Invited Symposium: Carbon Monoxide and Cardiovascular Function
Kozma, F (Second Department of Physiology, Semmelweis Medical University-Budapest, Hungary)
Heme oxygenase is a widely distributed enzyme which catalyzes the conversion of monomeric free heme to iron, biliverdin and carbon monoxide. A seminal work by Gerald Marks noted the ability of carbon monoxide to promote endothelium-independent relaxation of vascular smooth muscle and boldly forwarded the suggestion that heme-derived carbon monoxide may exert similar actions to contribute to vascular tone. Indeed, that suggestion has served as an impetus to many, like ourselves, to explore the potential biological actions of this well-established heme-heme oxygenase carbon monoxide system. Evidence is currently mounting to strongly suggest that heme-derived carbon monoxide can exert a vasodilatory influence on vascular preparations, but there has been little effort to isolate the role of endothelium as it participates in this process. Indeed the endothelium is a rich source of autacoid and vasoactive hormones, many of which are derived from carbon monoxide-sensitive heme-bearing enzymes, that may potentially contribute to the vascular actions of heme-derived carbon monoxide. The aim of this presentation, is to highlight the potential vasoactive contribution of the endothelium, as it may impact on the vascular functions arising from the heme-heme oxygenase-carbon monoxide system.
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|Johnson, RA; Kozma, F; (1998). Endothelial-Dependent and -Independent Actions of Heme and Carbon Monoxide on Vascular Tone. Presented at INABIS '98 - 5th Internet World Congress on Biomedical Sciences at McMaster University, Canada, Dec 7-16th. Invited Symposium. Available at URL http://www.mcmaster.ca/inabis98/wang/johnson0831/index.html|
|© 1998 Author(s) Hold Copyright|