This study aimed to test these hypotheses: cystathionine ␥-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.

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Neuronal nitric oxide synthase is expressed in the vascular smooth muscle of patients undergoing bypass, and the amount in the internal thoracic artery is the same as in the saphenous vein.