Heme oxygenase-1 and carbon monoxide in pulmonary medicine
Heme oxygenase-1 (HO-1), an inducible stress protein, confers cytoprotection against oxidative stress in vitro and in vivo. In addition to its physiological role in heme degradation, HO-1 may influence a number of cellular processes, including growth, inflammation, and apoptosis. By virtue of anti-i...
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BioMed Central
2003
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC193681/ |
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pubmed-1936812003-09-15 Heme oxygenase-1 and carbon monoxide in pulmonary medicine Slebos, Dirk-Jan Ryter, Stefan W Choi, Augustine MK Review Heme oxygenase-1 (HO-1), an inducible stress protein, confers cytoprotection against oxidative stress in vitro and in vivo. In addition to its physiological role in heme degradation, HO-1 may influence a number of cellular processes, including growth, inflammation, and apoptosis. By virtue of anti-inflammatory effects, HO-1 limits tissue damage in response to proinflammatory stimuli and prevents allograft rejection after transplantation. The transcriptional upregulation of HO-1 responds to many agents, such as hypoxia, bacterial lipopolysaccharide, and reactive oxygen/nitrogen species. HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXα, ferrous iron, and carbon monoxide (CO). The mechanisms by which HO-1 provides protection most likely involve its enzymatic reaction products. Remarkably, administration of CO at low concentrations can substitute for HO-1 with respect to anti-inflammatory and anti-apoptotic effects, suggesting a role for CO as a key mediator of HO-1 function. Chronic, low-level, exogenous exposure to CO from cigarette smoking contributes to the importance of CO in pulmonary medicine. The implications of the HO-1/CO system in pulmonary diseases will be discussed in this review, with an emphasis on inflammatory states. BioMed Central 2003 2003-08-07 /pmc/articles/PMC193681/ /pubmed/12964953 http://dx.doi.org/10.1186/1465-9921-4-7 Text en Copyright © 2003 Slebos et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Slebos, Dirk-Jan Ryter, Stefan W Choi, Augustine MK |
| spellingShingle |
Slebos, Dirk-Jan Ryter, Stefan W Choi, Augustine MK Heme oxygenase-1 and carbon monoxide in pulmonary medicine |
| author_facet |
Slebos, Dirk-Jan Ryter, Stefan W Choi, Augustine MK |
| author_sort |
Slebos, Dirk-Jan |
| title |
Heme oxygenase-1 and carbon monoxide in pulmonary medicine |
| title_short |
Heme oxygenase-1 and carbon monoxide in pulmonary medicine |
| title_full |
Heme oxygenase-1 and carbon monoxide in pulmonary medicine |
| title_fullStr |
Heme oxygenase-1 and carbon monoxide in pulmonary medicine |
| title_full_unstemmed |
Heme oxygenase-1 and carbon monoxide in pulmonary medicine |
| title_sort |
heme oxygenase-1 and carbon monoxide in pulmonary medicine |
| description |
Heme oxygenase-1 (HO-1), an inducible stress protein, confers cytoprotection against oxidative stress in vitro and in vivo. In addition to its physiological role in heme degradation, HO-1 may influence a number of cellular processes, including growth, inflammation, and apoptosis. By virtue of anti-inflammatory effects, HO-1 limits tissue damage in response to proinflammatory stimuli and prevents allograft rejection after transplantation. The transcriptional upregulation of HO-1 responds to many agents, such as hypoxia, bacterial lipopolysaccharide, and reactive oxygen/nitrogen species. HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXα, ferrous iron, and carbon monoxide (CO). The mechanisms by which HO-1 provides protection most likely involve its enzymatic reaction products. Remarkably, administration of CO at low concentrations can substitute for HO-1 with respect to anti-inflammatory and anti-apoptotic effects, suggesting a role for CO as a key mediator of HO-1 function. Chronic, low-level, exogenous exposure to CO from cigarette smoking contributes to the importance of CO in pulmonary medicine. The implications of the HO-1/CO system in pulmonary diseases will be discussed in this review, with an emphasis on inflammatory states. |
| publisher |
BioMed Central |
| publishDate |
2003 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC193681/ |
| _version_ |
1611367275973050368 |