S-NO-actin: S-nitrosylation kinetics and the effect on isolated vascular smooth muscle.

Abstract:

:We describe the modification of reactive actin sulfhydryls by S-nitrosoglutathione. Kinetics of S-nitrosylation and denitrosylation suggest that only one cysteine of actin is involved in the reactions. By using the bifunctional sulfhydryl cross-linking reagent N,N'-1,4-phenylenebismaleimide and the monofunctional reagent N-iodoacetyl-N'-(5-sulpho-1-naphthyl)ethylenediamine, we identified this residue as Cys374. The time course of filament formation followed by high-shear viscosity changes revealed that S-nitrosylated G-actin polymerizes less efficiently than native monomers. The observed decrease in specific viscosity at steady state is due mainly to a marked inhibition of filament end-to-end annealing and, partially, to a reduction in F-actin concentration. Finally, S-nitrosylated actin acts as nitric oxide donor showing a fast, potent vasodilating activity at unusually low concentrations, being comparable with that of low molecular weight nitrosothiols.

authors

Dalle-Donne I,Milzani A,Giustarini D,Di Simplicio P,Colombo R,Rossi R

doi

10.1023/a:1005671319604

keywords:

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

171-81

issue

2

eissn

0142-4319

issn

1573-2657

journal_volume

21

pub_type

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