Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro

李洪; 肖颖彬; 高玉琪; 杨天德

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Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro

Updated：2026-03-12

- Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro
- Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro
- 解放军医学杂志（英文版） 2006年第3期页码：143-147
- Affiliations：
  
  1. Departments of Anesthesiology Xinqiao Hospital
  2. Third Military Medical University
  3. ,Chongqing,400038
  4. Department of Pathophysiology
  5. College of High Altitude Military Medicine
  6. Departments of Cardiovascular Surgery Xinqiao Hospital Third Military Medical University Chongqing China,400037
- Author bio：
- Funds：
  
  Supported by the National Natural Science Foundation of China （No. 30200089 and No. 30500211）
- DOI：
  中图分类号： R654
- 纸质出版：2006
- Accepted：
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Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro[J]. 解放军医学杂志（英文版）, 2006,(3):143-147.

[1]李洪,肖颖彬,高玉琪,杨天德.Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro[J].Journal of Medical Colleges of PLA,2006(03):143-147.
Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro[J]. 解放军医学杂志（英文版）, 2006,(3):143-147. DOI：

[1]李洪,肖颖彬,高玉琪,杨天德.Differentially expressed phosphoproteins in diazoxide-pretreated ventricular myocytes by two-dimensional electrophoresis and mass spectrometry in vitro[J].Journal of Medical Colleges of PLA,2006(03):143-147. DOI：

摘要

Abstract

<正>Objective: To analyze and identify differentially expressed phosphoproteins associated with mitochondrial KATP channel opening. Methods: Adult rat ventricular myocytes were isolated

cultured

and identified

and pretreated without or with 100μmol/L diazoxide for 10 min. Phosphoproteins prepared and enriched from the control and diazoxide-pretreated cells were separated by two-dimensional gel elec-trophoresis （2-DE） followed by sliver staining. The obtained interesting phosphoproteins were further i-dentified by mass spectrometry. Results: Associated with diazoxide preconditioning

the proteins of chap-eronin containing TCP-1 and hypothetical protein XP- 346548 were phosphorylated significantly （P< 0. 01）

while the 94-kDa glucose-regulated protein

calpactin I heavy chain and ferritin were dephosphory-lated markedly （P<0. 01）. Conclusion: These findings suggest that cardiomyocytes undergo significant posttranslational modification via phosphorylation in a multitude of proteins in order to respond diazoxide preconditioning

and these phosphorylated protein may mediate the downstream signaling of cardioprotec-tion by mitochondrial KATP channel opening induced by ischemic preconditioning.

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