Oncotarget

Clinical Research Papers:

In-depth proteomic profiling of left ventricular tissues in human end-stage dilated cardiomyopathy

Shanshan Liu, Yan Xia, Xiaohui Liu, Yi Wang, Zhangwei Chen, Juanjuan Xie, Juying Qian, Huali Shen _ and Pengyuan Yang

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Oncotarget. 2017; 8:48321-48332. https://doi.org/10.18632/oncotarget.15689

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Abstract

Shanshan Liu1,2, Yan Xia4, Xiaohui Liu3, Yi Wang1,2, Zhangwei Chen4, Juanjuan Xie1,2, Juying Qian4, Huali Shen1,2,3 and Pengyuan Yang1,2,3

1 Institutes of Biomedical Sciences of Shanghai Medical School and Minhang Hospital, Fudan University, Shanghai, China

2 Department of Systems Biology for Medicine and School of Basic Medical Sciences, Fudan University, Shanghai, China

3 Department of chemistry, Fudan University, Shanghai, China

4 Department of Cardiology, Shanghai Institute of Cardiovascular Diseases, Zhongshan Hospital, Fudan University, Shanghai, China

Correspondence to:

Huali Shen, email:

Juying Qian, email:

Pengyuan Yang, email:

Keywords: dilated cardiomyopathy, left ventricle, cell death, S100A1, eEF2

Received: December 15, 2016 Accepted: February 12, 2017 Published: February 25, 2017

Abstract

Dilated cardiomyopathy (DCM) is caused by reduced left ventricular (LV) myocardial function, which is one of the most common causes of heart failure (HF). We performed iTRAQ-coupled 2D-LC-MS/MS to profile the cardiac proteome of LV tissues from healthy controls and patients with end-stage DCM. We identified 4263 proteins, of which 125 were differentially expressed in DCM tissues compared to LV controls. The majority of these were membrane proteins related to cellular junctions and neuronal metabolism. In addition, these proteins were involved in membrane organization, mitochondrial organization, translation, protein transport, and cell death process. Four key proteins involved in the cell death process were also detected by western blotting, indicated that cell death was activated in DCM tissues. Furthermore, S100A1 and eEF2 were enriched in the “cellular assembly and organization” and “cell cycle” networks, respectively. We verified decreases in these two proteins in end-stage DCM LV samples through multiple reaction monitoring (MRM). These observations demonstrate that our understanding of the mechanisms underlying DCM can be deepened through comparison of the proteomes of normal LV tissues with that from end-stage DCM in humans.


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