Comparative phosphoproteome analysis of cardiomyocytes preconditioned by diazoxide |
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Authors: | LI Hong XIAO Ying-bin YANG Tian-de MOU Zhi-rong ZOU Li-yun HUANG He |
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Affiliation: | 1.Department of Anesthesiology, Xinqiao Hospital, 2Department of Cardiovascular Surgery, Xinqiao Hospital, 3Institute of Immunology, The Third Military Medical University, Chongqing 400037, China. E-mail: lihong881@vip. sina.com |
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Abstract: | AIM: To analyze and identify the phosphoproteins associated with diazoxide preconditioning. METHODS: Proteomics technique was used to investigate the changes of phosphoprotein after diazoxide preconditioning. Adult rat ventricular myocytes were pretreated in the presence and absence of 200 μmol/L diazoxide for 10 min. Phosphoproteins prepared and enriched respectively from control and diazoxide pretreated groups were then separated by two-dimensional (2D) gel electrophoresis and stained with sliver staining kit. Phosphoproteins of interest were further identified by mass spectrometry. RESULTS: Associated with diazoxide preconditioning, the proteins of chaperonin containing TCP-1 and hypothetical protein XP_346548 were phosphorylated significantly. The proteins of 94 kD glucose-regulated protein, calpactin I heavy chain and ferritin were dephosphorylated markedly (P<0.05). CONCLUSION: These findings suggest that cardiomyocytes undergo significant posttranslational modification via phosphorylation in a multitude of proteins in response to diazoxide preconditioned signaling, which may mediate myocardioprotection signaling downstream mitochondrial staining dish KATP channel induced by ischemic preconditioning. |
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Keywords: | Proteome Cardiomyocytes Diazoxide |
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