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Eur J Pharmacol. 1993 Mar 16;233(1):119-25.

Selective inhibition of the inducible nitric oxide synthase by aminoguanidine.

Author information

1
Department of Molecular Pharmacology, Monsanto Corporate Research, St. Louis, MO 63167.

Abstract

Overproduction of the free radical nitric oxide (NO) has been implicated in the pathogenesis of a variety of inflammatory and immunologically mediated diseases as well as complications of diabetes. In the present study we have demonstrated that aminoguanidine selectively inhibits the cytokine-inducible isoform of NO synthase which appears to be responsible for the excess production of NO linked to these disease states. By using organ, cell, and enzyme-based measurements we have shown that aminoguanidine is equipotent to NG-monomethyl-L-arginine (L-NMA) as an inhibitor of the cytokine-induced isoform of NO synthase but is 10 to 100-fold less potent as an inhibitor of the constitutive isoform. Thus, aminoguanidine may be useful as a selective inhibitor of the inducible NO synthase in the treatment of disease states characterized by the pathological overproduction of NO.

PMID:
7682510
DOI:
10.1016/0014-2999(93)90357-n
[Indexed for MEDLINE]

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