Quantitative analysis of redox-sensitive proteome with DIGE and ICAT

Cexiong Fu, Jun Hu, Tong Liu, Tetsuro Ago, Junichi Sadoshima, Hong Li

研究成果: ジャーナルへの寄稿学術誌査読

90 被引用数 (Scopus)

抄録

Oxidative modifications of protein thiols are important mechanisms for regulating protein functions. The present study aimed to compare the relative effectiveness of two thiol-specific quantitative proteomic techniques, difference gel electrophoresis (DIGE) and isotope coded affinity tag (ICAT), for the discovery of redox-sensitive proteins in heart tissues. We found that these two methods were largely complementary; each could be used to reveal a set of unique redox-sensitive proteins. Some of these proteins are low-abundant signaling proteins and membrane proteins. From DIGE analysis, we found that both NF-κ:B-repressing protein and epoxide hydrolase were sensitive to H 2O 2 oxidation. In ICAT analysis, we found that specific cysteines within sacroplasmic endoplamic reticulum calcium ATPase 2 and voltage-dependent anion-selective channel protein 1 were sensitive to H 2O 2 oxidation. From these analyses, we conclude that both methods should be employed for proteome-wide studies, to maximize the possibility of identifying proteins containing redox-sensitive cysteinyl thiols in complex biological systems.

本文言語英語
ページ(範囲)3789-3802
ページ数14
ジャーナルJournal of Proteome Research
7
9
DOI
出版ステータス出版済み - 9月 2008
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 化学 (全般)

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