Proteomic analysis of metabolic, cytoskeletal and stress response proteins in human heart failure

Journal of Cellular and Molecular Medicine

Weiming Li⁵  Rong Rong³  Sheng Zhao¹  Xiaoming Zhu⁵  Ke Zhang²  Xin Xiong⁴  Xueqing Yu³  Qinghua Cui⁶  Shuqiang Li⁷  Li Chen⁸  Jun Cai⁵ 

[1] Department of Cardiac Surgery, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China;German Research Center for Environmental Health, Technische Universität München, München, Germany;Department of Nephrology, The First Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China;The First Affiliated Hospital, Chongqing Medical University, Chongqing, China;Department of Cardiology, Chaoyang Hospital, The Key Laboratory of Remodelling-related Cardiovascular Diseases, Capital Medical University, Ministry of Education, Beijing, China;Department of Biomedical Informatics, Peking University Health Science Center, Beijing, China;Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, USA;Texas Heart Institute, Houston, TX, USA

关键词: heart failure;    proteomics;    metabolism;    cytoskeleton;    heat shock protein;   

DOI  :  10.1111/j.1582-4934.2011.01336.x

来源: Wiley

【 摘 要 】

Abstract

Human heart failure is a complex syndrome and a primary cause of morbidity and mortality in the world. However, the molecular pathways involved in the remodelling process are poorly understood. In this study, we performed exhaustive global proteomic surveys of cardiac ventricle isolated from failing and non-failing human hearts, and determined the regulatory pathway to uncover the mechanism underlying heart failure. Two-dimensional gel electrophoresis (2-DE) coupled with tandem mass spectrometry was used to identify differentially expressed proteins in specimens from failing (n = 9) and non-failing (n = 6) human hearts. A total of 25 proteins with at least 1.5-fold change in the failing heart were identified; 15 proteins were up-regulated and 10 proteins were down-regulated. The altered proteins belong to three broad functional categories: (i) metabolic [e.g. NADH dehydrogenase (ubiquinone), dihydrolipoamide dehydrogenase, and the cytochrome c oxidase subunit]; (ii) cytoskeletal (e.g. myosin light chain proteins, troponin I type 3 and transthyretin) and (iii) stress response (e.g. αB-crystallin, HSP27 and HSP20). The marked differences in the expression of selected proteins, including HSP27 and HSP20, were further confirmed by Western blot. Thus, we carried out full-scale screening of the protein changes in human heart failure and profiled proteins that may be critical in cardiac dysfunction for future mapping.

【 授权许可】

Unknown   
© 2011 The Authors Journal of Cellular and Molecular Medicine © 2011 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd