PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32408627-2 2020 Carbon monoxide (CO) produced by heme oxygenase (HMOX) activity or released from its donor, tricarbonyldichlororuthenium (II) dimer (CORM-2) was reported to protect gastric mucosa against acid-dependent non-steroidal anti-inflammatory drug-induced damage. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 33-47 34194603-0 2021 Carbon Monoxide Releasing Molecule-3 Enhances Heme Oxygenase-1 Induction via ROS-Dependent FoxO1 and Nrf2 in Brain Astrocytes. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 46-62 34194603-1 2021 Carbon monoxide releasing molecule-3 (CORM-3) has been shown to protect inflammatory diseases via the upregulation of heme oxygenases-1 (HO-1). Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 118-135 34194603-1 2021 Carbon monoxide releasing molecule-3 (CORM-3) has been shown to protect inflammatory diseases via the upregulation of heme oxygenases-1 (HO-1). Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 137-141 34945812-5 2021 In the mouse sarcoma S180 solid tumor model and the rat hepatoma AH136B ascitic tumor model, HO-1 expression in the tumor, as indicated by the end product of HO-1 activation, i.e., carbon monoxide, gradually increased along with tumor growth. Carbon Monoxide 181-196 heme oxygenase 1 Rattus norvegicus 93-97 34945812-5 2021 In the mouse sarcoma S180 solid tumor model and the rat hepatoma AH136B ascitic tumor model, HO-1 expression in the tumor, as indicated by the end product of HO-1 activation, i.e., carbon monoxide, gradually increased along with tumor growth. Carbon Monoxide 181-196 heme oxygenase 1 Rattus norvegicus 158-162 3525562-18 1986 HO-1 and HO-2 had similar requirements for cofactor and flavoprotein reductase and were inhibited by heme-ligands (CO, KCN, NaN3). Carbon Monoxide 115-117 heme oxygenase 1 Rattus norvegicus 0-4 32760814-0 2020 The protective role of localized nitric oxide production during inflammation may be mediated by the heme oxygenase-1/carbon monoxide pathway. Carbon Monoxide 117-132 heme oxygenase 1 Rattus norvegicus 100-116 33659548-1 2020 Heme oxygenase-1 (HO-1) is a stress responsive enzyme that metabolizes heme and releases free iron, carbon monoxide (CO), and biliverdin (BV), which rapidly undergoes conversion to bilirubin (BL). Carbon Monoxide 100-115 heme oxygenase 1 Rattus norvegicus 0-16 33659548-1 2020 Heme oxygenase-1 (HO-1) is a stress responsive enzyme that metabolizes heme and releases free iron, carbon monoxide (CO), and biliverdin (BV), which rapidly undergoes conversion to bilirubin (BL). Carbon Monoxide 100-115 heme oxygenase 1 Rattus norvegicus 18-22 33659548-1 2020 Heme oxygenase-1 (HO-1) is a stress responsive enzyme that metabolizes heme and releases free iron, carbon monoxide (CO), and biliverdin (BV), which rapidly undergoes conversion to bilirubin (BL). Carbon Monoxide 117-119 heme oxygenase 1 Rattus norvegicus 0-16 33659548-1 2020 Heme oxygenase-1 (HO-1) is a stress responsive enzyme that metabolizes heme and releases free iron, carbon monoxide (CO), and biliverdin (BV), which rapidly undergoes conversion to bilirubin (BL). Carbon Monoxide 117-119 heme oxygenase 1 Rattus norvegicus 18-22 32408627-2 2020 Carbon monoxide (CO) produced by heme oxygenase (HMOX) activity or released from its donor, tricarbonyldichlororuthenium (II) dimer (CORM-2) was reported to protect gastric mucosa against acid-dependent non-steroidal anti-inflammatory drug-induced damage. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 49-53 32408627-2 2020 Carbon monoxide (CO) produced by heme oxygenase (HMOX) activity or released from its donor, tricarbonyldichlororuthenium (II) dimer (CORM-2) was reported to protect gastric mucosa against acid-dependent non-steroidal anti-inflammatory drug-induced damage. Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 33-47 32408627-2 2020 Carbon monoxide (CO) produced by heme oxygenase (HMOX) activity or released from its donor, tricarbonyldichlororuthenium (II) dimer (CORM-2) was reported to protect gastric mucosa against acid-dependent non-steroidal anti-inflammatory drug-induced damage. Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 49-53 30274172-0 2018 Alterations in Gastric Mucosal Expression of Calcitonin Gene-Related Peptides, Vanilloid Receptors, and Heme Oxygenase-1 Mediate Gastroprotective Action of Carbon Monoxide against Ethanol-Induced Gastric Mucosal Lesions. Carbon Monoxide 156-171 heme oxygenase 1 Rattus norvegicus 104-120 31037602-1 2019 Carbon monoxide (CO) presents anti-inflammatory and antioxidant activities as a new gaseous neuromessenger produced by heme oxygenase-1 (HO-1) in the body. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 119-135 31037602-1 2019 Carbon monoxide (CO) presents anti-inflammatory and antioxidant activities as a new gaseous neuromessenger produced by heme oxygenase-1 (HO-1) in the body. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 137-141 31037602-1 2019 Carbon monoxide (CO) presents anti-inflammatory and antioxidant activities as a new gaseous neuromessenger produced by heme oxygenase-1 (HO-1) in the body. Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 119-135 31037602-1 2019 Carbon monoxide (CO) presents anti-inflammatory and antioxidant activities as a new gaseous neuromessenger produced by heme oxygenase-1 (HO-1) in the body. Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 137-141 29519277-1 2018 OBJECTIVE: To investigate the effects of heme oxygenase-1/carbon monoxide (HO-1/CO) pathway on mitochondrial fusion in rat alveolar epithelial type II cells (AEC II) stimulated by lipopolysaccharide (LPS). Carbon Monoxide 58-73 heme oxygenase 1 Rattus norvegicus 75-79 29362850-0 2018 Heme oxygenase-1/biliverdin/carbon monoxide pathway downregulates hypernociception in rats by a mechanism dependent on cGMP/ATP-sensitive K+ channels. Carbon Monoxide 28-43 heme oxygenase 1 Rattus norvegicus 0-16 29055786-1 2018 Carbon monoxide (CO), produced by heme oxygenase-1 (HO-1), is an endogenous paracrine factor involved in the regulation of cardiovascular structure and function. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 34-50 29055786-1 2018 Carbon monoxide (CO), produced by heme oxygenase-1 (HO-1), is an endogenous paracrine factor involved in the regulation of cardiovascular structure and function. Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 34-50 29154837-7 2018 In primary mesencephalic cultures, heme oxygenase-1, upregulated by TPNA10168 in astrocytes, provided protection of dopaminergic neurons via a guanylate cyclase/protein kinase G signaling pathway via carbon monoxide. Carbon Monoxide 200-215 heme oxygenase 1 Rattus norvegicus 35-51 28088559-4 2017 Here, we report that the carbon monoxide (CO) producing enzymes HO-1 and HO-2 are present in the MPOA and are differentially influenced by sexual experience in a manner similar to that previously reported for NO enzymes. Carbon Monoxide 25-40 heme oxygenase 1 Rattus norvegicus 64-77 28472389-4 2017 We have reported that induction of the carbon monoxide (CO) producing protein heme oxygenase-1 restored angiogenic imbalance and reduced blood pressure in a rat model of placental ischemia, and that CO blocks hypoxia-induced sFlt-1 production from placental tissue in vitro. Carbon Monoxide 39-54 heme oxygenase 1 Rattus norvegicus 78-94 28472389-4 2017 We have reported that induction of the carbon monoxide (CO) producing protein heme oxygenase-1 restored angiogenic imbalance and reduced blood pressure in a rat model of placental ischemia, and that CO blocks hypoxia-induced sFlt-1 production from placental tissue in vitro. Carbon Monoxide 56-58 heme oxygenase 1 Rattus norvegicus 78-94 29209167-0 2017 Heme Oxygenase-1 Induction by Carbon Monoxide Releasing Molecule-3 Suppresses Interleukin-1beta-Mediated Neuroinflammation. Carbon Monoxide 30-45 heme oxygenase 1 Rattus norvegicus 0-16 29209167-2 2017 In cellular anti-oxidant systems, heme oxygenase-1 (HO-1) is an oxidative-sensor protein induced by ROS generation or carbon monoxide (CO) release. Carbon Monoxide 118-133 heme oxygenase 1 Rattus norvegicus 34-50 29209167-2 2017 In cellular anti-oxidant systems, heme oxygenase-1 (HO-1) is an oxidative-sensor protein induced by ROS generation or carbon monoxide (CO) release. Carbon Monoxide 118-133 heme oxygenase 1 Rattus norvegicus 52-56 29209167-2 2017 In cellular anti-oxidant systems, heme oxygenase-1 (HO-1) is an oxidative-sensor protein induced by ROS generation or carbon monoxide (CO) release. Carbon Monoxide 135-137 heme oxygenase 1 Rattus norvegicus 34-50 29209167-2 2017 In cellular anti-oxidant systems, heme oxygenase-1 (HO-1) is an oxidative-sensor protein induced by ROS generation or carbon monoxide (CO) release. Carbon Monoxide 135-137 heme oxygenase 1 Rattus norvegicus 52-56 28088559-4 2017 Here, we report that the