Differential selectivity of protein modification by the cyclopentenone prostaglandins PGA1 and 15-deoxy-Δ12,14-PGJ2:: Role of glutathione

被引：47

作者：

Gayarre, J ^{[1
]}

Stamatakis, K ^{[1
]}

Renedo, M ^{[1
]}

Pérez-Sala, D ^{[1
]}

机构：

[1] CSIC, Ctr Invest Biol, Dept Estruct & Func Prot, E-28040 Madrid, Spain

来源：

FEBS LETTERS | 2005年 / 579卷 / 25期

关键词：

prostaglandin; posttranslational modification; Michael addition; glutathione;

D O I：

10.1016/j.febslet.2005.09.069

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cyclopentenone prostaglandins (cyPG) with antiinflammatory and antiproliferative properties have been envisaged as leads for the development of therapeutic agents. Because cyPG effects are mediated in part by the formation of covalent adducts with critical signaling proteins, it is important to assess the specificity of this interaction. By using biotinylated derivatives of 15-deoxy-Delta (12,14)-PGJ(2) (15d-PGJ(2)-B) and PGA(1) (PGA(1)-B) we herein provide novel evidence for the differential selectivity of protein modification by distinct cyPG. The marked quantitative and qualitative differences in the binding of 15d-PGJ(2)-B and PGA(1)-B to cellular proteins were related to a differential reactivity in the presence of glutathione (GSH), both in vitro and in intact cells. Therefore GSH levels may influence not only the intensity but also the specificity of cyPG action. (c) 2005 Published by Elsevier B.V.

引用

页码：5803 / 5808

页数：6

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