disease models, such as IRI and organ transplantation, via its antiinflammatory, antiapoptotic, antiproliferative, and antioxidant properties, as well as its effects on the immune response. Bilirubin 48-57 heme oxygenase 1 Homo sapiens 96-100 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. Bilirubin 196-205 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. Bilirubin 196-205 heme oxygenase 1 Homo sapiens 106-110 17279724-2 2007 It is known to inhibit heme-oxygenase-1 (HO-1), resulting in suppressed biliverdin/bilirubin production accompanying lowered antioxidative capacity. Bilirubin 83-92 heme oxygenase 1 Homo sapiens 23-39 17671894-14 2007 On the contrary, HO-1 is highly upregulated and it plays a very important role of antioxidation, because HO-1 generates biliverdin, which being converted to bilirubin exhibits a very potent antioxidative effect, and hence antiapoptosis in tumors. Bilirubin 157-166 heme oxygenase 1 Homo sapiens 17-21 17671894-14 2007 On the contrary, HO-1 is highly upregulated and it plays a very important role of antioxidation, because HO-1 generates biliverdin, which being converted to bilirubin exhibits a very potent antioxidative effect, and hence antiapoptosis in tumors. Bilirubin 157-166 heme oxygenase 1 Homo sapiens 105-109 17671894-15 2007 Thus this oxidation therapy, by inhibiting this HO-1 dependent antioxidant (bilirubin) formation by ZnPP, and by enhancing ROS generation, is expected to offer a powerful therapeutic modality for future anticancer therapy. Bilirubin 76-85 heme oxygenase 1 Homo sapiens 48-52 17508911-7 2007 These novel findings provide a link between the increase in HO-1 activity, with its concurrent enhanced production of carbon monoxide (CO) and bilirubin, a decrease in infiltrated CD11c(+) dendritic cells and an increase in anti-apoptotic proteins, including RSK and BcL-xL, in the interdiction of the diabetic state. Bilirubin 143-152 heme oxygenase 1 Homo sapiens 60-64 17679649-10 2007 Thus, systemic expression of HO-1 suppresses NADPH oxidase activity by mechanisms at least partly mediated by the bile pigment bilirubin, thereby reducing oxidative stress. Bilirubin 127-136 heme oxygenase 1 Homo sapiens 29-33 18044280-1 2007 INTRODUCTION: Heme-Oxygenase-1 catalyzes hemoglobin into bilirubin, iron, and carbon monoxide, a well known vasodilator. Bilirubin 57-66 heme oxygenase 1 Homo sapiens 14-30 17678632-10 2007 Moreover, we found that the different products of HO-1, carbon monoxide and bilirubin, exerted anti-inflammatory effects that were additive or synergistic in HT-29 cells stimulated with TNF-alpha. Bilirubin 76-85 heme oxygenase 1 Homo sapiens 50-54 17416426-2 2007 Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life. Bilirubin 174-183 heme oxygenase 1 Homo sapiens 0-16 17416426-2 2007 Heme oxygenase-1 (HO-1) is a key enzyme that is integral to the temporal and spatial regulation of the host response and, together with its products carbon monoxide (CO) and bilirubin, is crucial for maintaining homeostasis and the preservation of function and life. Bilirubin 174-183 heme oxygenase 1 Homo sapiens 18-22 17392485-0 2007 Reduction of bilirubin by targeting human heme oxygenase-1 through siRNA. Bilirubin 13-22 heme oxygenase 1 Homo sapiens 42-58 17392485-3 2007 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme that generates bilirubin. Bilirubin 65-74 heme oxygenase 1 Homo sapiens 0-16 17392485-3 2007 Heme oxygenase-1 (HO-1) is a rate-limiting enzyme that generates bilirubin. Bilirubin 65-74 heme oxygenase 1 Homo sapiens 18-22 17245120-5 2007 This combined with experimental data showing anti-atherosclerotic properties of the enzyme heme oxygenase-1 encouraged us to hypothesize that bilirubin and its precursor biliverdin, would act to ameliorate components of atherosclerosis, in a manner similar to what has been shown with HO-1. Bilirubin 142-151 heme oxygenase 1 Homo sapiens 91-107 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. Bilirubin 262-271 heme oxygenase 1 Homo sapiens 57-73 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. Bilirubin 262-271 heme oxygenase 1 Homo sapiens 75-79 17325212-5 2007 Because bilirubin production plays a critical role during the neonatal period, the HO-1 promoter polymorphism may be an important genetic factor for the clinical outcome of neonatal hyperbilirubinemia. Bilirubin 8-17 heme oxygenase 1 Homo sapiens 83-87 16999951-6 2006 RESULTS: HO-1 expression and activity (5.3+/-2.1 nmol bilirubin/mg protein/h) were only present in ECs from advanced atherosclerotic lesions. Bilirubin 54-63 heme oxygenase 1 Homo sapiens 9-13 17020887-8 2006 Our results indicate that lipid peroxidation is a significant cause of NO-induced necrosis in human lung epithelial cells, and that the increased NO survival of L1 cells is due at least in part to decreased lipid peroxidation mediated by HO-1-generated biliverdin or bilirubin. Bilirubin 267-276 heme oxygenase 1 Homo sapiens 238-242 16943657-2 2006 HO-1 degradation of heme yields biliverdin, bilirubin, carbon monoxide and iron. Bilirubin 44-53 heme oxygenase 1 Homo sapiens 0-4 16982957-7 2006 Moreover, the heme oxygenase-1 end product bilirubin directly inhibited fully functional NADPH oxidase and seemed to interrupt the assembly and activation of the oxidase. Bilirubin 43-52 heme oxygenase 1 Homo sapiens 14-30 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. Bilirubin 128-137 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. Bilirubin 128-137 heme oxygenase 1 Homo sapiens 79-83 16678019-5 2006 Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation. Bilirubin 71-80 heme oxygenase 1 Homo sapiens 35-39 16678019-5 2006 Among the catabolic metabolites of HO-1, both carbon monoxide (CO) and bilirubin were directly involved in the protective role of HO-1 against cisplatin through inhibition of reactive oxygen species generation. Bilirubin 71-80 heme oxygenase 1 Homo sapiens 130-134 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. Bilirubin 185-194 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. Bilirubin 185-194 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). Bilirubin 199-208 heme oxygenase 1 Homo sapiens 75-79 16677090-5 2006 Of the various HSPs, heme oxygenase-I (HO-1), by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 127-136 heme oxygenase 1 Homo sapiens 39-43 16254033-5 2006 Donor treatment with bilirubin up-regulated mRNA expression of protective genes such as HO-1 and bcl-2 and suppressed proinflammatory and proapoptotic genes including monocyte chemoattractant protein-1 and caspase-3 and -8 in the islet grafts before transplantation. Bilirubin 21-30 heme oxygenase 1 Homo sapiens 88-92 16234431-12 2005 Moreover, serum levels of bilirubin, a metabolite of HO-1, were elevated in rheumatoid arthritis patients without bone damage, suggesting HO-1 affects bone loss in humans. Bilirubin 26-35 heme oxygenase 1 Homo sapiens 53-57 16697692-9 2006 This study shows an antiapoptotic effect of heme oxygenase-1 in colon cancer cells which could be mediated by the formation of bilirubin and biliverdin. Bilirubin 127-136 heme oxygenase 1 Homo sapiens 44-60 16373841-0 2005 Mechanisms of heme oxygenase-1-mediated cardiac and pulmonary vascular protection in chronic hypoxia: roles of carbon monoxide and bilirubin. Bilirubin 131-140 heme oxygenase 1 Homo sapiens 14-30 16234431-12 2005 Moreover, serum levels of bilirubin, a metabolite of HO-1, were elevated in rheumatoid arthritis patients without bone damage, suggesting HO-1 affects bone loss in humans. Bilirubin 26-35 heme oxygenase 1 Homo sapiens 138-142 16198234-2 2005 Heme oxygenase-1 (HO-1), implicated in a role in NO resistance, might confer its protective