carbon monoxide (CO) producing enzymes HO-1 and HO-2 are present in the MPOA and are differentially influenced by sexual experience in a manner similar to that previously reported for NO enzymes. Carbon Monoxide 42-44 heme oxygenase 1 Rattus norvegicus 64-77 27575447-0 2016 Heme Oxygenase-1/Carbon Monoxide-regulated Mitochondrial Dynamic Equilibrium Contributes to the Attenuation of Endotoxin-induced Acute Lung Injury in Rats and in Lipopolysaccharide-activated Macrophages. Carbon Monoxide 17-32 heme oxygenase 1 Rattus norvegicus 0-16 27575447-12 2016 CONCLUSIONS: The HO-1/carbon monoxide system modulated the imbalance of the dynamic mitochondrial fusion/fission process evoked by lipopolysaccharide and efficiently ameliorated endotoxin-induced lung injury in vivo and in vitro. Carbon Monoxide 22-37 heme oxygenase 1 Rattus norvegicus 17-21 27021659-9 2016 The Hb promotes HO-1 expression in KCs, thereby produces iron, bilirubin, and carbon monoxide (CO). Carbon Monoxide 78-93 heme oxygenase 1 Rattus norvegicus 16-20 27486402-4 2016 Heme oxygenase-1 (HO-1) forms an important protective mechanism by breaking down heme into the strong anti-oxidants biliverdin/bilirubin and the signaling molecule carbon monoxide. Carbon Monoxide 164-179 heme oxygenase 1 Rattus norvegicus 0-16 27486402-4 2016 Heme oxygenase-1 (HO-1) forms an important protective mechanism by breaking down heme into the strong anti-oxidants biliverdin/bilirubin and the signaling molecule carbon monoxide. Carbon Monoxide 164-179 heme oxygenase 1 Rattus norvegicus 18-22 27021659-9 2016 The Hb promotes HO-1 expression in KCs, thereby produces iron, bilirubin, and carbon monoxide (CO). Carbon Monoxide 95-97 heme oxygenase 1 Rattus norvegicus 16-20 25348283-14 2016 CO poisoning could activate HO-1/Nrf-2 pathway, start oxidative stress response. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 28-32 25148934-1 2015 Upregulation of heme oxygenase 1 (HO-1) by carbon monoxide (CO) delivered by CO-releasing molecules (CORMs) may be utilized as a therapeutic intervention for neurodegenerative diseases. Carbon Monoxide 43-58 heme oxygenase 1 Rattus norvegicus 16-32 25148934-0 2015 CO Induces Nrf2-Dependent Heme Oxygenase-1 Transcription by Cooperating with Sp1 and c-Jun in Rat Brain Astrocytes. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 26-42 27432233-7 2016 Endogenous CO concentration in the liver of control rats remained very low but was elevated significantly after LPS treatment (6, 12, 24 hr), which was in accordance with the changes of HO-1. Carbon Monoxide 11-13 heme oxygenase 1 Rattus norvegicus 186-190 26392811-3 2015 Heme oxygenase-1 (HO-1)-a stress-responsive enzyme that catabolizes heme into iron, carbon monoxide, and biliverdin-has an important role in the neuroprotective mechanism against ischemic stroke. Carbon Monoxide 84-99 heme oxygenase 1 Rattus norvegicus 0-16 26392811-3 2015 Heme oxygenase-1 (HO-1)-a stress-responsive enzyme that catabolizes heme into iron, carbon monoxide, and biliverdin-has an important role in the neuroprotective mechanism against ischemic stroke. Carbon Monoxide 84-99 heme oxygenase 1 Rattus norvegicus 18-22 25148934-1 2015 Upregulation of heme oxygenase 1 (HO-1) by carbon monoxide (CO) delivered by CO-releasing molecules (CORMs) may be utilized as a therapeutic intervention for neurodegenerative diseases. Carbon Monoxide 43-58 heme oxygenase 1 Rattus norvegicus 34-38 25148934-1 2015 Upregulation of heme oxygenase 1 (HO-1) by carbon monoxide (CO) delivered by CO-releasing molecules (CORMs) may be utilized as a therapeutic intervention for neurodegenerative diseases. Carbon Monoxide 60-62 heme oxygenase 1 Rattus norvegicus 16-32 25148934-1 2015 Upregulation of heme oxygenase 1 (HO-1) by carbon monoxide (CO) delivered by CO-releasing molecules (CORMs) may be utilized as a therapeutic intervention for neurodegenerative diseases. Carbon Monoxide 60-62 heme oxygenase 1 Rattus norvegicus 34-38 25715797-8 2015 Both the Hmox1 inducer cobalt protoporphyrin and a compound that releases the Hmox1 product carbon monoxide (CO) attenuated microglial death produced by LPS/IL-13. Carbon Monoxide 92-107 heme oxygenase 1 Rattus norvegicus 78-83 25715797-8 2015 Both the Hmox1 inducer cobalt protoporphyrin and a compound that releases the Hmox1 product carbon monoxide (CO) attenuated microglial death produced by LPS/IL-13. Carbon Monoxide 109-111 heme oxygenase 1 Rattus norvegicus 9-14 25715797-8 2015 Both the Hmox1 inducer cobalt protoporphyrin and a compound that releases the Hmox1 product carbon monoxide (CO) attenuated microglial death produced by LPS/IL-13. Carbon Monoxide 109-111 heme oxygenase 1 Rattus norvegicus 78-83 25501830-11 2014 Our findings indicate that HO-1 protects against Abeta toxicity via production of CO. Carbon Monoxide 82-84 heme oxygenase 1 Rattus norvegicus 27-31 24117853-6 2014 Thus, the present study was performed to evaluate the hypothesis that RIIH produces hypertension via induction of heme oxygenase (HO)-1, promoting a significant increase in endogenous carbon monoxide (CO). Carbon Monoxide 184-199 heme oxygenase 1 Rattus norvegicus 114-135 24148277-1 2014 Carbon monoxide (CO), a product of heme oxygenase (HMOX), has many beneficial biological functions and is a promising therapeutic agent for many pathological conditions. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 35-49 24148277-1 2014 Carbon monoxide (CO), a product of heme oxygenase (HMOX), has many beneficial biological functions and is a promising therapeutic agent for many pathological conditions. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 51-55 24148277-1 2014 Carbon monoxide (CO), a product of heme oxygenase (HMOX), has many beneficial biological functions and is a promising therapeutic agent for many pathological conditions. Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 35-49 24148277-1 2014 Carbon monoxide (CO), a product of heme oxygenase (HMOX), has many beneficial biological functions and is a promising therapeutic agent for many pathological conditions. Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 51-55 23592614-4 2013 Administration of hemin (4 mg/kg body weight) every other day for 4 weeks induced a massive increase in HO-1 expression and activity, as shown by the increased levels of the two main metabolic products of heme degradation, bilirubin and carbon monoxide (CO). Carbon Monoxide 237-252 heme oxygenase 1 Rattus norvegicus 104-108 23592614-4 2013 Administration of hemin (4 mg/kg body weight) every other day for 4 weeks induced a massive increase in HO-1 expression and activity, as shown by the increased levels of the two main metabolic products of heme degradation, bilirubin and carbon monoxide (CO). Carbon Monoxide 254-256 heme oxygenase 1 Rattus norvegicus 104-108 23000891-0 2013 Heme oxygenase 1-generated carbon monoxide and biliverdin attenuate the course of experimental necrotizing pancreatitis. Carbon Monoxide 27-42 heme oxygenase 1 Rattus norvegicus 0-16 23704825-12 2013 CONCLUSION: Reducing hepatic iron deposition and CO levels by inhibiting HO-1 activity though the Nrf2/Keap pathway could be helpful in improving hepatic fibrosis and regulating PVP. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 73-77 23525258-2 2013 Heme oxygenase (HO)-1 and its by-products, iron and carbon monoxide (CO), play crucial roles in hepatic fibrosis. Carbon Monoxide 52-67 heme oxygenase 1 Rattus norvegicus 0-21 23525258-2 2013 Heme oxygenase (HO)-1 and its by-products, iron and carbon monoxide (CO), play crucial roles in hepatic fibrosis. Carbon Monoxide 69-71 heme oxygenase 1 Rattus norvegicus 0-21 23215739-2 2013 HO-1 catalyzes the conversion of heme protein to biliverdin, free iron, and carbon monoxide. Carbon Monoxide 76-91 heme oxygenase 1 Rattus norvegicus 0-4 22185821-4 2012 The protection required functional heme oxygenase-1 activity, since zinc protoporphyrin IX, a heme oxygenase-1 inhibitor, prevented NF-kappaB inhibition, and the presence of exogenous carbon monoxide and bilirubin afforded cytoprotection against paraquat-induced toxicity by preventing NF-kappaB activation. Carbon Monoxide 184-199 heme oxygenase 1 Rattus norvegicus 35-51 23224421-0 2013 Pharmacological activation of heme oxygenase (HO)-1/carbon monoxide pathway prevents the development of peripheral neuropathic pain in Wistar rats. Carbon Monoxide 52-67 heme oxygenase 1 Rattus norvegicus 30-51 20018301-3 2011 The inducible heme oxygenase-1 (HO-1) catalyzes the stepwise degradation of heme to produce equimolar quantities of biliverdin, iron, and carbon monoxide; it has also been suggested to promote the important cholesterol-independent cytoprotective action of statins against oxidative insults. Carbon Monoxide 138-153 heme oxygenase 1 Rattus norvegicus 14-30 21849637-2 2011 HO-derived metabolites, presumably carbon monoxide (CO), mediate vasodilatory