Co-induction of Arginase and Nitric Oxide Synthase in Murine Macrophages Activated by Lipopolysaccharide

Wang, Winnie W.; Jenkinson, Christopher P.; Griscavage, Jeanette M.; Kern, Rita M.; Arabolos, Nicole; Byrns, Russell E.; Cederbaum, Stephen D.; Ignarro, Louis J.

doi:10.1006/bbrc.1995.1757

Cited by 209 publications

(142 citation statements)

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“…It was noted that nitrate, the completely oxidized end product of NO, is not inhibitory to arginase activity. Although liver and macrophage arginases are different isoenzymes [22], we found that macrophage and bovine liver Fg. 2.…”

Section: Effect Of Nitrite On Argandase Activitymentioning

confidence: 53%

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The inhibitory effect of nitrite, a stable product of nitric oxide (NO) formation, on arginase

et al. 1996

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Macrophages contain arginase and an inducible NO synthase, demonstrated by using L-arginine, the common substrate, for production of both nitric oxide and urea. Arginase was inhibited by nitrite, the stable end product of NO. This inhibition was non-competitive, and could not be explained by the reaction of nitrite with arginine, or by the irreversible covalent modification of arginase, or by the removal of Mn 2+, a cofactor of arginase.

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Section: Effect Of Nitrite On Argandase Activitymentioning

confidence: 53%

“…1). This is c, resistent with the observations of others [22,23] who have rL'ported that arginase isoenzymes can be distinguished mainly by immunological methods.…”

Section: Effect Of Nitrite On Argandase Activitymentioning

confidence: 73%

The inhibitory effect of nitrite, a stable product of nitric oxide (NO) formation, on arginase

et al. 1996

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“…The anti-oxidant agent PDTC has been widely used as a specific inhibitor of NF-xB activation in various kinds of nonhepatic cells [13,[27][28][29]. Surprisingly, none of the several doses (from 10 _8 to 10 -3 M) of PDTC we tested by adding them to the synthetic MEM medium 1 hour earlier than TPA (10 -9 M) could suppress either the prior activation of NF-xB (Fig.…”

Section: Nuclear Transcription Factors and Inos Gene Expressionmentioning

confidence: 88%

TPA and cycloheximide modulate the activation of NF‐κB and the induction and stability of nitric oxide synthase transcript in primary neonatal rat hepatocytes

et al. 1996

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“…Arginase [148,202,242] and ODC [243,244] are also induced in murine macrophage lines by LPS or cAMP. Moreover, induction of these enzymes is synergistic when LPS and cAMP are combined [202,244].…”

Section: Figure 6 Developmental Changes In Arginine Catabolism By Pigmentioning

confidence: 98%

Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,389

2,036

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Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline, glutamate, creatine and agmatine. Of the enzymes that catalyse rate-controlling steps in arginine synthesis and catabolism, argininosuccinate synthase, the two arginase isoenzymes, the three nitric oxide synthase isoenzymes and arginine decarboxylase have been recognized in recent years as key factors in regulating newly identified aspects of arginine metabolism. In particular, changes in the activities of argininosuccinate synthase, the arginases, the inducible isoenzyme of nitric oxide synthase and also cationic amino acid transporters play major roles in determining the metabolic fates of arginine in health and disease, and recent studies have identified

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Co-induction of Arginase and Nitric Oxide Synthase in Murine Macrophages Activated by Lipopolysaccharide

Cited by 209 publications

References 0 publications

The inhibitory effect of nitrite, a stable product of nitric oxide (NO) formation, on arginase

The inhibitory effect of nitrite, a stable product of nitric oxide (NO) formation, on arginase

TPA and cycloheximide modulate the activation of NF‐κB and the induction and stability of nitric oxide synthase transcript in primary neonatal rat hepatocytes

Arginine metabolism: nitric oxide and beyond

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