Hydrogen peroxide elicits activation of bovine pulmonary arterial soluble guanylate cyclase by a mechanism associated with its metabolism by catalase |
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| Authors: | M S Wolin T M Burke |
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| Affiliation: | 1. Department of Anesthesia, Critical Care and Pain Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA, USA;2. Department of Bioscience, College of Life and Environmental Science, University of Exeter, UK;3. University of Exeter Medical School, St. Luke’s Campus, Exeter, England, UK |
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| Abstract: | ![]()
Guanylate cyclase activity in the soluble extract of bovine pulmonary arteries is activated by hydrogen peroxide generated by glucose oxidase only in the presence of catalase. This mechanism of guanylate cyclase activation is not blocked by scavengers for superoxide anion or hydroxyl radical, but is selectively inhibited by methylene blue, inactivation of catalase and ethanol. The time dependency of increases in guanylate cyclase activity in the presence of peroxides that are substrates for catalase are associated with the spectral detection of compound I, a species of catalase formed during the metabolism of peroxide. Thus, activation of soluble guanylate cyclase appears to be elicited by compound I of catalase or by a mediator generated by this species. |
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