influences in the renal circulation, particularly in conditions linked to elevated HO-1 protein expression or diminished nitric oxide (NO) levels. Carbon Monoxide 35-50 heme oxygenase 1 Rattus norvegicus 161-165 21849637-2 2011 HO-derived metabolites, presumably carbon monoxide (CO), mediate vasodilatory influences in the renal circulation, particularly in conditions linked to elevated HO-1 protein expression or diminished nitric oxide (NO) levels. Carbon Monoxide 52-54 heme oxygenase 1 Rattus norvegicus 161-165 20018301-3 2011 The inducible heme oxygenase-1 (HO-1) catalyzes the stepwise degradation of heme to produce equimolar quantities of biliverdin, iron, and carbon monoxide; it has also been suggested to promote the important cholesterol-independent cytoprotective action of statins against oxidative insults. Carbon Monoxide 138-153 heme oxygenase 1 Rattus norvegicus 32-36 21518603-3 2011 It has been demonstrated that the heme oxygenase-1/carbon monoxide (HO-1/CO) system plays an important role in the control of vascular tone. Carbon Monoxide 51-66 heme oxygenase 1 Rattus norvegicus 34-50 21198546-8 2011 Both products of the HO-1 reaction, CO and bilirubin, inhibited (by 30-40%) NFAT3 activation and production of the pro-apoptotic proteins Bcl-XS/Bax. Carbon Monoxide 36-38 heme oxygenase 1 Rattus norvegicus 21-25 21383306-1 2011 Recent in vitro studies have reported that heme oxygenase 1 (HO-1) downregulates the angiostatic protein soluble fms-like tyrosine kinase 1 from placental villous explants and that the HO-1 metabolites CO and bilirubin negatively regulate endothelin 1 and reactive oxygen species. Carbon Monoxide 202-204 heme oxygenase 1 Rattus norvegicus 43-59 21383306-1 2011 Recent in vitro studies have reported that heme oxygenase 1 (HO-1) downregulates the angiostatic protein soluble fms-like tyrosine kinase 1 from placental villous explants and that the HO-1 metabolites CO and bilirubin negatively regulate endothelin 1 and reactive oxygen species. Carbon Monoxide 202-204 heme oxygenase 1 Rattus norvegicus 61-65 21383306-1 2011 Recent in vitro studies have reported that heme oxygenase 1 (HO-1) downregulates the angiostatic protein soluble fms-like tyrosine kinase 1 from placental villous explants and that the HO-1 metabolites CO and bilirubin negatively regulate endothelin 1 and reactive oxygen species. Carbon Monoxide 202-204 heme oxygenase 1 Rattus norvegicus 185-189 21239629-2 2011 Heme oxygenases (HO-1 and HO-2) release carbon monoxide (CO) and biliverdin, which may help control renal function. Carbon Monoxide 40-55 heme oxygenase 1 Rattus norvegicus 17-30 21239629-2 2011 Heme oxygenases (HO-1 and HO-2) release carbon monoxide (CO) and biliverdin, which may help control renal function. Carbon Monoxide 57-59 heme oxygenase 1 Rattus norvegicus 17-30 21239629-10 2011 We concluded that HO-1 and HO-2 in the nephron inhibit TGF by releasing CO and biliverdin. Carbon Monoxide 72-74 heme oxygenase 1 Rattus norvegicus 18-31 20422170-0 2011 Dynamic changes of heme oxygenase-1 in the hippocampus of rats after acute carbon monoxide poisoning. Carbon Monoxide 75-90 heme oxygenase 1 Rattus norvegicus 19-35 20422170-1 2011 Heme oxygenase-1 (HO-1), an inducible enzyme, degrades heme to carbon monoxide (CO), iron, and bilirubin. Carbon Monoxide 63-78 heme oxygenase 1 Rattus norvegicus 0-16 20422170-1 2011 Heme oxygenase-1 (HO-1), an inducible enzyme, degrades heme to carbon monoxide (CO), iron, and bilirubin. Carbon Monoxide 63-78 heme oxygenase 1 Rattus norvegicus 18-22 20422170-1 2011 Heme oxygenase-1 (HO-1), an inducible enzyme, degrades heme to carbon monoxide (CO), iron, and bilirubin. Carbon Monoxide 80-82 heme oxygenase 1 Rattus norvegicus 0-16 20422170-1 2011 Heme oxygenase-1 (HO-1), an inducible enzyme, degrades heme to carbon monoxide (CO), iron, and bilirubin. Carbon Monoxide 80-82 heme oxygenase 1 Rattus norvegicus 18-22 21115498-0 2011 Heme oxygenase-1/carbon monoxide induces vascular endothelial growth factor expression via p38 kinase-dependent activation of Sp1. Carbon Monoxide 17-32 heme oxygenase 1 Rattus norvegicus 0-16 21115498-1 2011 Heme oxygenase-1 (HO-1) is a stress-inducible enzyme catalyzing the oxidative degradation of heme to free iron, CO, and biliverdin. Carbon Monoxide 112-114 heme oxygenase 1 Rattus norvegicus 0-16 21115498-1 2011 Heme oxygenase-1 (HO-1) is a stress-inducible enzyme catalyzing the oxidative degradation of heme to free iron, CO, and biliverdin. Carbon Monoxide 112-114 heme oxygenase 1 Rattus norvegicus 18-22 21518603-3 2011 It has been demonstrated that the heme oxygenase-1/carbon monoxide (HO-1/CO) system plays an important role in the control of vascular tone. Carbon Monoxide 51-66 heme oxygenase 1 Rattus norvegicus 68-75 20053955-0 2010 Carbon monoxide releasing molecule-2 inhibits pancreatic stellate cell proliferation by activating p38 mitogen-activated protein kinase/heme oxygenase-1 signaling. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 136-152 19520142-0 2009 Induction of heme oxygenase-1 with hemin attenuates hippocampal injury in rats after acute carbon monoxide poisoning. Carbon Monoxide 91-106 heme oxygenase 1 Rattus norvegicus 13-29 19171794-9 2009 HO-1 expression was measured by Western blot analysis and HO-1 activity by serum carbon monoxide content. Carbon Monoxide 81-96 heme oxygenase 1 Rattus norvegicus 58-62 19444967-1 2009 UNLABELLED: There is increasing evidence that carbon monoxide (CO), a signaling molecule generated during the degradation of heme by heme oxygenase-1 (HO-1) in biological systems, has a variety of cytoprotective actions, including anti-hypoxic effects at low temperatures. Carbon Monoxide 46-61 heme oxygenase 1 Rattus norvegicus 133-149 19444967-1 2009 UNLABELLED: There is increasing evidence that carbon monoxide (CO), a signaling molecule generated during the degradation of heme by heme oxygenase-1 (HO-1) in biological systems, has a variety of cytoprotective actions, including anti-hypoxic effects at low temperatures. Carbon Monoxide 63-65 heme oxygenase 1 Rattus norvegicus 133-149 18795901-1 2009 BACKGROUND/OBJECTIVE: Carbon monoxide (CO) produced by haem-oxygenase isoforms (HO-1 & HO-2) is involved in the regulation of systemic vascular tone. Carbon Monoxide 22-37 heme oxygenase 1 Rattus norvegicus 55-84 18795901-1 2009 BACKGROUND/OBJECTIVE: Carbon monoxide (CO) produced by haem-oxygenase isoforms (HO-1 & HO-2) is involved in the regulation of systemic vascular tone. Carbon Monoxide 39-41 heme oxygenase 1 Rattus norvegicus 55-84 19356108-9 2008 In conclusion, there appears to be a temporal HO-1-adiponectin relationship that has a key role in vascular protection in Type 1 diabetes via a mechanism that involves increased levels of carbon monoxide. Carbon Monoxide 188-203 heme oxygenase 1 Rattus norvegicus 46-50 18756386-5 2009 CO and bilirubin up-regulated the heme oxygenase-1 (HO-1), which was required for the protective effect of CO, and a single bilirubin treatment increased DOX-induced apoptosis in H9c2 cells. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 34-50 18756386-5 2009 CO and bilirubin up-regulated the heme oxygenase-1 (HO-1), which was required for the protective effect of CO, and a single bilirubin treatment increased DOX-induced apoptosis in H9c2 cells. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 52-56 18179459-1 2008 INTRODUCTION: Cyclic guanosine monophosphate (cGMP) levels can be regulated by heme oxygenase-1 and 2 (HO-1 and HO-2)-derived carbon monoxide (CO). Carbon Monoxide 126-141 heme oxygenase 1 Rattus norvegicus 79-101 18768868-1 2008 Heme oxygenase (HO)-1 catalyzes the rate-limiting step of heme degradation and plays an important anti-inflammatory role via its enzymatic products carbon monoxide and biliverdin. Carbon Monoxide 148-163 heme oxygenase 1 Rattus norvegicus 0-21 18179459-1 2008 INTRODUCTION: Cyclic guanosine monophosphate (cGMP) levels can be regulated by heme oxygenase-1 and 2 (HO-1 and HO-2)-derived carbon monoxide (CO). Carbon Monoxide 126-141 heme oxygenase 1 Rattus norvegicus 103-107 18179459-1 2008 INTRODUCTION: Cyclic guanosine monophosphate (cGMP) levels can be regulated by heme oxygenase-1 and 2 (HO-1 and HO-2)-derived carbon monoxide (CO). Carbon Monoxide 143-145 heme oxygenase 1 Rattus norvegicus 79-101 18179459-1 2008 INTRODUCTION: Cyclic guanosine monophosphate (cGMP) levels can be regulated by heme oxygenase-1 and 2 (HO-1 and HO-2)-derived carbon monoxide (CO). Carbon Monoxide 143-145 heme oxygenase 1 Rattus norvegicus 103-107 17681938-0 2007 Carbon monoxide produced by heme oxygenase-1 in response to nitrosative stress induces expression of glutamate-cysteine ligase in PC12 cells via activation of phosphatidylinositol 3-kinase and Nrf2 signaling. