期刊
JOURNAL OF LIPID RESEARCH
卷 56, 期 10, 页码 1972-1984出版社
ELSEVIER
DOI: 10.1194/jlr.M062372
关键词
proteome; lipidome; neutral lipid hydrolase; adipose triglyceride lipase
资金
- Austrian Science Fund (FWF) [P25193, P21296, W901, F30 SFB Lipotox]
- NAWI Graz
- Austrian Science Fund (FWF) [P24944, P25193] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [F 3002, P 25193, P 24944, W 901] Funding Source: researchfish
Lipid droplets (LDs) of hepatic stellate cells (HSCs) contain large amounts of vitamin A [in the form of retinyl esters (REs)] as well as other neutral lipids such as TGs. During times of insufficient vitamin A availability, RE stores are mobilized to ensure a constant supply to the body. To date, little is known about the enzymes responsible for the hydrolysis of neutral lipid esters, in particular of REs, in HSCs. In this study, we aimed to identify LD-associated neutral lipid hydrolases by a proteomic approach using the rat stellate cell line HSC-T6. First, we loaded cells with retinol and FAs to promote lipid synthesis and deposition within LDs. Then, LDs were isolated and lipid composition and the LD proteome were analyzed. Among other proteins, we found perilipin 2, adipose TG lipase (ATGL), and comparative gene identification-58 (CGI-58), known and established LD proteins. Bioinformatic search of the LD proteome for /-hydrolase fold-containing proteins revealed no yet uncharacterized neutral lipid hydrolases. In in vitro activity assays, we show that rat (r)ATGL, coactivated by rat (r)CGI-58, efficiently hydrolyzes TGs and REs. These findings suggest that rATGL and rCGI-58 are LD-resident proteins in HSCs and participate in the mobilization of both REs and TGs.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据