PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34346143-0 2021 Arbutin attenuates ethanol-induced acute hepatic injury by the modulation of oxidative stress and Nrf-2/HO-1 signaling pathway. Ethanol 19-26 heme oxygenase 1 Homo sapiens 104-108 34346143-12 2021 Arbutin triggered Nrf-2/HO-1 signaling cascade liver tissues of ethanol-provoked animals. Ethanol 64-71 heme oxygenase 1 Homo sapiens 24-28 30974805-0 2019 Ethanol-Mediated Stress Promotes Autophagic Survival and Aggressiveness of Colon Cancer Cells via Activation of Nrf2/HO-1 Pathway. Ethanol 0-7 heme oxygenase 1 Homo sapiens 117-121 33035580-6 2020 Production of CYP2E1, Nrf2 and HO-1, which produced in response to increased oxidative stress, were regulated in TAR treated, ethanol-induced hepatocytes. Ethanol 126-133 heme oxygenase 1 Homo sapiens 31-35 33747471-0 2021 Intracellular ethanol-mediated oxidation and apoptosis in HepG2/CYP2E1 cells impaired by two active peptides from seahorse (Hippocampus kuda bleeler) protein hydrolysates via the Nrf2/HO-1 and akt pathways. Ethanol 14-21 heme oxygenase 1 Homo sapiens 184-188 30974805-6 2019 EtOH treatment also upregulates the antioxidant enzymes SOD, catalase, and heme oxygenase (HO-1) and promotes the nuclear translocation of both Nrf2 and HO-1. Ethanol 0-4 heme oxygenase 1 Homo sapiens 91-95 30974805-6 2019 EtOH treatment also upregulates the antioxidant enzymes SOD, catalase, and heme oxygenase (HO-1) and promotes the nuclear translocation of both Nrf2 and HO-1. Ethanol 0-4 heme oxygenase 1 Homo sapiens 153-157 30974805-8 2019 Nrf2 silencing or preventing HO-1 nuclear translocation by the protease inhibitor E64d abrogates the EtOH-induced increase in the antioxidant enzyme levels as well as the migration markers. Ethanol 101-105 heme oxygenase 1 Homo sapiens 29-33 30974805-9 2019 Taken together, our results suggest that EtOH mediates both the activation of Nrf2 and HO-1 to sustain colon cancer cell survival, thus leading to the acquisition of a more aggressive phenotype. Ethanol 41-45 heme oxygenase 1 Homo sapiens 87-91 23816986-0 2013 The activation of HO-1/Nrf-2 contributes to the protective effects of diallyl disulfide (DADS) against ethanol-induced oxidative stress. Ethanol 103-110 heme oxygenase 1 Homo sapiens 18-22 26072076-0 2015 Protective effect of HO-1 transfection against ethanol-induced osteoblast damage. Ethanol 47-54 heme oxygenase 1 Homo sapiens 21-25 26072076-2 2015 The aim of this study was to observe if HO-1 transfection could inhibit the damage of osteoblasts induced by ethanol. Ethanol 109-116 heme oxygenase 1 Homo sapiens 40-44 26072076-8 2015 These results suggest that HO-1 plays a protective role in osteoblasts, and HO-1 transfection can effectively inhibit bone damage induced by ethanol. Ethanol 141-148 heme oxygenase 1 Homo sapiens 76-80 23816986-12 2013 CONCLUSION: These results demonstrate that DADS could induce the activation of HO-1/Nrf-2 pathway, which may contribute to the protective effects of DADS against ethanol-induced liver injury. Ethanol 162-169 heme oxygenase 1 Homo sapiens 79-83 23412940-10 2013 The data suggest that ethanol-induced upregulation of HO-1 in oesophageal squamous cell carcinoma is accompanied by the activation of the p38MAPK and mTOR pathways. Ethanol 22-29 heme oxygenase 1 Homo sapiens 54-58 23583009-9 2013 CO donor dose-dependently inactivated CYP2E1 of ethanol-incubated microsome, which was mimicked by HO-1 substrate but abolished by CO scavenger. Ethanol 48-55 heme oxygenase 1 Homo sapiens 99-103 23583009-10 2013 Thus, CYP2E1-mediated ethanol hepatotoxicity was alleviated by quercetin through HO-1 induction. Ethanol 22-29 heme oxygenase 1 Homo sapiens 81-85 23583009-2 2013 However, the precise mechanism by which quercetin counteracts CYP2E1-mediated ethanol hepatotoxicity through HO-1 system is still remained unclear. Ethanol 78-85 heme oxygenase 1 Homo sapiens 109-113 23583009-5 2013 Our data showed that chronic ethanol over-activated CYP2E1 but suppressed HO-1 with concurrent hepatic oxidative damage, which was partially normalized by quercetin (100mg/kg.bw.). Ethanol 29-36 heme