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 28-44 17999922-2 2008 During stress, the inducible heme oxygenase-1 protein and its reaction products, including carbon monoxide, also exert potent hepatoprotective effects. Carbon Monoxide 91-106 heme oxygenase 1 Rattus norvegicus 29-45 17681938-2 2007 In this study, we investigated the potential role of carbon monoxide (CO), one of the by-products of the HO-1 reaction, in the adaptive survival response to peroxynitrite-induced PC12 cell death. Carbon Monoxide 53-68 heme oxygenase 1 Rattus norvegicus 105-109 17681938-2 2007 In this study, we investigated the potential role of carbon monoxide (CO), one of the by-products of the HO-1 reaction, in the adaptive survival response to peroxynitrite-induced PC12 cell death. Carbon Monoxide 70-72 heme oxygenase 1 Rattus norvegicus 105-109 17330989-4 2007 Consistent with the induction of HO-1, a platelet bioassay revealed production of carbon monoxide by reoxygenated astrocytes. Carbon Monoxide 82-97 heme oxygenase 1 Rattus norvegicus 33-37 17526019-2 2007 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in the oxidative degradation of heme to ferrous iron, carbon monoxide, and biliverdin, is upregulated in affected PD astroglia and may contribute to abnormal mitochondrial iron sequestration in these cells. Carbon Monoxide 104-119 heme oxygenase 1 Rattus norvegicus 0-16 17526019-2 2007 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in the oxidative degradation of heme to ferrous iron, carbon monoxide, and biliverdin, is upregulated in affected PD astroglia and may contribute to abnormal mitochondrial iron sequestration in these cells. Carbon Monoxide 104-119 heme oxygenase 1 Rattus norvegicus 18-22 17849050-1 2007 Hemin is a heme oxygenase-1 (HO-1) inducer which provides endogenous carbon monoxide known for playing roles in cell proliferation, inflammation or aggregation process. Carbon Monoxide 69-84 heme oxygenase 1 Rattus norvegicus 11-27 17849050-1 2007 Hemin is a heme oxygenase-1 (HO-1) inducer which provides endogenous carbon monoxide known for playing roles in cell proliferation, inflammation or aggregation process. Carbon Monoxide 69-84 heme oxygenase 1 Rattus norvegicus 29-33 16785033-2 2006 Heme oxygenases (HO-1/HO-2) and the products of their activity, biliverdin/bilirubin and carbon monoxide (CO), play a physiological role in the vascular system. Carbon Monoxide 89-104 heme oxygenase 1 Rattus norvegicus 17-26 17173083-1 2006 OBJECTIVE: To investigate the protective role of heme oxygenase-1 and its reaction product, carbon monoxide against acute liver injury induced by carbon tetrachloride in rats. Carbon Monoxide 92-107 heme oxygenase 1 Rattus norvegicus 49-65 16978757-1 2006 Heme oxygenase-1, a stress-responsive enzyme that catabolizes hemes into carbon monoxide, biliverdin, and iron, has been shown to play a pivotal role in many physiological and pathological situations. Carbon Monoxide 73-88 heme oxygenase 1 Rattus norvegicus 0-16 16844915-1 2006 Heme oxygenases (HO-1 and HO-2) catalyze the conversion of heme to carbon monoxide (CO), iron, and biliverdin. Carbon Monoxide 67-82 heme oxygenase 1 Rattus norvegicus 0-30 16844915-1 2006 Heme oxygenases (HO-1 and HO-2) catalyze the conversion of heme to carbon monoxide (CO), iron, and biliverdin. Carbon Monoxide 84-86 heme oxygenase 1 Rattus norvegicus 0-30 17057755-1 2006 BACKGROUND AND PURPOSE: Carbon monoxide (CO) generated by the enzyme haeme oxygenase-1 (HO-1) during the breakdown of haeme is known to mediate a number of biological effects. Carbon Monoxide 24-39 heme oxygenase 1 Rattus norvegicus 69-92 17057755-1 2006 BACKGROUND AND PURPOSE: Carbon monoxide (CO) generated by the enzyme haeme oxygenase-1 (HO-1) during the breakdown of haeme is known to mediate a number of biological effects. Carbon Monoxide 41-43 heme oxygenase 1 Rattus norvegicus 69-92 16565166-0 2006 Induction of heme oxygenase-1 is involved in carbon monoxide-mediated central cardiovascular regulation. Carbon Monoxide 45-60 heme oxygenase 1 Rattus norvegicus 13-29 16785033-2 2006 Heme oxygenases (HO-1/HO-2) and the products of their activity, biliverdin/bilirubin and carbon monoxide (CO), play a physiological role in the vascular system. Carbon Monoxide 106-108 heme oxygenase 1 Rattus norvegicus 17-26 16771696-5 2006 Interestingly, the HO-1 repression following TAR plus beta-carotene treatment caused a resynchronization of RAT-1 cell-cycle with a significant increase in the S-phase, and this was probably due to the decreased intracellular levels of carbon monoxide and bilirubin, both of which have antiproliferative effects. Carbon Monoxide 236-251 heme oxygenase 1 Rattus norvegicus 19-23 16598857-1 2006 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in catalyzing heme degradation into biliverdin, free iron, and carbon monoxide (CO), serves as a protective enzyme against oxidative and nitrosative stresses. Carbon Monoxide 113-128 heme oxygenase 1 Rattus norvegicus 0-16 16628357-0 2006 [Simvastatin inhibits hypertension-induced cardiac hypertrophy in rats through activation of heme oxygenase-1/carbon monoxide pathway]. Carbon Monoxide 110-125 heme oxygenase 1 Rattus norvegicus 93-109 16598857-1 2006 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in catalyzing heme degradation into biliverdin, free iron, and carbon monoxide (CO), serves as a protective enzyme against oxidative and nitrosative stresses. Carbon Monoxide 113-128 heme oxygenase 1 Rattus norvegicus 18-22 16598857-1 2006 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in catalyzing heme degradation into biliverdin, free iron, and carbon monoxide (CO), serves as a protective enzyme against oxidative and nitrosative stresses. Carbon Monoxide 130-132 heme oxygenase 1 Rattus norvegicus 0-16 16598857-1 2006 Heme oxygenase-1 (HO-1), the rate-limiting enzyme in catalyzing heme degradation into biliverdin, free iron, and carbon monoxide (CO), serves as a protective enzyme against oxidative and nitrosative stresses. Carbon Monoxide 130-132 heme oxygenase 1 Rattus norvegicus 18-22 15452083-0 2004 Heme oxygenase-1-related carbon monoxide and flavonoids in ischemic/reperfused rat retina. Carbon Monoxide 25-40 heme oxygenase 1 Rattus norvegicus 0-16 16309593-1 2005 Emerging evidence reveals that heme oxygenase-1 (HO-1) and its product carbon monoxide (CO) can exert diverse biological and cytoprotective effects. Carbon Monoxide 71-86 heme oxygenase 1 Rattus norvegicus 31-47 16309593-1 2005 Emerging evidence reveals that heme oxygenase-1 (HO-1) and its product carbon monoxide (CO) can exert diverse biological and cytoprotective effects. Carbon Monoxide 71-86 heme oxygenase 1 Rattus norvegicus 49-53 16309593-1 2005 Emerging evidence reveals that heme oxygenase-1 (HO-1) and its product carbon monoxide (CO) can exert diverse biological and cytoprotective effects. Carbon Monoxide 88-90 heme oxygenase 1 Rattus norvegicus 31-47 16309593-1 2005 Emerging evidence reveals that heme oxygenase-1 (HO-1) and its product carbon monoxide (CO) can exert diverse biological and cytoprotective effects. Carbon Monoxide 88-90 heme oxygenase 1 Rattus norvegicus 49-53 15641110-4 2005 Among the various heat shock proteins, heme oxygenase-1 has received considerable attention; it has been recently demonstrated that heme oxygenase-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. Carbon Monoxide 198-213 heme oxygenase 1 Rattus norvegicus 39-55 15641110-4 2005 Among the various heat shock proteins, heme oxygenase-1 has received considerable attention; it has been recently demonstrated that heme oxygenase-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. Carbon Monoxide 198-213 heme oxygenase 1 Rattus norvegicus 132-148 15582353-1 2005 Heme oxygenase-1 (HO-1) is a 32-kDa stress induced enzyme that degrades heme to carbon monoxide (CO) and biliverdin. Carbon Monoxide 80-95 heme oxygenase 1 Rattus norvegicus 0-16 15582353-1 2005 Heme oxygenase-1 (HO-1) is a 32-kDa stress induced enzyme that degrades heme to carbon monoxide (CO) and biliverdin. Carbon Monoxide 80-95 heme oxygenase 1 Rattus norvegicus 18-22 15582353-1 2005 Heme oxygenase-1 (HO-1) is a 32-kDa stress induced enzyme that degrades heme to carbon monoxide (CO) and biliverdin. Carbon Monoxide 97-99 heme oxygenase 1 Rattus norvegicus 0-16 15582353-1 2005 Heme oxygenase-1 (HO-1) is a 32-kDa stress induced enzyme that degrades heme to carbon monoxide (CO) and biliverdin. Carbon Monoxide 97-99 heme oxygenase 1 Rattus norvegicus 18-22 15607619-1 2004 BACKGROUND: The aim of this study was to observe the time-course changes of heme oxygenase-1 (HO-1) and inducible nitric oxide synthase (iNOS) induction in aorta during the development of hypertension, as well as the relationship of HO-1/carbon monoxide (CO) system and iNOS/nitric oxide (NO) system in spontaneously hypertensive rats (SHR). Carbon Monoxide 238-253 heme oxygenase 1 Rattus norvegicus 76-92 15838352-3 2004 Carbon monoxide has the same attenuation effect and is synthesized by inducible heme-oxygenase- 1 or constitutive heme-oxygenase-2. