Comparative proteomics reveals abnormal binding of ATGL and dysferlin on lipid droplets from pressure overload-induced dysfunctional rat hearts

Scientific Reports
Linghai LiPingsheng Liu

Abstract

Excessive retention of neutral lipids in cardiac lipid droplets (LDs) is a common observation in cardiomyopathy. Thus, the systematic investigation of the cardiac LD proteome will help to dissect the underlying mechanisms linking cardiac steatosis and myocardial dysfunction. Here, after isolation of LDs from normal and dysfunctional Sprague-Dawley rat hearts, we identified 752 heart-associated LD proteins using iTRAQ quantitative proteomic method, including 451 proteins previously unreported on LDs. The most noteworthy finding was the identification of the membrane resealing protein, dysferlin. An analysis of dysferlin truncation mutants indicated that its C2 domain was responsible for its LD localization. Quantitative proteomic results further determined that 27 proteins were increased and 16 proteins were decreased in LDs from post pressure overload-induced dysfunctional hearts, compared with normal hearts. Notably, adipose triacylglycerol lipase (ATGL) was dramatically decreased and dysferlin was substantially increased on dysfunctional cardiac LDs. This study for the first time reveals the dataset of the heart LD proteome in healthy tissue and the variation of it under cardiac dysfunction. These findings highlight an associ...Continue Reading

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Citations

Oct 21, 2016·Muscle & Nerve·Marina Fanin, Corrado Angelini
Jun 8, 2017·World Journal of Biological Chemistry·Angelica F ArcanjoCelio Geraldo Freire-de-Lima
Mar 17, 2019·Cells·Xuehan LiXuelin Zhang
Jun 17, 2019·Journal of Lipid Research·Vanessa R HaynesMatthew J Watt
Sep 15, 2018·Proteomics·Congyan Zhang, Pingsheng Liu
Jan 5, 2017·Journal of Cell Science·Abdou Rachid Thiam, Mathias Beller

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Methods Mentioned

BETA
Transmission electron microscopy

Software Mentioned

Quantity One
Proteome Discovery
PATRHE

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