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Arginase activity in endothelial cells: inhibition by NG-hydroxy-L-arginine during high-output NO production

Arginase activity in endothelial cells: inhibition by NG-hydroxy-L-arginine during high-output NO... STUDIES from this laboratory revealed that lipopolysaccharide (LPS) duces the concomitant appearance argase ducible nitric oxide synthase () activities mure macrophage RAW 264.7 cells (42). Negligible activities either enzyme were found unactivated cells, immunoprecipitation experiments revealed that argase-II not argase-I was duced by LPS. At least two distct nonhomologous argase genes exist mammals, their products are termed argase-I argase-II for the hepatic extrahepatic isorms, rePREVIOUS Hl988 0363-6135/96 $5.00 Copyright o 1996 spectively (11, 16). Both argase isorms share certa physicochemical properties but are immunologically distct (26, 39). Because extrahepatic tissues do not possess a complete urea cycle, the function argase-II such tissues is unclear. One function might be the production ornithe, which is a precursor prole, polyames, related substances. Another function argase-II, for example, LPS-activated macrophages, might be to regulate the tracellular arge concentration (8, 14, 32), perhaps by makg less arge available as a substrate for , thereby leadg to dimished production NO (42). To the extent that arge is necessary for expression macrophage-mediated cytotoxicity (22, 24) as the substrate for -catalyzed production cytotoxic quantities NO (23), argase-II duction could dimish the cytotoxic role activated macrophages. However, no clear evidence for this potential mechanism exists. A recent http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Heart and Circulatory Physiology The American Physiological Society

Arginase activity in endothelial cells: inhibition by NG-hydroxy-L-arginine during high-output NO production

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Publisher
The American Physiological Society
Copyright
Copyright © 1996 the American Physiological Society
ISSN
0363-6135
eISSN
1522-1539
Publisher site
See Article on Publisher Site

Abstract

STUDIES from this laboratory revealed that lipopolysaccharide (LPS) duces the concomitant appearance argase ducible nitric oxide synthase () activities mure macrophage RAW 264.7 cells (42). Negligible activities either enzyme were found unactivated cells, immunoprecipitation experiments revealed that argase-II not argase-I was duced by LPS. At least two distct nonhomologous argase genes exist mammals, their products are termed argase-I argase-II for the hepatic extrahepatic isorms, rePREVIOUS Hl988 0363-6135/96 $5.00 Copyright o 1996 spectively (11, 16). Both argase isorms share certa physicochemical properties but are immunologically distct (26, 39). Because extrahepatic tissues do not possess a complete urea cycle, the function argase-II such tissues is unclear. One function might be the production ornithe, which is a precursor prole, polyames, related substances. Another function argase-II, for example, LPS-activated macrophages, might be to regulate the tracellular arge concentration (8, 14, 32), perhaps by makg less arge available as a substrate for , thereby leadg to dimished production NO (42). To the extent that arge is necessary for expression macrophage-mediated cytotoxicity (22, 24) as the substrate for -catalyzed production cytotoxic quantities NO (23), argase-II duction could dimish the cytotoxic role activated macrophages. However, no clear evidence for this potential mechanism exists. A recent

Journal

AJP - Heart and Circulatory PhysiologyThe American Physiological Society

Published: Nov 1, 1996

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