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 80-130 16316349-1 2005 BACKGROUND: The heme oxygenase system (HO-1 and HO-2) catalyzes the conversion of heme to free iron, carbon monoxide (CO), a vasodepressor, and biliverdin, which is further converted to bilirubin, an antioxidant. Carbon Monoxide 101-116 heme oxygenase 1 Rattus norvegicus 39-43 16316349-1 2005 BACKGROUND: The heme oxygenase system (HO-1 and HO-2) catalyzes the conversion of heme to free iron, carbon monoxide (CO), a vasodepressor, and biliverdin, which is further converted to bilirubin, an antioxidant. Carbon Monoxide 118-120 heme oxygenase 1 Rattus norvegicus 39-43 16309565-1 2005 Recent studies indicate that systemic induction of heme oxygenase-1 (HO-1), which oxidatively degrades heme into iron, biliverdin, and carbon monoxide (CO), or adenoviral-mediated gene transfer of HO-1 inhibits neointima formation after experimental vascular injury. Carbon Monoxide 135-150 heme oxygenase 1 Rattus norvegicus 51-67 16309565-1 2005 Recent studies indicate that systemic induction of heme oxygenase-1 (HO-1), which oxidatively degrades heme into iron, biliverdin, and carbon monoxide (CO), or adenoviral-mediated gene transfer of HO-1 inhibits neointima formation after experimental vascular injury. Carbon Monoxide 135-150 heme oxygenase 1 Rattus norvegicus 69-73 16309565-1 2005 Recent studies indicate that systemic induction of heme oxygenase-1 (HO-1), which oxidatively degrades heme into iron, biliverdin, and carbon monoxide (CO), or adenoviral-mediated gene transfer of HO-1 inhibits neointima formation after experimental vascular injury. Carbon Monoxide 152-154 heme oxygenase 1 Rattus norvegicus 51-67 16309565-1 2005 Recent studies indicate that systemic induction of heme oxygenase-1 (HO-1), which oxidatively degrades heme into iron, biliverdin, and carbon monoxide (CO), or adenoviral-mediated gene transfer of HO-1 inhibits neointima formation after experimental vascular injury. Carbon Monoxide 152-154 heme oxygenase 1 Rattus norvegicus 69-73 15821039-8 2005 These data demonstrate that an increase in HO-1 protein and activity, i.e., CO and bilirubin production, in diabetic rats brings about a robust increase in EC-SOD, catalase, and eNOS with a concomitant increase in endothelial relaxation and a decrease in O2-. Carbon Monoxide 76-78 heme oxygenase 1 Rattus norvegicus 43-47 15561977-2 2005 HO-1 degrades heme into carbon monoxide (CO) and biliverdin; the latter is then converted to bilirubin. Carbon Monoxide 24-39 heme oxygenase 1 Rattus norvegicus 0-4 15561977-2 2005 HO-1 degrades heme into carbon monoxide (CO) and biliverdin; the latter is then converted to bilirubin. Carbon Monoxide 41-43 heme oxygenase 1 Rattus norvegicus 0-4 16200866-1 2004 OBJECTIVE: To explore the impact of hydrogen sulfide (H2S) on the carbon monoxide (CO)/heme oxygenase-1 (HO-1) system in pulmonary artery of hypoxic rats. Carbon Monoxide 66-81 heme oxygenase 1 Rattus norvegicus 105-109 12924938-0 2003 Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1. Carbon Monoxide 34-36 heme oxygenase 1 Rattus norvegicus 73-89 15225803-3 2004 Heat shock protein-32 is a well-established marker of the cerebral oxidative stress response and contributes to neuroprotection by metabolising cytotoxic free heme to carbon monoxide, iron and biliverdin. Carbon Monoxide 167-182 heme oxygenase 1 Rattus norvegicus 0-21 14759565-2 2004 Hsp32, also known as heme oxygenase 1, catalyzes the degradation of heme to produce carbon monoxide and bilirubin, which play a variety of cytoprotective functions at physiological concentrations, and iron, which is rapidly sequestered by the iron-binding protein ferritin. Carbon Monoxide 84-99 heme oxygenase 1 Rattus norvegicus 0-5 14600247-1 2004 Carbon monoxide (CO), a product of heme metabolism by heme-oxygenase (HO), has biological actions similar to those of nitric oxide (NO). Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 70-72 14600247-1 2004 Carbon monoxide (CO), a product of heme metabolism by heme-oxygenase (HO), has biological actions similar to those of nitric oxide (NO). Carbon Monoxide 17-19 heme oxygenase 1 Rattus norvegicus 70-72 14687464-13 2003 CONCLUSIONS: The expression of HO-1 gene in PASMCs is upregulated by hypoxia and the production of endogenous CO is elevated as well. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 31-35 15300591-2 2004 By degrading heme, HO-1 generates carbon monoxide (CO), iron and biliverdin. Carbon Monoxide 34-49 heme oxygenase 1 Rattus norvegicus 19-23 15300591-2 2004 By degrading heme, HO-1 generates carbon monoxide (CO), iron and biliverdin. Carbon Monoxide 51-53 heme oxygenase 1 Rattus norvegicus 19-23 14759565-2 2004 Hsp32, also known as heme oxygenase 1, catalyzes the degradation of heme to produce carbon monoxide and bilirubin, which play a variety of cytoprotective functions at physiological concentrations, and iron, which is rapidly sequestered by the iron-binding protein ferritin. Carbon Monoxide 84-99 heme oxygenase 1 Rattus norvegicus 21-37 14662543-13 2003 The enhanced induction of HO1 expression and activity in females after trauma and hemorrhage may attenuate hepatocellular dysfunction and injury by maintaining microcirculation via the increased production of carbon monoxide. Carbon Monoxide 209-224 heme oxygenase 1 Rattus norvegicus 26-29 12924938-0 2003 Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1. Carbon Monoxide 34-36 heme oxygenase 1 Rattus norvegicus 91-95 12924938-0 2003 Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1. Carbon Monoxide 34-36 heme oxygenase 1 Rattus norvegicus 183-187 12855890-2 2003 Heme-oxygenase-1 (HO-1) metabolizes heme, a potent cytotoxic agent, to carbon monoxide and biliverdin. Carbon Monoxide 71-86 heme oxygenase 1 Rattus norvegicus 0-16 12819027-2 2003 There is mounting evidence that the stress response gene heme oxygenase-1 (HO-1) and/or its catalytic by-product carbon monoxide (CO) confers cytoprotection against tissue and cellular injury. Carbon Monoxide 113-128 heme oxygenase 1 Rattus norvegicus 57-73 12819027-2 2003 There is mounting evidence that the stress response gene heme oxygenase-1 (HO-1) and/or its catalytic by-product carbon monoxide (CO) confers cytoprotection against tissue and cellular injury. Carbon Monoxide 113-128 heme oxygenase 1 Rattus norvegicus 75-79 12855890-2 2003 Heme-oxygenase-1 (HO-1) metabolizes heme, a potent cytotoxic agent, to carbon monoxide and biliverdin. Carbon Monoxide 71-86 heme oxygenase 1 Rattus norvegicus 18-22 12133272-0 2002 Heme oxygenase 1 gene transfer prevents CD95/Fas ligand-mediated apoptosis and improves liver allograft survival via carbon monoxide signaling pathway. Carbon Monoxide 117-132 heme oxygenase 1 Rattus norvegicus 0-16 12593860-1 2003 Heme oxygenase-1 (HO-1) is an inducible form of heme oxygenase that catabolizes heme to carbon monoxide, biliverdin, and ferrous iron. Carbon Monoxide 88-103 heme oxygenase 1 Rattus norvegicus 0-16 12593860-1 2003 Heme oxygenase-1 (HO-1) is an inducible form of heme oxygenase that catabolizes heme to carbon monoxide, biliverdin, and ferrous iron. Carbon Monoxide 88-103 heme oxygenase 1 Rattus norvegicus 18-22 12548710-1 2003 Heme oxygenase-1 (HO1) catalyzes oxidation of the heme molecule in concert with NADPH-cytochrome P450 reductase following the specific cleavage of heme into carbon monoxide, iron, and biliverdin, which is rapidly metabolized to bilirubin. Carbon Monoxide 157-172 heme oxygenase 1 Rattus norvegicus 0-16 12548710-1 2003 Heme oxygenase-1 (HO1) catalyzes oxidation of the heme molecule in concert with NADPH-cytochrome P450 reductase following the specific cleavage of heme into carbon monoxide, iron, and biliverdin, which is rapidly metabolized to bilirubin. Carbon Monoxide 157-172 heme oxygenase 1 Rattus norvegicus 18-21 21174820-1 2002 AIM: To investigate the expression of heme oxygenase-1 gene and production of endogenous carbon monoxide in the rat lung tissue at different time points of chronic hypoxic pulmonary hypertension and the effect of hemin, an inducer of heme oxygenase, on the expression of HO-1 gene and production of endogenous carbon monoxide and pulmonary hypertension. Carbon Monoxide 310-325 heme oxygenase 1 Rattus norvegicus 38-54 12218538-1 2002 BACKGROUND: Although precise mechanisms remain to be determined, recent studies show that heme oxygenase-1 (HO-1), providing endogenous carbon monoxide (CO) and bilirubin, serves as an antiinflammatory enzyme. Carbon Monoxide 136-151 heme oxygenase 1 Rattus norvegicus 90-106 12218538-1 2002 BACKGROUND: Although precise mechanisms remain to be determined, recent studies show that heme oxygenase-1 (HO-1), providing endogenous carbon monoxide (CO) and bilirubin, serves as an antiinflammatory enzyme. Carbon Monoxide 136-151 heme oxygenase 1 Rattus