Proteomic Study and Marker Protein Identification of Caenorhabditis elegans Lipid Droplets

• Published in: Molecular & cellular proteomics Vol. 11; no. 8; pp. 317 - 328
• Main Authors: Zhang, Peng, Na, Huimin, Liu, Zhenglong, Zhang, Shuyan, Xue, Peng, Chen, Yong, Pu, Jing, Peng, Gong, Huang, Xun, Yang, Fuquan, Xie, Zhensheng, Xu, Tao, Xu, Pingyong, Ou, Guangshuo, Zhang, Shaobing O., Liu, Pingsheng
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.08.2012; The American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Biomarkers - analysis; Blotting, Western; Butyryl-CoA Dehydrogenase - analysis; Caenorhabditis elegans - metabolism; Caenorhabditis elegans Proteins - analysis; Cytoplasmic Vesicles - metabolism; Cytoplasmic Vesicles - ultrastructure; Lipid Metabolism; Lipids - chemistry; Mass Spectrometry; Microscopy, Confocal; Microscopy, Electron, Transmission; Proteome - analysis; Proteomics - methods
• ISSN: 1535-9476; 1535-9484
• DOI: 10.1074/mcp.M111.016345

Lipid droplets (LDs) are a neutral lipid storage organelle that is conserved across almost all species. Many metabolic syndromes are directly linked to the over-storage of neutral lipids in LDs. The study of LDs in Caenorhabditis elegans (C. elegans) has been difficult because of the lack of specific LD marker proteins. Here we report the purification and proteomic analysis of C. elegans lipid droplets for the first time. We identified 306 proteins, 63% of these proteins were previously known to be LD-proteins, suggesting a similarity between mammalian and C. elegans LDs. Using morphological and biochemical analyses, we show that short-chain dehydrogenase, DHS-3 is almost exclusively localized on C. elegans LDs, indicating that it can be used as a LD marker protein in C. elegans. These results will facilitate further mechanistic studies of LDs in this powerful genetic system, C. elegans.