effect through the direct products biliverdin and CO or the secondary product bilirubin. Bilirubin 170-179 heme oxygenase 1 Homo sapiens 0-16 16198234-2 2005 Heme oxygenase-1 (HO-1), implicated in a role in NO resistance, might confer its protective effect through the direct products biliverdin and CO or the secondary product bilirubin. Bilirubin 170-179 heme oxygenase 1 Homo sapiens 18-22 16249618-2 2005 Heme oxygenase-1 (HO-1) catalyzes heme breakdown, eventually generating bilirubin, iron and carbon monoxide. Bilirubin 72-81 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. Bilirubin 72-81 heme oxygenase 1 Homo sapiens 18-22 16020495-2 2005 Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous antioxidant bilirubin and carbon monoxide, both of which exert antiinflammatory and antiproliferative effects. Bilirubin 84-93 heme oxygenase 1 Homo sapiens 0-16 16309585-2 2005 HO-1 catalyzes the conversion of heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Bilirubin 122-131 heme oxygenase 1 Homo sapiens 0-4 16309585-3 2005 The beneficial effects of HO-1 induction include decreasing pro-oxidants (heme), increasing anti-oxidants (biliverdin and bilirubin), and producing a vasodilator with anti-apoptotic and anti-inflammatory properties (CO). Bilirubin 122-131 heme oxygenase 1 Homo sapiens 26-30 15901614-4 2005 The protective effects of heme oxygenase-1 and products of its enzymatic activity, including carbon monoxide, biliverdin and bilirubin, and ferritin, have opened the door to potential therapeutic and disease-monitoring possibilities that one day may be applicable to pulmonary medicine. Bilirubin 125-134 heme oxygenase 1 Homo sapiens 26-42 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. Bilirubin 179-188 heme oxygenase 1 Homo sapiens 33-37 16020495-2 2005 Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous antioxidant bilirubin and carbon monoxide, both of which exert antiinflammatory and antiproliferative effects. Bilirubin 84-93 heme oxygenase 1 Homo sapiens 18-22 15911218-7 2005 When added exogenously to the cells at low micromolar concentrations, the HO-1 metabolite, bilirubin, virtually abolished NADPH-dependent oxidative stress. Bilirubin 91-100 heme oxygenase 1 Homo sapiens 74-78 16146339-5 2005 The antioxidant effect of L-methionine was mimicked by the HO-1 product bilirubin, which suppressed free radical formation almost completely. Bilirubin 72-81 heme oxygenase 1 Homo sapiens 59-63 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. Bilirubin 92-101 heme oxygenase 1 Homo sapiens 12-28 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. Bilirubin 92-101 heme oxygenase 1 Homo sapiens 30-34 15896810-13 2005 Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 246-255 heme oxygenase 1 Homo sapiens 24-29 15896810-13 2005 Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 246-255 heme oxygenase 1 Homo sapiens 63-67 15896810-13 2005 Among the various HSPs, HSP32, also known as heme oxygenase I (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 246-255 heme oxygenase 1 Homo sapiens 149-153 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. Bilirubin 165-174 heme oxygenase 1 Homo sapiens 15-31 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. Bilirubin 165-174 heme oxygenase 1 Homo sapiens 33-37 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. Bilirubin 199-208 heme oxygenase 1 Homo sapiens 0-16 15890016-1 2005 Heme oxygenase isoforms (HO-1/HO-2) catalyze the conversion of heme to carbon monoxide (CO) and bilirubin. Bilirubin 96-105 heme oxygenase 1 Homo sapiens 0-34 15869055-2 2005 These products have important physiologic effects: bilirubin is a potent antioxidant that can act against ischemia/reperfusion injury; there is a negative correlation between the content of HO-1 and the incidence of coronary heart disease (CHD). Bilirubin 51-60 