norvegicus 108-112 12218538-1 2002 BACKGROUND: Although precise mechanisms remain to be determined, recent studies show that heme oxygenase-1 (HO-1), providing endogenous carbon monoxide (CO) and bilirubin, serves as an antiinflammatory enzyme. Carbon Monoxide 153-155 heme oxygenase 1 Rattus norvegicus 90-106 12218538-1 2002 BACKGROUND: Although precise mechanisms remain to be determined, recent studies show that heme oxygenase-1 (HO-1), providing endogenous carbon monoxide (CO) and bilirubin, serves as an antiinflammatory enzyme. Carbon Monoxide 153-155 heme oxygenase 1 Rattus norvegicus 108-112 12201358-2 2002 Heme oxygenase-1 (HO-1) is a tissue protective molecule which degrades heme into carbon monoxide (CO), free iron and biliverdin. Carbon Monoxide 81-96 heme oxygenase 1 Rattus norvegicus 0-16 12201358-2 2002 Heme oxygenase-1 (HO-1) is a tissue protective molecule which degrades heme into carbon monoxide (CO), free iron and biliverdin. Carbon Monoxide 81-96 heme oxygenase 1 Rattus norvegicus 18-22 12201358-2 2002 Heme oxygenase-1 (HO-1) is a tissue protective molecule which degrades heme into carbon monoxide (CO), free iron and biliverdin. Carbon Monoxide 98-100 heme oxygenase 1 Rattus norvegicus 0-16 12201358-2 2002 Heme oxygenase-1 (HO-1) is a tissue protective molecule which degrades heme into carbon monoxide (CO), free iron and biliverdin. Carbon Monoxide 98-100 heme oxygenase 1 Rattus norvegicus 18-22 21207851-1 2003 AIM: To explore the effects of heme- heme oxygenase-1 (HO-1)-carbon monoxide(CO)-cyclic GMP (cGMP)on aortic vascular reactivity in endotoxemic rats and its molecular mechanism. Carbon Monoxide 61-76 heme oxygenase 1 Rattus norvegicus 37-53 21207851-1 2003 AIM: To explore the effects of heme- heme oxygenase-1 (HO-1)-carbon monoxide(CO)-cyclic GMP (cGMP)on aortic vascular reactivity in endotoxemic rats and its molecular mechanism. Carbon Monoxide 77-80 heme oxygenase 1 Rattus norvegicus 37-53 12392996-1 2002 Heme oxygenase-1 (HO-1) is a heat shock protein catalysing the degradation of heme to yield biliverdin, carbon monoxide and iron. Carbon Monoxide 104-119 heme oxygenase 1 Rattus norvegicus 0-16 12392996-1 2002 Heme oxygenase-1 (HO-1) is a heat shock protein catalysing the degradation of heme to yield biliverdin, carbon monoxide and iron. Carbon Monoxide 104-119 heme oxygenase 1 Rattus norvegicus 18-22 12123779-1 2002 OBJECTIVE: Carbon monoxide (CO) is generated from vascular smooth muscle cells via the degradation of heme by the enzyme heme oxygenase-1. Carbon Monoxide 11-26 heme oxygenase 1 Rattus norvegicus 121-137 12123779-1 2002 OBJECTIVE: Carbon monoxide (CO) is generated from vascular smooth muscle cells via the degradation of heme by the enzyme heme oxygenase-1. Carbon Monoxide 28-30 heme oxygenase 1 Rattus norvegicus 121-137 12133272-9 2002 To deliver CO, one of the downstream HO-1 mediators, allogeneic OLT recipients were exposed to methylene chloride. Carbon Monoxide 11-13 heme oxygenase 1 Rattus norvegicus 37-41 11772880-1 2002 BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into biliverdin, iron, and carbon monoxide (CO). Carbon Monoxide 97-112 heme oxygenase 1 Rattus norvegicus 12-28 12006175-3 2002 We hypothesized that carbon monoxide (CO), a major catalytic byproduct of heme catalysis by HO-1, may mediate this antiinflammatory effect by modulating signal transduction pathways, in particular the mitogen-activated protein (MAP) kinase pathway. Carbon Monoxide 21-36 heme oxygenase 1 Rattus norvegicus 92-96 12006175-3 2002 We hypothesized that carbon monoxide (CO), a major catalytic byproduct of heme catalysis by HO-1, may mediate this antiinflammatory effect by modulating signal transduction pathways, in particular the mitogen-activated protein (MAP) kinase pathway. Carbon Monoxide 38-40 heme oxygenase 1 Rattus norvegicus 92-96 11915027-1 2002 A direct role of carbon monoxide (CO), an effector-signaling molecule during heme oxygenase-1 (HO-1) catalysis of heme, in the protection against hepatic ischemia/reperfusion (I/R) injury needs to be established. Carbon Monoxide 17-32 heme oxygenase 1 Rattus norvegicus 77-93 11915027-1 2002 A direct role of carbon monoxide (CO), an effector-signaling molecule during heme oxygenase-1 (HO-1) catalysis of heme, in the protection against hepatic ischemia/reperfusion (I/R) injury needs to be established. Carbon Monoxide 17-32 heme oxygenase 1 Rattus norvegicus 95-99 11915027-1 2002 A direct role of carbon monoxide (CO), an effector-signaling molecule during heme oxygenase-1 (HO-1) catalysis of heme, in the protection against hepatic ischemia/reperfusion (I/R) injury needs to be established. Carbon Monoxide 34-36 heme oxygenase 1 Rattus norvegicus 77-93 11915027-1 2002 A direct role of carbon monoxide (CO), an effector-signaling molecule during heme oxygenase-1 (HO-1) catalysis of heme, in the protection against hepatic ischemia/reperfusion (I/R) injury needs to be established. Carbon Monoxide 34-36 heme oxygenase 1 Rattus norvegicus 95-99 11915027-6 2002 Moreover, adjunctive use of zinc protoporphyrin, a competitive HO-1 inhibitor, has shown that exogenous CO could fully substitute for endogenous HO-1 in preventing hepatic I/R insult. Carbon Monoxide 104-106 heme oxygenase 1 Rattus norvegicus 63-67 11882623-1 2002 Heme oxygenase enzymes (HO-1 and HO-2) catalyze the conversion of heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 101-116 heme oxygenase 1 Rattus norvegicus 24-28 11882623-1 2002 Heme oxygenase enzymes (HO-1 and HO-2) catalyze the conversion of heme to biliverdin, free iron, and carbon monoxide (CO). Carbon Monoxide 118-120 heme oxygenase 1 Rattus norvegicus 24-28 11801258-1 2002 Heme oxygenase (HO)-1 catalyzes the rate-limiting step in heme degradation releasing iron, carbon monoxide, and biliverdin. Carbon Monoxide 91-106 heme oxygenase 1 Rattus norvegicus 0-21 12180836-1 2002 Heme oxygenase 1 (HO-1) is an enzyme which degrades heme into tree end products: biliverdin, free iron and carbon monoxide. Carbon Monoxide 107-122 heme oxygenase 1 Rattus norvegicus 0-16 12180836-1 2002 Heme oxygenase 1 (HO-1) is an enzyme which degrades heme into tree end products: biliverdin, free iron and carbon monoxide. Carbon Monoxide 107-122 heme oxygenase 1 Rattus norvegicus 18-22 12006174-2 2002 HO-1 degrades heme to carbon monoxide (CO), iron, and biliverdin, the latter being reduced to bilirubin by biliverdin reductase. Carbon Monoxide 22-37 heme oxygenase 1 Rattus norvegicus 0-4 12006174-2 2002 HO-1 degrades heme to carbon monoxide (CO), iron, and biliverdin, the latter being reduced to bilirubin by biliverdin reductase. Carbon Monoxide 39-41 heme oxygenase 1 Rattus norvegicus 0-4 11772880-1 2002 BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into biliverdin, iron, and carbon monoxide (CO). Carbon Monoxide 97-112 heme oxygenase 1 Rattus norvegicus 30-34 11772880-1 2002 BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into biliverdin, iron, and carbon monoxide (CO). Carbon Monoxide 114-116 heme oxygenase 1 Rattus norvegicus 12-28 11772880-1 2002 BACKGROUND: Heme oxygenase-1 (HO-1) catalyzes the degradation of heme into biliverdin, iron, and carbon monoxide (CO). Carbon Monoxide 114-116 heme oxygenase 1 Rattus norvegicus 30-34 12086318-7 2001 The data reviewed focus on the role of one of such genes, the stress responsive gene heme oxygenase-1, and of its byproduct carbon monoxide, which can suppress graft rejection and lead to long-term graft survival. Carbon Monoxide 124-139 heme oxygenase 1 Rattus norvegicus 85-101 11465558-1 2001 BACKGROUND: Heme oxygenase 1 (HO-1), induced by a variety of stressors, provides endogenous carbon monoxide (CO) and bilirubin, both of which play consequential roles in organs. Carbon Monoxide 92-107 heme oxygenase 1 Rattus norvegicus 12-28 11465558-10 2001 CONCLUSIONS: These results indicate that endogenous CO via HO-1 induction attenuates sevoflurane-induced microvascular endothelial interactions with leukocytes and platelets, although local nitric oxide levels appear to dominate microvascular flow in situ. