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Proteomic identification of the candidate target proteins of 15‐deoxy‐delta12,14‐prostaglandin J 2
Author(s) -
Marcone Simone,
Fitzgerald Desmond J.
Publication year - 2013
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201200289
Subject(s) - biotinylation , biochemistry , chemistry , proteomics , biology , microbiology and biotechnology , gene
15‐ D eoxy‐delta12, 14‐prostaglandin J 2 (15d‐ PGJ 2 ) is an endogenous anti‐inflammatory lipid derived from PGD 2 . One potential mechanism for its activity is the covalent modification of cellular proteins, via a reactive α,β‐unsaturated carbonyl group in its cyclopentenone ring, which in turn alters protein function. In order to identify the candidate target proteins covalently modified by 15d‐ PGJ 2 in human aortic endothelial cell ( EC ), EC was treated with biotinylated‐15d‐ PGJ 2 , the modified proteins extracted by N eutravidin affinity‐purification and the proteins identified by LTQ O rbitrap mass spectrometer. Classification of the 358 identified proteins was performed using PANTHER classification system ( www.pantherdb.org ), showing that the proteins mapped to metabolic process, cellular process, and transport activity. This protein data set highlights the potential for 15d‐ PGJ 2 to covalently modify cellular proteins and provides a source of data that will aid further studies on the mechanism of action of this endogenous regulator of inflammation.