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Prostanoids with cyclopentenone structure as tools for the characterization of electrophilic lipid-protein interactomes.

AuthorsStamatakis, Konstantinos ; Pérez-Sala, Dolores
KeywordsCyclopentenone prostaglandins
Posttranslational modification
Issue Date1-Jul-2014
AbstractElectrophilic eicosanoids arise from the free radical-induced peroxidation of arachidonic acid or its metabolites. These reactive species may play an important role in pathophysiological processes associated with inflammation and oxidative stress. Cyclopentenone prostaglandins(cyPG) and isoprostanes are reactive eicosanoids that can form covalent adducts with cysteine residues in proteins through Michael addition. In pharmacological studies, cyPG have shown potent protective effects in experimental models of inflammation and tissue injury, and they have been proposed to contribute to inflammatory resolution. An important mechanism for the anti-inflammatory effects of cyPG is the covalent modification of critical cysteine residues in proteins involved in the modulation of inflammation, such as transcription factors NF- B and AP-1. In recent years, analogs of electrophilic prostanoids have been used in various approaches to identify biologically relevant protein targets for this modification. Prostanoids with cyclopentenone structure have been shown to target a defined subproteome that is beginning to be characterized. Structural studies suggest that diverse cyPG may modify distinct proteins selectively. Functional studies put forward a dual role for these compounds in the cellular response to inflammation or stress. Therefore, a detailed knowledge of targets of electrophilic eicosanoids and the functional consequences of their modification will contribute to the understanding of their mechanism of action and help assess whether these endogenous mediators can be exploited as the basis for the development of novel therapeutic strategies.
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