Proteomic studies on protein modification by cyclopentenone prostaglandins: Expanding our view on electrophile actions

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• 作者：Beatriz  ; Garzó ; n^a ; Clara L.  ; Oeste^a ; Beatriz  ; Dí ; ez-Dacal^a ; Dolores  ; Pé ; rez-Sala ;   ; ^a ;   ; ^{dperezsala@cib.csic.es}
• 关键词：Cyclopentenone prostaglandins ; Posttranslational modification ; Ras proteins ; Proteomics ; 15-deoxy-¦¤12 ; 14-prostaglandin J2 ; Inflammation and tumorigenesis
• 刊名：Journal of Proteomics
• 出版年：2011
• 出版时间：19 October 2011
• 年：2011
• 卷：74
• 期：11
• 页码：2243-2263
• 全文大小：1737 K

文摘

Cyclopentenone prostaglandins (cyPG) are lipid mediators that participate in the mechanisms regulating inflammation and tumorigenesis. cyPG are electrophilic compounds that act mainly through the covalent modification of cellular proteins. The stability of many cyPG-protein adducts makes them suitable for proteomic analysis. Indeed, methodological advances in recent years have allowed identifying many cyPG targets, including components of pro-inflammatory transcription factors, cytoskeletal proteins, signaling kinases and proteins involved in redox control. Insight into the diversity of cyPG targets is providing a better understanding of their mechanism of action, uncovering novel links between resolution of inflammation, proliferation and redox regulation. Moreover, identification of the target residues has unveiled the selectivity of protein modification by these electrophiles, providing valuable information for potential pharmacological applications. Among the challenges ahead, the detection of proteins modified by endogenous cyPG and the quantitative aspects of the modification require further efforts. Importantly, only a few years after the appearance of the first proteomic studies, research on cyPG targets is yielding new paradigms for redox and electrophilic signaling.