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

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

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Title: Proteomic analysis of metabolic, cytoskeletal and stress response proteins in human heart failure
Author: Li, Weiming; Rong, Rong; Zhao, Sheng; Zhu, Xiaoming; Zhang, Ke; Xiong, Xin; Yu, Xueqing; Cui, Qinghua; Li, Shuqiang; Chen, Li; Cai, Jun; Du, Jie

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Citation: Li, W., R. Rong, S. Zhao, X. Zhu, K. Zhang, X. Xiong, X. Yu, et al. 2011. “Proteomic analysis of metabolic, cytoskeletal and stress response proteins in human heart failure.” Journal of Cellular and Molecular Medicine 16 (1): 59-71. doi:10.1111/j.1582-4934.2011.01336.x. http://dx.doi.org/10.1111/j.1582-4934.2011.01336.x.
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Abstract: 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.
Published Version: doi:10.1111/j.1582-4934.2011.01336.x
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3823093/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:14351295
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