S-NO-actin: S-nitrosylation kinetics and the effect on isolated vascular smooth muscle
S-NO-actin: S-nitrosylation kinetics and the effect on isolated vascular smooth muscle
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DOI：
10.1023/a:1005671319604
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发表时间：
2000-02-01
影响因子：
2.7
通讯作者：
Rossi, R
中科院分区：
文献类型：
--
作者：
Dalle-Donne, I;Milzani, A;Rossi, R
本文报道了S-亚硝基谷胱甘肽对反应性肌动蛋白的修饰。S-亚硝化和反硝化反应动力学表明，只有一个半胱氨酸的肌动蛋白参与反应。用双官能硫基交联剂N，N‘-1，4-苯双马来酰亚胺和单官能团试剂N-iodoacetyl-N’-(5-sulpho-1-naphthyl)ethylenediamine，鉴定该残基为半胱氨酸(374)。长丝形成和高剪切粘度变化的时间进程表明，S硝化G-肌动蛋白的聚合效率低于天然单体。观察到的稳定状态下比粘度的下降主要是由于显著抑制了细丝端到端的退火，部分是由于F-肌动蛋白浓度的降低。最后，S硝化肌动蛋白作为一氧化氮供体，在极低的浓度下表现出快速、有效的血管扩张活性，与低分子亚硝硫醇相当。
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 Cys(374). 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.