oxygenase 1 Homo sapiens 74-78 23583009-7 2013 Ethanol-stimulated (100mM) CYP2E1 upregulation was suppressed by quercetin but further enhanced by HO-1 inhibition with resultant heme accumulation. Ethanol 0-7 heme oxygenase 1 Homo sapiens 99-103 22484158-7 2012 Interestingly, the profound up-regulation of HO-1 and Nrf-2 were observed in only ethanol-challenged cells, which evidenced that lucidone-induced induction of HO-/Nrf-2 were specific with oxidative stress. Ethanol 82-89 heme oxygenase 1 Homo sapiens 45-49 23412940-8 2013 HO-1 expression was upregulated in the presence of ethanol, and was accompanied by activation of p38MAPK and mTOR. Ethanol 51-58 heme oxygenase 1 Homo sapiens 0-4 23412940-9 2013 However, ethanol-treated cells exposed to HO-1 inhibitor showed no effect on p38MAPK and mTOR activation. Ethanol 9-16 heme oxygenase 1 Homo sapiens 42-46 22842631-0 2012 Globular adiponectin inhibits ethanol-induced apoptosis in HepG2 cells through heme oxygenase-1 induction. Ethanol 30-37 heme oxygenase 1 Homo sapiens 79-95 22842631-8 2012 Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells. Ethanol 244-251 heme oxygenase 1 Homo sapiens 75-79 22842631-8 2012 Treatment with SnPP, a pharmacological inhibitor of HO-1, and knockdown of HO-1 with small interfering RNA (siRNA) restored caspase-3 activity suppressed by gAcrp, indicating a critical role of HO-1 in mediating the protective role of gAcrp in ethanol-induced apoptosis in liver cells. Ethanol 244-251 heme oxygenase 1 Homo sapiens 75-79 22842631-10 2012 In conclusion, these data demonstrated that globular adiponectin prevents ethanol-induced apoptosis in HepG2 cells via HO-1 induction and revealed a novel biological response of globular adiponectin in the protection of liver injury from alcohol consumption. Ethanol 74-81 heme oxygenase 1 Homo sapiens 119-123 22484158-6 2012 Furthermore, Western blot and quantitative-PCR analyses showed that ethanol-exposure apparently down-regulated endogenous anti-oxidant hemoxygenase-1 (HO-1) expression, whereas pretreatment with lucidone significantly up-regulates HO-1 expression followed by the transcriptional activation of NF-E2 related factor-2 (Nrf-2). Ethanol 68-75 heme oxygenase 1 Homo sapiens 135-155 22484158-6 2012 Furthermore, Western blot and quantitative-PCR analyses showed that ethanol-exposure apparently down-regulated endogenous anti-oxidant hemoxygenase-1 (HO-1) expression, whereas pretreatment with lucidone significantly up-regulates HO-1 expression followed by the transcriptional activation of NF-E2 related factor-2 (Nrf-2). Ethanol 68-75 heme oxygenase 1 Homo sapiens 151-155 20833713-3 2010 We showed that Kupffer cells from ethanol-fed rats and ethanol-treated rat Kupffer cells and THP-1 cells displayed increased mRNA expression of HO-1, NQO1, and hypoxia-inducible factor-1alpha (HIF-1alpha). Ethanol 34-41 heme oxygenase 1 Homo sapiens 144-148 20833713-3 2010 We showed that Kupffer cells from ethanol-fed rats and ethanol-treated rat Kupffer cells and THP-1 cells displayed increased mRNA expression of HO-1, NQO1, and hypoxia-inducible factor-1alpha (HIF-1alpha). Ethanol 55-62 heme oxygenase 1 Homo sapiens 144-148 21146245-7 2011 Indeed, in CYP2E1-expressing HepG2 cells exposed to ethanol, the expression of ISR target genes (HMOX-1, GCLC, AsnS, IGFBP-1, GADD34,CHOP, ATF3, CHAC1) was induced. Ethanol 52-59 heme oxygenase 1 Homo sapiens 97-103 19325051-0 2009 The protective role of HO-1 and its generated products (CO, bilirubin, and Fe) in ethanol-induced human hepatocyte damage. Ethanol 82-89 heme oxygenase 1 Homo sapiens 23-27 21525764-9 2010 RESULTS: Ethanol and TGF-beta rapidly increase ROI and reduce GSH in hHeps, causing apoptosis with a release of approximately 40% total LDH after 72 h. Similar to incubation with hemin preincubation and co-incubation of cells with nifedipine, verapamil and quercetin significantly reduce oxidative stress and resulting cellular damage, in a dose-dependent manner, by initiating nuclear translocation of Nrf2 which in turn induces HO-1 under the control of p38 and ERK. Ethanol 9-16 heme oxygenase 1 Homo sapiens 