IR@PKUHSC  > 北京大学基础医学院  > 生物物理学系
学科主题基础医学
Shotgun proteomic analysis of sarcoplasmic reticulum preparations from rabbit skeletal muscle
Liu, Zhouying; Du, Xiangning; Yin, Changcheng; Chang, Zhenzhan
关键词Animal proteomics Bioinformatic analysis Excitation-contraction coupling Mitochondrion Sarcoplasmic reticulum
刊名PROTEOMICS
2013-08-01
DOI10.1002/pmic.201200138
13期:15页:2335-2338
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemical Research Methods ; Biochemistry & Molecular Biology
资助者National Natural Science Foundation of China ; Beijing Natural Science Foundation ; Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry ; National Natural Science Foundation of China ; Beijing Natural Science Foundation ; Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]DIMENSIONAL GEL-ELECTROPHORESIS ; CALCIUM-RELEASE UNITS ; HPLC-ESI-MS/MS ; RYANODINE RECEPTOR ; PROTEINS ; MITOCHONDRIA ; MEMBRANE ; HEART
英文摘要

To obtain a comprehensive understanding of proteins involved in excitation-contraction coupling, a catalog of proteins from sarcoplasmic reticulum (SR) membrane fractions of New Zealand white rabbit skeletal muscle was analyzed by an optimized shotgun proteomic method. Light and heavy SR membrane fractions were obtained by nonlinear sucrose gradient centrifugation and separated by 1DE followed by a highly reproducible, automated LC-MS/MS on the hybrid linear ion trap (LTQ) Orbitrap mass spectrometer. By integrating as low as 1% false discovery rate as one of the features for quality control method, 483 proteins were identified from both of the two independent SR preparations. Proteins involved in calcium release unit complex, including ryanodine receptor 1, dihydropyridine receptor, calmodulin, triadin, junctin, and calsequestrin, were all detected, which offered validation for this protein identification method. Rigorous bioinformatics analysis was performed. Protein pI value, molecular weight range, hydrophobicity index, and transmembrane region were calculated using bioinformatics softwares. Eighty-three proteins were classified as hydrophobic proteins and 175 proteins were recognized as membrane proteins. Based on the proteomic analysis results, we found as the first time that not only transverse tubule but also mitochondrion physically connected to SR. The complete mapping of these proteomes may help in the elucidation of the process of excitation-contraction coupling and excitation-metabolism coupling.

语种英语
所属项目编号31070650 ; 5102023
资助者National Natural Science Foundation of China ; Beijing Natural Science Foundation ; Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry ; National Natural Science Foundation of China ; Beijing Natural Science Foundation ; Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry
WOS记录号WOS:000327008300014
Citation statistics
Cited Times:8[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/66549
Collection北京大学基础医学院_生物物理学系
作者单位Peking Univ, Dept Biophys, Sch Basic Med Sci, Beijing 100191, Peoples R China
Recommended Citation
GB/T 7714
Liu, Zhouying,Du, Xiangning,Yin, Changcheng,et al. Shotgun proteomic analysis of sarcoplasmic reticulum preparations from rabbit skeletal muscle[J]. PROTEOMICS,2013,13(15):2335-2338.
APA Liu, Zhouying,Du, Xiangning,Yin, Changcheng,&Chang, Zhenzhan.(2013).Shotgun proteomic analysis of sarcoplasmic reticulum preparations from rabbit skeletal muscle.PROTEOMICS,13(15),2335-2338.
MLA Liu, Zhouying,et al."Shotgun proteomic analysis of sarcoplasmic reticulum preparations from rabbit skeletal muscle".PROTEOMICS 13.15(2013):2335-2338.
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