Phospho-proteomic approach to identify new targets of leucine deprivation in muscle cells

被引:10
|
作者
Talvas, Jeremie [1 ]
Obled, Alain [1 ]
Sayd, Thierry [2 ]
Chambon, Christophe [2 ]
Mordier, Sylvie [1 ]
Fafournaux, Pierre [1 ]
机构
[1] INRA, Ctr Clermont Ferrand Theix, Unite Nutr Humaine, F-63122 St Genes Champanelle, France
[2] INRA, Ctr Clermont Ferrand Theix, UR Qual Prod Anim 370, F-63122 St Genes Champanelle, France
关键词
D O I
10.1016/j.ab.2008.05.038
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The aim of this Study was to optimize a protocol that allows identifying changes at the phosphorylation level of specific proteins in response to cell stimulation by leucine starvation. To make possible the identification of differentially phosphorylated proteins by the combination of two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), we prepared fraction enriched in phosphoproteins. For that purpose, we adapted the immobilized metal affinity chromatography (IMAC) technique to make it compatible with 2D-PAGE. On the whole, this procedure allowed identifying regulated targets of leucine deprivation: molecular chaperones glucose-regulated protein 58 kDa (GRP58) and BiP (GRP78), RNA helicase DEAD box polypeptide 3, and eukaryotic translation initiation factor 4B (eIF4B). (c) 2008 Elsevier Inc. All rights reserved.
引用
收藏
页码:148 / 150
页数:3
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