The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Induction of Heme Oxygenase-1 Inhibits NAD(P)H Oxidase Activity by Down-regulating Cytochrome b558 Expression via the Reduction of Heme Availability
Open accessAbstract
Heme-oxygenase-1 (HO-1), the rate-limiting enzyme of heme degradation, has powerful anti-oxidant properties related to the production of the reactive oxygen species scavenger bilirubin. However, some data suggest that HO-1 could also inhibit the cellular production of reactive oxygen species. Therefore, we investigated whether the anti-oxidant properties of HO-1 could be mediated by modulation of the activity and/or expression of the heme-containing NAD(P)H oxidase, the main source of the superoxide anion (O(2)(-)) in phagocytic cells. Increasing HO-1 expression in RAW 264.7 macrophages effectively decreased NAD(P)H oxidase activity and expression of gp91(phox), its heme-containing catalytic component, because of deficient protein maturation and increased degradation. Loading cells with heme reversed the decrease in O(2)(-) production and gp91(phox) expression induced by HO-1 overexpression. Similar results were obtained in vivo in rat alveolar macrophages after pharmacological modulation of HO-1 expression or activity. These results show that a decrease in heme content due to HO-1 activation limits heme availability for maturation of the gp91(phox) subunit and assembly of the functional NAD(P)H oxidase. This study provides a new mechanism to explain HO-1 anti-oxidant properties.
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Cites
Gp91 phox is the heme binding subunit of the superoxide-generating NADPH oxidase
Yu, L., Quinn, M. T., Cross, A. R., & Dinauer, M. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.7993 · Cited by 202
Cited by
Simpson, D. S. A., & Oliver, P. L. (2020) · Antioxidants · doi:10.3390/antiox9080743 · Cited by 1,044
“This was mediated by both a reduction in heme availability and biliverdin and carbon monoxide, by-products of heme metabolism by HO-1 which may facilitate attenuation of TLR4 signalling by NOX inhibition [173,174].”
BackgroundCarbon Monoxide: Endogenous Production, Physiological Functions, and Pharmacological Applications
Wu, L., & Wang, R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.3 · Cited by 962
Oxidative stress in vascular disease: causes, defense mechanisms and potential therapies
Förstermann, U. (2008) · Nature Clinical Practice Cardiovascular Medicine · doi:10.1038/ncpcardio1211 · Cited by 576
Macrophages and Iron Metabolism
Soares, M. P., & Hamza, I. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.016 · Cited by 401
Momen-Heravi, F., Bala, S., Kodys, K., & Szabo, G. (2015) · Scientific Reports · doi:10.1038/srep09991 · Cited by 347
Metadata
- Authors
- Taillé, C., El-Benna, J., Lanone, S., Dang, M.-C., Ogier-Denis, E., Aubier, M., & Boczkowski, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-07
- Volume
- 279
- Issue
- 27
- Pages
- 28681-28688
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2165088386
- Cited by
- 181
- References
- 1
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- The paper
- Taillé, C., El-Benna, J., Lanone, S., Dang, M.-C., Ogier-Denis, E., Aubier, M., & Boczkowski, J. (2004). Induction of Heme Oxygenase-1 Inhibits NAD(P)H Oxidase Activity by Down-regulating Cytochrome b558 Expression via the Reduction of Heme Availability. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m310661200
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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