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Biochem Biophys Res Commun. 2006 Oct 20;349(2):869-73. Epub 2006 Aug 31.

Reduction of Nomega-hydroxy-L-arginine to L-arginine by pig liver microsomes, mitochondria, and human liver microsomes.

Author information

1
Pharmazeutisches Institut, Christian-Albrechts-Universit├Ąt zu Kiel, Gutenbergstrasse 76, D-24118 Kiel, Germany. bclement@pharmazie.uni-kiel.de

Abstract

Nomega-Hydroxy-L-arginine, the intermediate in nitric oxide formation from L-arginine catalyzed by NO synthase, can be released into the extracellular space. It has been suggested that it can circulate and exert paracrine effects. Since it cannot only be used as substrate by NO synthases, but can also be oxidized by cytochrome P450 and other hemoproteins in a superoxide-dependent manner, it has been proposed that it can serve as NO donor. In the present study, the in vitro reduction of Nomega-hydroxy-L-arginine was examined. Pig and human liver microsomes as well as pig liver mitochondria were capable of reducing Nomega-hydroxy-L-arginine to L-arginine in an oxygen-insensitive enzymatic reaction. These results demonstrate that this metabolic pathway has to be considered when suggesting Nomega-hydroxy-L-arginine as NO-precursor. The reconstituted liver microsomal system of a pig liver CYP2D enzyme, the benzamidoxime reductase, was unable to replace microsomes to produce L-arginine from Nomega-hydroxy-L-arginine.

PMID:
16959215
DOI:
10.1016/j.bbrc.2006.08.123
[Indexed for MEDLINE]

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