L-arginine stimulates an endogenous ADP-ribosyltransferase.

Abstract:

:An ubiquitous biochemical pathway known to synthesize nitric oxide (NO) from L-arginine has been identified in many cell types. Recent studies indicate that besides activating soluble guanylate cyclase NO is likely to have effects unrelated to the known signal transduction pathway. Activation of the soluble NO synthase stimulates an endogenous ADP-ribosylation of a predominant 39 kDa protein, known to be activated by NO releasing agents. This is demonstrated using the cytosolic fraction of rat cerebellum and HL-60 cells. The ADP-ribosylation is suppressed by the known NO synthase inhibitors N-nitro-L-arginine and N-methyl-L-arginine. These observations indicate that NO derived from its physiological precursor L-arginine activates an endogenous ADP-ribosyltransferase.

authors

Dimmeler S,Brüne B

doi

10.1016/0006-291x(91)90968-d

subject

Has Abstract

pub_date

1991-08-15 00:00:00

pages

848-55

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)90968-D

journal_volume

178

pub_type

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