430-434 19325051-9 2009 These results suggested that quercetin virtually attenuated ethanol-derived oxidative damage via HO-1 induction. Ethanol 60-67 heme oxygenase 1 Homo sapiens 97-101 17433488-0 2007 Quercetin protects human hepatocytes from ethanol-derived oxidative stress by inducing heme oxygenase-1 via the MAPK/Nrf2 pathways. Ethanol 42-49 heme oxygenase 1 Homo sapiens 87-103 17225922-9 2007 Micelle formulations prepared with ethanol/Tween40 resulted in the lowest LDH release, the highest carotenoid uptake and the lowest stress response (changes in HO-1 mRNA expression). Ethanol 35-42 heme oxygenase 1 Homo sapiens 160-164 15602829-0 2004 Induction of heme oxygenase-1 in human hepatocytes to protect them from ethanol-induced cytotoxicity. Ethanol 72-79 heme oxygenase 1 Homo sapiens 13-29 15602829-1 2004 UNLABELLED: We investigated the relationship between ethanol exposure and heme oxygenase (HO-1) in human hepatocytes in order to ascertain if induction of HO-1 can prevent ethanol induced cellular damage. Ethanol 53-60 heme oxygenase 1 Homo sapiens 90-94 15602829-1 2004 UNLABELLED: We investigated the relationship between ethanol exposure and heme oxygenase (HO-1) in human hepatocytes in order to ascertain if induction of HO-1 can prevent ethanol induced cellular damage. Ethanol 172-179 heme oxygenase 1 Homo sapiens 155-159 15602829-6 2004 RESULTS: We first demonstrated a dose-dependent response between ethanol exposure and HO-1 mRNA and protein expression in human hepatocytes. Ethanol 65-72 heme oxygenase 1 Homo sapiens 86-90 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. Ethanol 87-94 heme oxygenase 1 Homo sapiens 49-53 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. Ethanol 121-128 heme oxygenase 1 Homo sapiens 49-53 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. Ethanol 121-128 heme oxygenase 1 Homo sapiens 49-53 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. Ethanol 121-128 heme oxygenase 1 Homo sapiens 49-53 15612472-0 2004 [Effect of acute ethanol exposure on HO-1 enzyme activity in human primary hepatocytes]. Ethanol 17-24 heme oxygenase 1 Homo sapiens 37-41 15612472-1 2004 OBJECTIVE: To study the effect of ethanol exposure on the expression of HO-1 enzymes in human primary culture hepatocytes. Ethanol 34-41 heme oxygenase 1 Homo sapiens 72-76 15612472-6 2004 Moreover, we also observed that ethanol exposure could affect HO-1 enzyme activity and HO-1 protein level, at the beginning, it went up significantly then went down. Ethanol 32-39 heme oxygenase 1 Homo sapiens 62-91 15612472-7 2004 CONCLUSION: The increase of HO-1 enzyme activity and protein level after ethanol exposure may be relative to prevent against ethanol-induced oxidative injury in human primary hepatocytes. Ethanol 73-80 heme oxygenase 1 Homo sapiens 28-32 15612472-7 2004 CONCLUSION: The increase of HO-1 enzyme activity and protein level after ethanol exposure may be relative to prevent against ethanol-induced oxidative injury in human primary hepatocytes. Ethanol 125-132 heme oxygenase 1 Homo sapiens 28-32 17295091-0 2007 Heme oxygenase-1 and interleukin-11 are overexpressed in stress-induced premature senescence of human WI-38 fibroblasts induced by tert-butylhydroperoxide and ethanol. Ethanol 159-166 heme oxygenase 1 Homo sapiens 0-16 17295091-2 2007 In the present work we found an increased mRNA and protein level of interleukin-11 and heme oxygenase-1 in premature senescence of WI-38 human diploid foetal lung fibroblasts induced by both tert-butylhydroperoxide and ethanol. Ethanol 219-226 heme oxygenase 1 Homo sapiens 87-103 17295091-3 2007 We tested whether interleukin-11 and heme oxygenase-1 could protect against tert-butylhydroperoxide- or ethanol-induced premature senescence when stable overexpression was established using a retroviral vector-based transduction. Ethanol 104-111 heme oxygenase 1 Homo sapiens 37-53 15602829-11 2004 CONCLUSION: HO-1 expression in cells or organs could lead to new strategies for better prevention and treatment of ethanol-induced oxidative damage in human liver. Ethanol 115-122 heme oxygenase 1 Homo sapiens 12-16