heme oxygenase 1 Homo sapiens 190-194 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. Bilirubin 148-157 heme oxygenase 1 Homo sapiens 39-43 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. Bilirubin 199-208 heme oxygenase 1 Homo sapiens 18-22 15541371-6 2004 The HO-1 metabolite bilirubin, when added exogenously to the cells, virtually abolished NADPH-dependent oxidative stress. Bilirubin 20-29 heme oxygenase 1 Homo sapiens 4-8 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. Bilirubin 181-190 heme oxygenase 1 Homo sapiens 0-30 14977878-1 2004 Biliverdin, a product of heme oxygenase-1 (HO-1) enzymatic action, is converted into bilirubin, which has been considered a waste product in the past. Bilirubin 85-94 heme oxygenase 1 Homo sapiens 25-41 15530192-12 2004 Bilirubin, but not carboxyhemoglobin, correlated with heme oxygenase-1 expression (p = .0013). Bilirubin 0-9 heme oxygenase 1 Homo sapiens 54-70 15530192-14 2004 Heme oxygenase-1 expression correlated with serum bilirubin levels. Bilirubin 50-59 heme oxygenase 1 Homo sapiens 0-16 15530192-15 2004 The increase in heme oxygenase-1 expression may add to the understanding of the increase in serum bilirubin observed in patients with SIRS/sepsis. Bilirubin 98-107 heme oxygenase 1 Homo sapiens 16-32 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. Bilirubin 141-150 heme oxygenase 1 Homo sapiens 6-22 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. Bilirubin 141-150 heme oxygenase 1 Homo sapiens 24-29 15602829-4 2004 HO-1 activity was indicated by bilirubin and Fe2+ formation. Bilirubin 31-40 heme oxygenase 1 Homo sapiens 0-4 15602829-7 2004 We further observed a time-dependent increase of HO-1 mRNA expression using 100 mmol/L ethanol starting 30 minutes after ethanol exposure, reaching its maximum between 3 h and 9 h. Being similar increased protein expression started to what had been demonstrated with the mRNA level, at 6 h after ethanol exposure, and kept continuous elevated over 18 h. In addition, we found that ethanol exposure to hepatocytes markedly increased HO-1 enzyme activity in a time-dependent manner measured as bilirubin and Fe2+ formation in human hepatocytes. Bilirubin 492-501 heme oxygenase 1 Homo sapiens 49-53 15341181-8 2004 In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 237-246 heme oxygenase 1 Homo sapiens 15-20 15341181-8 2004 In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 237-246 heme oxygenase 1 Homo sapiens 36-52 15341181-8 2004 In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 237-246 heme oxygenase 1 Homo sapiens 54-58 15341181-8 2004 In particular, HSP32, also known as heme oxygenase-1 (HO-1), has received considerable attention, as it has been recently demonstrated that HO-1 induction, by generating the vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, could represent a protective system potentially active against brain oxidative injury. Bilirubin 237-246 heme oxygenase 1 Homo sapiens 140-144 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. Bilirubin 72-81 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. Bilirubin 72-81 heme oxygenase 1 Homo sapiens 30-34 15531134-3 2004 The inducible enzyme, heme oxygenase-1 metabolizes and thus detoxifies free heme to the powerful endogenous antioxidants biliverdin and bilirubin therefore enhancing neuroprotection. Bilirubin 136-145 heme oxygenase 1 Homo sapiens 22-38 15233805-3 2004 HO-1 catalyzes heme breakdown to release iron, carbon monoxide, and biliverdin, which is reduced to bilirubin, a potent radical scavenger. Bilirubin 100-109 heme oxygenase 1 Homo sapiens 0-4 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. Bilirubin 132-141 heme oxygenase 1 Homo sapiens 0-16 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. Bilirubin 132-141 heme oxygenase 1 Homo sapiens 18-22 15004156-8 2004 Bilirubin