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• W2053179924 abstract "Beyond its vasodilator role, vascular nitric oxide (NO), which is synthesized by endothelial NO synthase (eNOS) via its activation, has been shown to play a number of other beneficial roles in the vascular system; it inhibits proliferation of vascular smooth muscle cells, prevents platelet aggregation, and regulates endothelial apoptosis. Such beneficial roles have been shown to be implicated in the regulation of endothelial functions. A loss of NO bioavailability that may result either from decreased eNOS expression and activity or from increased NO degradation is associated with endothelial dysfunction, a key factor in the development of vascular diseases. Heme oxygenase-1 (HO-1), an inducible enzyme, catalyzes the oxidative degradation of heme to free iron, carbon monoxide, and biliverdin, the latter being subsequently converted into bilirubin. In the vascular system, HO-1 and heme degradation products perform important physiological functions, which are ultimately linked to the protection of vascular cells. Studies have shown that HO-1 and heme degradation products exert vasodilatory, antioxidant, anti-inflammatory, antiproliferative and anti-apoptotic effects on vascular cells. Interestingly, these effects of HO-1 and its by-products are similar, at least in part, to those of eNOS-derived NO; this similarity may prompt investigators to study a possible relationship between eNOS-derived NO and HO-1 pathways. Many studies have been reported, and accumulating evidence suggests that HO-1 and heme degradation products can improve vascular function, at least in part, by compensating for the loss of NO bioavailability. This paper will provide the possible pathway explaining how HO-1 and heme degradation products can preserve vascular NO." @default.
• W2053179924 created "2016-06-24" @default.
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• W2053179924 creator A5087588859 @default.
• W2053179924 creator A5090068470 @default.
• W2053179924 date "2010-12-01" @default.
• W2053179924 modified "2023-10-16" @default.
• W2053179924 title "Role of heme oxygenase in preserving vascular bioactive NO" @default.
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• W2053179924 doi "https://doi.org/10.1016/j.niox.2010.08.002" @default.
• W2053179924 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20713168" @default.
• W2053179924 hasPublicationYear "2010" @default.
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