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 59-63 12030815-0 2001 Induction of alpha-calcitonin gene-related peptide mRNA expression in rat dorsal root ganglia by heat stress involves the heme oxygenase-1/carbon monoxide pathway. Carbon Monoxide 139-154 heme oxygenase 1 Rattus norvegicus 122-138 12030815-4 2001 These results indicate that induction of alpha-CGRP mRNA expression in rat DRG by heat stress involves the heme oxygenase-1/carbon monoxide pathway. Carbon Monoxide 124-139 heme oxygenase 1 Rattus norvegicus 107-123 11465558-1 2001 BACKGROUND: Heme oxygenase 1 (HO-1), induced by a variety of stressors, provides endogenous carbon monoxide (CO) and bilirubin, both of which play consequential roles in organs. Carbon Monoxide 92-107 heme oxygenase 1 Rattus norvegicus 30-34 11465558-1 2001 BACKGROUND: Heme oxygenase 1 (HO-1), induced by a variety of stressors, provides endogenous carbon monoxide (CO) and bilirubin, both of which play consequential roles in organs. Carbon Monoxide 109-111 heme oxygenase 1 Rattus norvegicus 12-28 11465558-1 2001 BACKGROUND: Heme oxygenase 1 (HO-1), induced by a variety of stressors, provides endogenous carbon monoxide (CO) and bilirubin, both of which play consequential roles in organs. Carbon Monoxide 109-111 heme oxygenase 1 Rattus norvegicus 30-34 11170717-2 2001 The neurotoxic heme is usually detoxified by the constitutive heme oxygenase-2 (HO-2) and its inducible isoform HO-1(heat shock protein 32) resulting in the formation of biliverdin which becomes reduced to bilirubin, carbon monoxide (CO), and iron. Carbon Monoxide 217-232 heme oxygenase 1 Rattus norvegicus 112-116 11302771-6 2001 In a rat model of radiation-induced nephropathy, we investigated changes in expression of heme oxygenase 1 (Hmox1, also known as HO-1), an enzyme that catalyzes conversion of heme into biliverdin, carbon monoxide and iron. Carbon Monoxide 197-212 heme oxygenase 1 Rattus norvegicus 90-106 11302771-6 2001 In a rat model of radiation-induced nephropathy, we investigated changes in expression of heme oxygenase 1 (Hmox1, also known as HO-1), an enzyme that catalyzes conversion of heme into biliverdin, carbon monoxide and iron. Carbon Monoxide 197-212 heme oxygenase 1 Rattus norvegicus 108-113 11302771-6 2001 In a rat model of radiation-induced nephropathy, we investigated changes in expression of heme oxygenase 1 (Hmox1, also known as HO-1), an enzyme that catalyzes conversion of heme into biliverdin, carbon monoxide and iron. Carbon Monoxide 197-212 heme oxygenase 1 Rattus norvegicus 129-133 11238670-3 2001 In the present study, we asked whether this protective effect was attributable to the generation of one of the catabolic products of HO-1, carbon monoxide (CO). Carbon Monoxide 139-154 heme oxygenase 1 Rattus norvegicus 133-137 11238670-3 2001 In the present study, we asked whether this protective effect was attributable to the generation of one of the catabolic products of HO-1, carbon monoxide (CO). Carbon Monoxide 156-158 heme oxygenase 1 Rattus norvegicus 133-137 11170717-2 2001 The neurotoxic heme is usually detoxified by the constitutive heme oxygenase-2 (HO-2) and its inducible isoform HO-1(heat shock protein 32) resulting in the formation of biliverdin which becomes reduced to bilirubin, carbon monoxide (CO), and iron. Carbon Monoxide 234-236 heme oxygenase 1 Rattus norvegicus 112-116 10942521-7 2000 In these conditions, compensatory upregulation of MnSOD may protect mitochondria from oxidative damage accruing from heme-derived free iron and carbon monoxide liberated by the activity of HO-1. Carbon Monoxide 144-159 heme oxygenase 1 Rattus norvegicus 189-193 16352050-1 2001 BACKGROUND: Haem oxygenase (HO-1), a heat shock or stress protein, is a rate-limiting enzyme in the conversion of pro-oxidant haem to biliverdin and carbon monoxide (CO). Carbon Monoxide 149-164 heme oxygenase 1 Rattus norvegicus 28-32 16352050-1 2001 BACKGROUND: Haem oxygenase (HO-1), a heat shock or stress protein, is a rate-limiting enzyme in the conversion of pro-oxidant haem to biliverdin and carbon monoxide (CO). Carbon Monoxide 166-168 heme oxygenase 1 Rattus norvegicus 28-32 16352050-10 2001 CONCLUSIONS: These results demonstrate that hypoxia markedly induces HO-1 expression and increases the production of CO in cardiac myocytes. Carbon Monoxide 0-2 heme oxygenase 1 Rattus norvegicus 69-73 11056178-1 2000 Heme oxygenase (HO-1, HSP32) catalyzes the oxidation of heme to biliverdin and carbon monoxide, a putative neurotransmitter. Carbon Monoxide 79-94 heme oxygenase 1 Rattus norvegicus 0-20 11056178-1 2000 Heme oxygenase (HO-1, HSP32) catalyzes the oxidation of heme to biliverdin and carbon monoxide, a putative neurotransmitter. Carbon Monoxide 79-94 heme oxygenase 1 Rattus norvegicus 22-27 11024540-1 2000 The enzyme heme oxygenase-1 (HO-1) is reducing heme to the gaseous mediator carbon monoxide, to iron and the antioxidant biliverdin. Carbon Monoxide 76-91 heme oxygenase 1 Rattus norvegicus 11-27 11024540-1 2000 The enzyme heme oxygenase-1 (HO-1) is reducing heme to the gaseous mediator carbon monoxide, to iron and the antioxidant biliverdin. Carbon Monoxide 76-91 heme oxygenase 1 Rattus norvegicus 29-33 10607912-1 2000 Heme oxygenase (HO)-2, the constitutive cognate of oxidative stress inducible HO-1 (HSP32), degrades heme to biliverdin, carbon monoxide, and iron. Carbon Monoxide 121-136 heme oxygenase 1 Rattus norvegicus 78-82 10749758-1 2000 Heme oxygenase (HO)-1 is an oxygen-dependent enzyme that may regulate vascular tone and cell proliferation through the production of carbon monoxide (CO). Carbon Monoxide 133-148 heme oxygenase 1 Rattus norvegicus 0-21 10749758-1 2000 Heme oxygenase (HO)-1 is an oxygen-dependent enzyme that may regulate vascular tone and cell proliferation through the production of carbon monoxide (CO). Carbon Monoxide 150-152 heme oxygenase 1 Rattus norvegicus 0-21 10607912-1 2000 Heme oxygenase (HO)-2, the constitutive cognate of oxidative stress inducible HO-1 (HSP32), degrades heme to biliverdin, carbon monoxide, and iron. Carbon Monoxide 121-136 heme oxygenase 1 Rattus norvegicus 84-89 10628624-1 1999 OBJECTIVE: To investigate the role of the vasodilator systems heme oxygenase-1/heat shock protein 32 (HO-1/HSP32) and nitric oxide synthase-II (NOS-II), generating carbon monoxide and nitric oxide respectively, as modulators of liver injury in an experimental model of reversible hemorrhagic shock. Carbon Monoxide 164-179 heme oxygenase 1 Rattus norvegicus 62-100 10628624-1 1999 OBJECTIVE: To investigate the role of the vasodilator systems heme oxygenase-1/heat shock protein 32 (HO-1/HSP32) and nitric oxide synthase-II (NOS-II), generating carbon monoxide and nitric oxide respectively, as modulators of liver injury in an experimental model of reversible hemorrhagic shock. Carbon Monoxide 164-179 heme oxygenase 1 Rattus norvegicus 102-106 10628624-1 1999 OBJECTIVE: To investigate the role of the vasodilator systems heme oxygenase-1/heat shock protein 32 (HO-1/HSP32) and nitric oxide synthase-II (NOS-II), generating carbon monoxide and nitric oxide respectively, as modulators of liver injury in an experimental model of reversible hemorrhagic shock. Carbon Monoxide 164-179 heme oxygenase 1 Rattus norvegicus 107-112 10628624-12 1999 Both metabolites generated by the heme oxygenase pathway, e.g., carbon monoxide (a vasodilator) and biliverdin (an antioxidant) seem to contribute to the salutary effects of induction of HO-1/HSP32. Carbon Monoxide 64-79 heme oxygenase 1 Rattus norvegicus 187-191 10628624-12 1999 Both metabolites generated by the heme oxygenase pathway, e.g., carbon monoxide (a vasodilator) and biliverdin (an antioxidant) seem to contribute to the salutary effects of induction of HO-1/HSP32. Carbon Monoxide 64-79 heme oxygenase 1 Rattus norvegicus 192-197 10564116-0 1999 Carbon monoxide overproduced by heme oxygenase-1 causes a reduction of vascular resistance in perfused rat liver. Carbon Monoxide 0-15 heme oxygenase 1 Rattus norvegicus 32-48 10548545-1 1999 Haem oxygenase-1 (HO-1) is a highly inducible stress protein that removes haem from cells with the release of biliverdin, carbon monoxide and low-molecular-mass iron (LMrFe). Carbon Monoxide 122-137 heme oxygenase 1 Rattus norvegicus 0-22 10564116-1 1999 This study aimed to examine whether livers overexpressing heme oxygenase (HO)-1 could alter the vascular resistance through the vasorelaxing action of carbon monoxide (CO). Carbon Monoxide 151-166 heme oxygenase 1 Rattus norvegicus 58-79 10559009-1 1999 Recent studies indicate that vascular smooth muscle cells (VSMCs) generate CO from the degradation of heme by the enzyme heme oxygenase-1 (HO-1). Carbon Monoxide 75-77 heme oxygenase 1 Rattus norvegicus 121-137 10559009-1 1999 Recent studies indicate that vascular smooth muscle cells (VSMCs) generate CO from the degradation of heme by the enzyme heme oxygenase-1 (HO-1). Carbon Monoxide 75-77 heme oxygenase 1 Rattus norvegicus 139-143 10564116-1 1999 This study aimed to examine whether livers overexpressing heme oxygenase (HO)-1 could alter the vascular resistance through the vasorelaxing action of carbon monoxide (CO). Carbon Monoxide 168-170 heme oxygenase 1 Rattus norvegicus 58-79 9721696-1 1998 Heme oxygenase (HO)-1 generates CO, a gas with vasodilatory properties, during heme metabolism. Carbon Monoxide 32-34 heme oxygenase 1 Rattus norvegicus 0-21 10213906-13 1999 Our results demonstrate, however, that the induction of HO-1 causes vasodepression, possibly via increased production of carbon monoxide. Carbon Monoxide 121-136 heme oxygenase 1 Rattus norvegicus 56-60 9734480-0 1998 Heme oxygenase-1-derived carbon monoxide contributes to the