Nitric oxide biosynthesis, nitric oxide synthase inhibitors and arginase competition for L-arginine utilization |
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Authors: | J L Boucher C Moali J P Tenu |
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Institution: | (1) Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, URA 400 CNRS, 45 rue des Saints Pères, F-75270 Paris Cedex 06 (France), Fax +33 1 42 86 83 87, e-mail: boucher@bisance.citi2.fr, FR;(2) ERS 571 CNRS, Bat. 430, Université Paris-Sud XI, F-91405 Orsay Cedex (France), FR |
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Abstract: | Nitric oxide (NO) is a recently discovered mediator produced by mammalian cells. It plays a key role in neurotransmission,
control of blood pressure, and cellular defense mechanisms. Nitric oxide synthases (NOSs) catalyze the oxidation of L-arginine
to NO and L-citrulline. NOSs are unique enzymes in that they possess on the same polypeptidic chain a reductase domain and
an oxygenase domain closely related to cytochrome P450s. NO and superoxide formation as well as NOS stability are finely regulated
by Ca2+/calmodulin interactions, by the cofactor tetrahydrobiopterin, and by substrate availability. Strong interactions between
the L-arginine-metabolizing enzymes are clearly demonstrated by competition between NOSs and arginases for L-arginine utilization,
and by potent inhibition of arginase activity by Nω-hydroxy-L-arginine, an intermediate in the L-arginine to NO pathway. |
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Keywords: | , L-Arginine, nitric oxide, nitric oxide synthase, arginase, urea cycle, Nω,-hydroxy-L-arginine, superoxide radical,,,,,,peroxynitrite, |
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