and/or Fe2+ chelation mimicked the effects of HO-1, whereas biliverdin or carbon monoxide did not. Bilirubin 0-9 heme oxygenase 1 Homo sapiens 56-60 15004156-10 2004 This effect of HO-1 is mediated by bilirubin and/or by a decrease of free intracellular Fe2+ but probably not by biliverdin or carbon monoxide. Bilirubin 35-44 heme oxygenase 1 Homo sapiens 15-19 14733911-5 2004 A protective effect similar to L-alanine was observed when preincubating the cells with iron-free apoferritin or the antioxidant HO-1 product, bilirubin. Bilirubin 143-152 heme oxygenase 1 Homo sapiens 129-133 12927812-3 2003 HO-1 induction was accompanied by a marked increase in catalytic activity of the enzyme as reflected by enhanced formation of both carbon monoxide and bilirubin. Bilirubin 151-160 heme oxygenase 1 Homo sapiens 0-4 14968347-7 2004 Additionally, PETriN enhanced the enzymatic activity of HO-1 measured as formation of the HO-1 metabolites bilirubin (Figure 3) and carbon monoxide (Figure 4) in lysates from endothelial cells. Bilirubin 107-116 heme oxygenase 1 Homo sapiens 56-60 14968347-7 2004 Additionally, PETriN enhanced the enzymatic activity of HO-1 measured as formation of the HO-1 metabolites bilirubin (Figure 3) and carbon monoxide (Figure 4) in lysates from endothelial cells. Bilirubin 107-116 heme oxygenase 1 Homo sapiens 90-94 15777021-6 2004 The existence of a constitutive haem oxygenase (HO-2), mainly present in the vasculature and nervous system, and an inducible haem oxygenase (HO-1), which is highly expressed during stress conditions in all tissues, also suggests that cells have evolved a fine control of this enzymic pathway to ultimately regulate haem consumption and to ensure production of CO, biliverdin/bilirubin and iron during physiological and pathophysiological situations. Bilirubin 376-385 heme oxygenase 1 Homo sapiens 142-146 14691581-0 2004 A microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with increased bilirubin and HDL levels but not with coronary artery disease. Bilirubin 97-106 heme oxygenase 1 Homo sapiens 37-53 14691581-1 2004 Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous anti-oxidant bilirubin which exerts beneficial effects against arteriosclerosis. Bilirubin 85-94 heme oxygenase 1 Homo sapiens 0-16 14691581-1 2004 Heme oxygenase 1 (HO-1) is involved in the generation of the endogenous anti-oxidant bilirubin which exerts beneficial effects against arteriosclerosis. Bilirubin 85-94 heme oxygenase 1 Homo sapiens 18-22 12927819-9 2003 Upregulation of HO-1 ensures the generation of bilirubin and carbon monoxide (CO) in G(0)/G(1) phase to counteract Ang II-mediated oxidative DNA damage. Bilirubin 47-56 heme oxygenase 1 Homo sapiens 16-20 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. Bilirubin 132-141 heme oxygenase 1 Homo sapiens 192-196 13678532-0 2003 Induction of heme oxygenase-1 in monocytes suppresses angiotensin II-elicited chemotactic activity through inhibition of CCR2: role of bilirubin and carbon monoxide generated by the enzyme. Bilirubin 135-144 heme oxygenase 1 Homo sapiens 13-29 13678532-7 2003 Exogenously applied bilirubin and carbon monoxide mimicked the inhibitory effect of HO-1 on the chemotactic response. Bilirubin 20-29 heme oxygenase 1 Homo sapiens 84-88 12511571-1 2003 Heme oxygenase 1 (HO-1) catalyzes heme breakdown, eventually releasing iron, carbon monoxide, and bilirubin IXalpha. Bilirubin 98-107 heme oxygenase 1 Homo sapiens 0-16 12891549-10 2003 These effects were ascribed to bilirubin, one of the products of HO-1-mediated heme degradation. Bilirubin 31-40 heme oxygenase 1 Homo sapiens 65-69 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. Bilirubin 134-143 heme oxygenase 1 Homo sapiens 69-85 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. Bilirubin 134-143 heme oxygenase 1 Homo sapiens 87-91 12622689-1 2003 NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin. Bilirubin 141-150 heme oxygenase 1 Homo sapiens 34-50 12622689-1 2003 NO potently up-regulates vascular haem oxygenase-1 (HO-1), an inducible defensive protein that degrades haem to CO, iron and the antioxidant bilirubin. Bilirubin 141-150 heme oxygenase 1 Homo sapiens 52-56 12622689-5 2003 A role for haem metabolites in modulating HO-1 expression by NO was assessed by exposing cells to SNAP, SNP or DETA/NO in medium derived from cells treated with haemin, which contained increased bilirubin levels. Bilirubin 195-204 heme oxygenase 1 Homo sapiens 42-46 12709581-6 2003 Elevation of HO-1 protein was accompanied by a marked increase in catalytic activity of the enzyme as reflected by enhanced formation of both carbon monoxide and the endogenous antioxidant, bilirubin. Bilirubin 190-199 heme oxygenase 1 Homo sapiens 13-17 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. Bilirubin 233-242 heme oxygenase 1 Homo sapiens 91-107 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. Bilirubin 233-242 heme oxygenase 1 Homo sapiens 109-113 12709592-8 2003 HO-1 activity was determined by the ability of the enzyme to generate bilirubin from hemin. Bilirubin 70-79 heme oxygenase 1 Homo sapiens 0-4 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). Bilirubin 124-133 heme oxygenase 1 Homo sapiens 0-21 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. Bilirubin 119-128 heme oxygenase 1 Homo sapiens 22-26 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. Bilirubin 168-177 heme oxygenase 1 Homo sapiens 0-3 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. Bilirubin 135-144 heme oxygenase 1 Homo sapiens 0-4 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. Bilirubin 152-161 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. Bilirubin 152-161 heme oxygenase 1 Homo sapiens 23-28 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). Bilirubin 143-160 heme oxygenase 1 Homo sapiens 0-4 14753445-0 2003 Transient elevation of serum bilirubin (a heme oxygenase-1 metabolite) level in hemorrhagic stroke: bilirubin is a marker of oxidant stress. Bilirubin 29-38 heme oxygenase 1 Homo sapiens 42-58 14753445-0 2003 Transient elevation of serum bilirubin (a heme oxygenase-1 metabolite) level in hemorrhagic stroke: bilirubin is a marker of oxidant stress. Bilirubin 100-109 heme oxygenase 1 Homo sapiens 42-58 14753445-2 2003 The production of Bil reflects heme oxygenase-1 expression in response to oxidative stress in various diseases. Bilirubin 18-21 heme oxygenase 1 Homo sapiens 31-47 12230871-4 2002 HO-1 cleaves the porphyrin macrocycle of heme at the expense of molecular oxygen to release a linear tetrapyrrole biliverdin, carbon monoxide, and ferrous iron; biliverdin is rapidly reduced to bilirubin. Bilirubin 194-203 heme oxygenase 1 Homo sapiens 0-4 12230873-2 2002 The importance of this protein in physiology and disease is underlined by the versatility of HO-1 inducers and the functional role attributed to HO-1 products (carbon monoxide and bilirubin) in conditions that are associated with moderate or severe cellular stress. Bilirubin 180-189 heme oxygenase 1 Homo sapiens 145-149 12006180-4 2002 Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin. Bilirubin 154-163 heme oxygenase 1 Homo sapiens 62-78 12006180-4 2002 Hypoxia transiently increases the transcriptional rate of the heme oxygenase-1 (HO-1) gene, resulting in increased production of carbon monoxide (CO) and bilirubin. Bilirubin 154-163 heme oxygenase 1 Homo sapiens 80-84 11572959-7 2001 Macrophage-inducible NOS generates NO to kill other cells, whereas HO1 generates bilirubin to exert antioxidant cytoprotective effects and also provides cytoprotection by facilitating iron extrusion from cells. Bilirubin 81-90 heme oxygenase 1 Homo sapiens 67-70 11668058-1 2001 Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron. Bilirubin 88-97 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. Bilirubin 88-97 heme oxygenase 1 Homo sapiens 18-22 11668058-3 2001 Here, we investigated the effect of severe hypoxia and reoxygenation on HO-1 expression in cardiomyocytes and determined whether HO-1 and its product, bilirubin, have a protective role against reoxygenation damage. Bilirubin 151-160 heme oxygenase 1 Homo sapiens 129-133 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. Bilirubin 37-46 heme oxygenase 1 Homo sapiens 32-36 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. Bilirubin 37-46 heme oxygenase 1 Homo sapiens 216-220 11854317-5 2002 CdCl(2)-elicited HO-1 occurred mostly in Leydig cells and coincided with CO generation, as judged by bilirubin-IXalpha immunoreactivity. Bilirubin 101-110 heme oxygenase 1 Homo sapiens 17-21 9276739-10 1997 These results suggest that HO-1 induced by mildly oxidized LDL may protect against the induction of inflammatory responses in artery wall cells through the production of the antioxidants biliverdin and bilirubin. Bilirubin 202-211 heme oxygenase 1 Homo sapiens 27-31 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. Bilirubin 41-50 heme oxygenase 1 Homo sapiens 0-4 11247059-0 2001 Increase in bilirubin levels of patients with obstructive sleep apnea in the morning--a possible explanation of induced heme oxygenase-1. Bilirubin 12-21 heme oxygenase 1 Homo sapiens 120-136 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. Bilirubin 140-149 heme oxygenase 1 Homo sapiens 36-52 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. Bilirubin 140-149 heme oxygenase 1 Homo sapiens 54-58 10839994-2 2000 In several circumstances, this cytoprotective effect has been attributed to increased generation of the antioxidant bilirubin during haem degradation by HO-1. Bilirubin 116-125 heme oxygenase 1 Homo sapiens 153-157 10839994-3 2000 However, a direct implication for HO-1-derived bilirubin in protection against oxidative stress remains to be established. Bilirubin 47-56 heme oxygenase 1 Homo sapiens 34-38 10839994-5 2000 We found that hemin-mediated increase in HO-1 protein expression and haem oxygenase activity is associated with augmented bilirubin levels. Bilirubin 122-131 heme oxygenase 1 Homo sapiens 41-45 10839994-8 2000 Interestingly, this protective effect was manifest only when cells were actively producing bilirubin as a consequence of increased haem availability and utilization by HO-1. Bilirubin 91-100 heme oxygenase 1 Homo sapiens 168-172 10839994-11 2000 Our findings provide direct evidence that bilirubin generated after up-regulation of the HO-1 pathway is cytoprotective against oxidative stress. Bilirubin 42-51 heme oxygenase 1 Homo sapiens 89-93 10773020-10 2000 The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes. Bilirubin 264-273 heme oxygenase 1 Homo sapiens 16-20 10773020-10 2000 The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes. Bilirubin 264-273 heme oxygenase 1 Homo sapiens 62-66 10773020-10 2000 The increase in HO-1 activity after adenovirus-mediated human HO-1 gene transfer may prove useful as a means of selectively increasing enzyme activity in a specific organ and regulating homeostasis by modulation of vasoactive molecules such as carbon monoxide and bilirubin and, in addition, providing a means of delivering the human HO-1 gene for experimental purposes. Bilirubin 264-273 heme oxygenase 1 Homo sapiens 62-66 10460761-9 1999 These findings suggest that HO-1 induction provides protection against H(2)O(2)-induced injury of the cultured human airway epithelial cells in part via the HO-bilirubin pathway. Bilirubin 160-169 heme oxygenase 1 Homo sapiens 28-32 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. Bilirubin 163-172 heme oxygenase 1 Homo sapiens 18-22 10193374-3 