The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
The heme oxygenase pathway and its interaction with nitric oxide in the control of cellular homeostasis
Abstract
Heme oxygenase is the rate limiting enzyme in heme degradation to carbon monoxide (CO), iron and bilirubin. The inducible isoform of the protein, heme oxygenase-1 (HO-1), is susceptible to up-regulation by a diverse variety of conditions and agents in mammalian tissue, leading to the common conception that HO-1 is a stress related enzyme. However, as attempts are made to unravel the mechanisms by which HO-1 is induced and as we discover that CO, iron and bilirubin may be important effector molecules, we are learning to appreciate that heme oxygenases may be central to the regulation of many physiological and pathophysiological processes besides their established function in heme catabolism. One such process may be closely linked to nitric oxide (NO). It has been demonstrated that NO and NO donors are capable of inducing HO-1 protein expression, in a mechanism depending on the de novo synthesis of RNA and protein. Thus, it is postulated that NO may serve as a signaling molecule in the modulation of the tissue stress response. This review will highlight the current ideas on the role of CO-heme oxygenase and NO-nitric oxide synthase in cell signaling and discuss how the two systems are interrelated.
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Cites
Nitric oxide: physiology, pathophysiology, and pharmacology.
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Biochemistry of nitric oxide and its redox-activated forms
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Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin.
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Inducible Nitric-oxide Synthase Generates Superoxide from the Reductase Domain
Xia, Y., Roman, L. J., Masters, B. S. S., & Zweier, J. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22635 · Cited by 388
Nitrosative stress: Metabolic pathway involving the flavohemoglobin
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Cited by
Carbon 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
Heme Oxygenase-1: The “Emerging Molecule” Has Arrived
Morse, D., & Choi, A. M. K. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.27.1.4862 · Cited by 532
Regulation of inflammation by the antioxidant haem oxygenase 1
Campbell, N. K., Fitzgerald, H. K., & Dunne, A. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-020-00491-x · Cited by 420
Braun, S., Hanselmann, C., Gassmann, M. G., auf dem Keller, U., Born-Berclaz, C., Chan, K., Kan, Y. W., & Werner, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5492-5505.2002 · Cited by 410
Sawle, P., Foresti, R., Mann, B. E., Johnson, T. R., Green, C. J., & Motterlini, R. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706241 · Cited by 391
Metadata
- Authors
- Foresti, R., & Motterlini, R.
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 1999-01
- Volume
- 31
- Issue
- 6
- Pages
- 459-475
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W2006861037
- Cited by
- 274
- References
- 7
- FWCI
- 4.78
- Type
- journal article
- Language
- en
- Open access
- closed
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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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