suppression of acute hypertensive responses in vivo. Carbon Monoxide 25-40 heme oxygenase 1 Rattus norvegicus 0-16 9734404-4 1998 The anti-inflammatory properties of HO-1 are thought to rely on the ability of this enzyme to degrade heme and generate bilirubin, free iron and carbon monoxide. Carbon Monoxide 145-160 heme oxygenase 1 Rattus norvegicus 36-40 9684983-8 1998 The physiological relevance of HO-1 induction might be an adaptive response to oxidative stress and vasodilatory effect of carbon monoxide on sinusoidal circulation. Carbon Monoxide 123-138 heme oxygenase 1 Rattus norvegicus 31-35 9498842-1 1998 The heme oxygenase-1 gene, HO-1, induced by heme, ischemia, and heat shock, metabolizes heme to biliverdin, free iron, and carbon monoxide. Carbon Monoxide 123-138 heme oxygenase 1 Rattus norvegicus 4-20 9498842-1 1998 The heme oxygenase-1 gene, HO-1, induced by heme, ischemia, and heat shock, metabolizes heme to biliverdin, free iron, and carbon monoxide. Carbon Monoxide 123-138 heme oxygenase 1 Rattus norvegicus 27-31 9507213-11 1998 Possible mechanisms by which HO-1 ameliorates disease include anti-complement or anti-oxidant effects of bilirubin and vasodilator and anti-platelet effects of carbon monoxide. Carbon Monoxide 160-175 heme oxygenase 1 Rattus norvegicus 29-33 9249506-7 1997 These results demonstrate that cAMP induces the expression of the HO-1 gene and stimulates the formation of CO and NO in vascular smooth muscle cells. Carbon Monoxide 108-110 heme oxygenase 1 Rattus norvegicus 66-70 9508041-3 1998 There are also a constitutive heme oxygenase (HO2) and an inducible form (HO1) which generate CO. Carbon Monoxide 94-96 heme oxygenase 1 Rattus norvegicus 74-77 9385081-15 1997 In its anabolic role, as noted above, heme oxygenase produces bile pigments, carbon monoxide, and iron, all of which are biologically active: bile pigments function as antioxidants; the carbon monoxide generated by HO activity has been correlated with the generation of cGMP; and iron regulates expression of various genes, including that of HO-1 itself, as well as transferrin receptors, ferritin, and NO synthase. Carbon Monoxide 77-92 heme oxygenase 1 Rattus norvegicus 342-346 9385081-15 1997 In its anabolic role, as noted above, heme oxygenase produces bile pigments, carbon monoxide, and iron, all of which are biologically active: bile pigments function as antioxidants; the carbon monoxide generated by HO activity has been correlated with the generation of cGMP; and iron regulates expression of various genes, including that of HO-1 itself, as well as transferrin receptors, ferritin, and NO synthase. Carbon Monoxide 186-201 heme oxygenase 1 Rattus norvegicus 342-346 8562688-2 1995 HO-2, together with HO-1 (HSP32), catalyzes oxidative cleavage of the heme molecule to biliverdin, carbon monoxide, and iron; HO-2 is the major isozyme of the testis. Carbon Monoxide 99-114 heme oxygenase 1 Rattus norvegicus 20-24 8950091-1 1996 Haem oxygenase-1 (HO-1) is a stress protein and a rate-limiting enzyme in haem degradation, generating ferrous iron, carbon monoxide and bile pigments. Carbon Monoxide 117-132 heme oxygenase 1 Rattus norvegicus 0-22 8950091-10 1996 These observations show a long-term induction of HO-1 protein and its activity following ischaemia-reperfusion brain injury, and indicate increased capacity for haem degradation and the generation of biologically active bile products, carbon monoxide and iron in astrocytes and some microglia/macrophages during focal brain ischaemia. Carbon Monoxide 235-250 heme oxygenase 1 Rattus norvegicus 49-53 8769112-1 1996 In this study the effect of increased nitric oxide (NO) production on the expression of rat liver heme oxygenase-1, an inducible stress protein responsible for the catalysis of heme to biliverdin and carbon monoxide, was investigated. Carbon Monoxide 200-215 heme oxygenase 1 Rattus norvegicus 98-114 8667253-3 1996 HO-1 is a stress protein (HSP32) and, together with HO-2, catalyzes oxidation of the heme molecule to generate CO, a likely signal molecule for the generation of cGMP, and bilirubin, an antioxidant. Carbon Monoxide 111-113 heme oxygenase 1 Rattus norvegicus 0-4 8667253-3 1996 HO-1 is a stress protein (HSP32) and, together with HO-2, catalyzes oxidation of the heme molecule to generate CO, a likely signal molecule for the generation of cGMP, and bilirubin, an antioxidant. Carbon Monoxide 111-113 heme oxygenase 1 Rattus norvegicus 26-31 8562688-2 1995 HO-2, together with HO-1 (HSP32), catalyzes oxidative cleavage of the heme molecule to biliverdin, carbon monoxide, and iron; HO-2 is the major isozyme of the testis. Carbon Monoxide 99-114 heme oxygenase 1 Rattus norvegicus 26-31 8584240-8 1995 Since heme is a potent inducer of HO-1, it is likely that the subarachnoid and/or intraparenchymal blood induced HO-1 in the glia where the heme was metabolized to biliverdin, iron, and carbon monoxide. Carbon Monoxide 186-201 heme oxygenase 1 Rattus norvegicus 113-117 7519667-1 1994 Heme oxygenase (HO)-1 and -2 produce carbon monoxide, which is suspected, as is nitric oxide (NO), to function as a neuronal messenger. Carbon Monoxide 37-52 heme oxygenase 1 Rattus norvegicus 0-28 7534336-1 1995 Activity of the stress protein, heme oxygenase-1 (hsp32; HO-1), produces carbon monoxide (CO), the potential messenger molecule for excitatory N-methyl-D-aspartate receptor-mediated events, in the hippocampus. Carbon Monoxide 73-88 heme oxygenase 1 Rattus norvegicus 32-48 7534336-1 1995 Activity of the stress protein, heme oxygenase-1 (hsp32; HO-1), produces carbon monoxide (CO), the potential messenger molecule for excitatory N-methyl-D-aspartate receptor-mediated events, in the hippocampus. Carbon Monoxide 73-88 heme oxygenase 1 Rattus norvegicus 50-55 7534336-1 1995 Activity of the stress protein, heme oxygenase-1 (hsp32; HO-1), produces carbon monoxide (CO), the potential messenger molecule for excitatory N-methyl-D-aspartate receptor-mediated events, in the hippocampus. Carbon Monoxide 73-88 heme oxygenase 1 Rattus norvegicus 57-61 7534336-1 1995 Activity of the stress protein, heme oxygenase-1 (hsp32; HO-1), produces carbon monoxide (CO), the potential messenger molecule for excitatory N-methyl-D-aspartate receptor-mediated events, in the hippocampus. Carbon Monoxide 90-92 heme oxygenase 1 Rattus norvegicus 32-48 7534336-1 1995 Activity of the stress protein, heme oxygenase-1 (hsp32; HO-1), produces carbon monoxide (CO), the potential messenger molecule for excitatory N-methyl-D-aspartate receptor-mediated events, in the hippocampus. Carbon Monoxide 90-92 heme oxygenase 1 Rattus norvegicus 50-55 7534336-1 1995 Activity of the stress protein, heme oxygenase-1 (hsp32; HO-1), produces carbon monoxide (CO), the potential messenger molecule for excitatory N-methyl-D-aspartate receptor-mediated events, in the hippocampus. Carbon Monoxide 90-92 heme oxygenase 1 Rattus norvegicus 57-61 7877760-7 1994 Assuming that the observed increase in mRNA levels is paralled by increased HO-1 protein synthesis, formation of the products of HO reaction, biliverdin and carbon monoxide, is activated after ischemia. Carbon Monoxide 157-172 heme oxygenase 1 Rattus norvegicus 76-80 8148372-1 1994 Heme oxygenase isozymes, HO-1 and HO-2, catalyze the cleavage of heme b (Fe-protoporphyrin-IX) at the alpha-meso carbon bridge to form the antioxidant, biliverdin IX alpha, and the putative cellular messenger, carbon monoxide. Carbon Monoxide 210-225 heme oxygenase 1 Rattus norvegicus 25-38 8360669-1 1993 Two heme oxygenase (HO) isozymes--HO-1, which is a heat shock protein (HSP32), and HO-2--catalyze the isomer-specific production of biliverdin IX alpha and carbon monoxide. Carbon Monoxide 156-171 heme oxygenase 1 Rattus norvegicus 34-38 8360669-1 1993 Two heme oxygenase (HO) isozymes--HO-1, which is a heat shock protein (HSP32), and HO-2--catalyze the isomer-specific production of biliverdin IX alpha and carbon monoxide. Carbon Monoxide 156-171 heme oxygenase 1 Rattus norvegicus 71-76 8455037-1 1993 In mammalian systems, the heme oxygenase (HO) isozymes HO-1 (HSP32) and HO-2 oxidatively cleave the heme molecule to produce bile pigments and carbon monoxide. Carbon Monoxide 143-158 heme oxygenase 1 Rattus norvegicus 55-59 19912899-1 1992 Heme oxygenase isozymes, HO-1 (HSP32) and HO-2, stereospecifically bind and degrade the potent prooxidant, the heme molecule, and convert it to the effective antioxidant, biliverdin, and the potential cellular messenger, carbon monoxide. Carbon Monoxide 221-236 heme oxygenase 1 Rattus norvegicus 25-29 19912899-1 1992 Heme oxygenase isozymes, HO-1 (HSP32) and HO-2, stereospecifically bind and degrade the potent prooxidant, the heme molecule, and convert it to the effective antioxidant, biliverdin, and the potential cellular messenger, carbon monoxide. Carbon Monoxide 221-236 heme oxygenase 1 Rattus norvegicus 31-36