1998 HO-1 catabolises heme to bilirubin, free iron and carbon monoxide (CO). Bilirubin 25-34 heme oxygenase 1 Homo sapiens 0-4 9828853-3 1998 HO-1 catabolises heme to bilirubin, free iron, and carbon monoxide (CO). Bilirubin 25-34 heme oxygenase 1 Homo sapiens 0-4 11247059-12 2001 CONCLUSIONS: The increase in bilirubin level by HO-1 might protect OSAHS patients from disorders related to hypoxemia. Bilirubin 29-38 heme oxygenase 1 Homo sapiens 48-52 9407320-2 1998 Overexpression of HO-1 in endothelial cells (EC) might, therefore, protect against oxidative stress produced under these pathological conditions, by generation of CO, a vasodilator, and bilirubin, which has antioxidant properties that enhance blood vessel formation to counteract hypoxia-induced injury. Bilirubin 186-195 heme oxygenase 1 Homo sapiens 18-22 33805292-4 2021 We systematically reviewed published evidence on HMOX1 polymorphisms in perinatal diseases and clarified their possible significant contribution to neonatal jaundice development, presumably due to their direct effect of inducing HO enzymatic activity in the bilirubin-producing pathway. Bilirubin 258-267 heme oxygenase 1 Homo sapiens 49-54 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Bilirubin 222-231 heme oxygenase 1 Homo sapiens 17-21 8679227-14 1996 The magnitude of HO-1 induction after oxidative stress and the wide distribution of this enzyme in systemic tissues coupled with the intriguing biological activities of the catalytic byproducts, carbon monoxide, iron, and bilirubin, makes HO-1 a highly attractive and interesting candidate stress-response protein which may play key role(s) in mediating protection against oxidant-mediated lung injury. Bilirubin 222-231 heme oxygenase 1 Homo sapiens 239-243 7525927-2 1994 Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin. Bilirubin 217-226 heme oxygenase 1 Homo sapiens 30-34 7525927-2 1994 Heme oxygenase (HO) isozymes, HO-1 (HSP32) and HO-2, catalyze the rate limiting step in the only known pathway in eukaryotes for the generation of the potential cellular message, carbon monoxide, and the antioxidant, bilirubin. Bilirubin 217-226 heme oxygenase 1 Homo sapiens 36-41 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. Bilirubin 163-172 heme oxygenase 1 Homo sapiens 15-31 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. Bilirubin 163-172 heme oxygenase 1 Homo sapiens 33-37 34841438-1 2022 Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin. Bilirubin 166-175 heme oxygenase 1 Homo sapiens 0-16 34841438-1 2022 Heme oxygenase-1 (HO-1) is an inducible cytoprotective enzyme that degrades heme into free iron, carbon monoxide and biliverdin, which is then rapidly converted into bilirubin. Bilirubin 166-175 heme oxygenase 1 Homo sapiens 18-22 34928467-3 2021 This study aimed to investigate the predictive value of the total bilirubin level, a marker of heme oxygenase-1 enzyme activity, in determining myocarditis in patients with COVID-19. Bilirubin 66-75 heme oxygenase 1 Homo sapiens 95-111 34943103-2 2021 The aim of our study was to assess the role of bilirubin, and the heme oxygenase 1 (HMOX1) and bilirubin UDP-glucuronosyl transferase (UGT1A1) promoter gene variants, which are involved in bilirubin homeostasis, in the NAFLD development in adult patients. Bilirubin 189-198 heme oxygenase 1 Homo sapiens 66-82 34943103-2 2021 The aim of our study was to assess the role of bilirubin, and the heme oxygenase 1 (HMOX1) and bilirubin UDP-glucuronosyl transferase (UGT1A1) promoter gene variants, which are involved in bilirubin homeostasis, in the NAFLD development in adult patients. Bilirubin 189-198 heme oxygenase 1 Homo sapiens 84-89 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. Bilirubin 174-183 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. Bilirubin 174-183 heme oxygenase 1 Homo sapiens 124-128