Journal
JOURNAL OF LIPID RESEARCH
Volume 58, Issue 4, Pages 681-694Publisher
ELSEVIER
DOI: 10.1194/jlr.M071407
Keywords
lipid droplet proteins; liver proteomics; isobaric tags for relative and absolute quantitation
Categories
Funding
- National International Cooperation [2012DFB30080]
- National High-Tech Research and Development Program of China 863 Program [2012AA020201]
- National Natural Science Foundation of China [31200582]
- Beijing Municipal Natural Science Foundation [5132012]
- National 1000 Young Talents Project
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Eukaryotic cells store neutral lipids in cytoplasmic lipid droplets (LDs) enclosed in a monolayer of phospholipids and associated proteins [LD proteins (LDPs)]. Growing evidence has demonstrated that LDPs play important roles in the pathogenesis of liver diseases. However, the composition of liver LDPs and the role of their alterations in hepatosteatosis are not well-understood. In this study, we performed liver proteome and LD sub-proteome profiling to identify enriched proteins in LDs as LDPs, and quantified their changes in a high-fat diet (HFD)-induced fatty liver model. Among 5,000 quantified liver proteins, 101 were enriched by greater than 10-fold in the LD sub-proteome and were classified as LDPs. Differential profiling of LDPs in HFD-induced fatty liver provided a list of candidate LDPs for functional investigation. We tested the function of an upregulated LDP, S100a10, in vivo with adenovirus-mediated gene silencing and found, unexpectedly, that knockdown of S100a10 accelerated progression of HFD-induced liver steatosis. The S100A10 interactome revealed a connection between S100A10 and lipid transporting proteins, suggesting that S100A10 regulates the development and formation of LDs by transporting and trafficking. This study identified LD-enriched sub-proteome in homeostatic as well as HFD-induced fatty livers, providing a rich resource for the LDP research field.
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