Contractile and Vasorelaxant Effects of Hydrogen Sulfide and Its Biosynthesis in the Human Internal Mammary Artery
| Autor: | Muhammed Yusuf Ali, Elizabeth A. Taylor, Chuen Neng Lee, Vernon M S Oh, George D. Webb, Edwin S. Y. Chan, Michael George Caleb, Reida El Oakley, Poo-Sing Wong, Soh Bee Yeo, Madhav Bhatia, Philip K. Moore, Lay Har Lim, Manuel Salto-Tellez, Yoke Ping Cheong |
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| Rok vydání: | 2007 |
| Předmět: |
Contraction (grammar)
Vasodilator Agents Internal thoracic artery Nitric oxide Glibenclamide chemistry.chemical_compound medicine.artery parasitic diseases Humans Medicine Hydrogen Sulfide Mammary Arteries Pharmacology biology business.industry Cystathionine gamma-Lyase Anatomy Cystathionine beta synthase Molecular biology Vasodilation Blot medicine.anatomical_structure chemistry Vasoconstriction biology.protein Molecular Medicine business Cysteine medicine.drug Artery |
| Zdroj: | Journal of Pharmacology and Experimental Therapeutics. 324:876-882 |
| ISSN: | 1521-0103 0022-3565 |
| DOI: | 10.1124/jpet.107.133538 |
| Popis: | This study aimed to test these hypotheses: cystathionine gamma-lyase (CSE) is expressed in a human artery, it generates hydrogen sulfide (H(2)S), and H(2)S relaxes a human artery. H(2)S is produced endogenously in rat arteries from cysteine by CSE. Endogenously produced H(2)S dilates rat resistance arteries. Although CSE is expressed in rat arteries, its presence in human blood vessels has not been described. In this study, we showed that both CSE mRNA, determined by reverse transcription-polymerase chain reaction, and CSE protein, determined by Western blotting, apparently occur in the human internal mammary artery (internal thoracic artery). Artery homogenates converted cysteine to H(2)S, and the H(2)S production was inhibited by dl-propargylglycine, an inhibitor of CSE. We also showed that H(2)S relaxes phenylephrine-precontracted human internal mammary artery at higher concentrations but produces contraction at low concentrations. The latter contractions are stronger in acetylcholine-prerelaxed arteries, suggesting inhibition of nitric oxide action. The relaxation is partially blocked by glibenclamide, an inhibitor of K(ATP) channels. The present results indicate that CSE protein is expressed in human arteries, that human arteries synthesize H(2)S, and that higher concentrations of H(2)S relax human arteries, in part by opening K(ATP) channels. Low concentrations of H(2)S contract the human internal mammary artery, possibly by reacting with nitric oxide to form an inactive nitrosothiol. The possibility that CSE, and the H(2)S it generates, together play a physiological role in regulating the diameter of arteries in humans, as has been demonstrated in rats, should be considered. |
| Databáze: | OpenAIRE |
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