title: Proteomic analysis of murine testes lipid droplets.
abstract: Testicular Leydig cells contain abundant cytoplasmic lipid droplets (LDs) as a cholesteryl-ester store for releasing cholesterols as the precursor substrate for testosterone biosynthesis. Here, we identified the protein composition of testicular LDs purified from adult mice by using mass spectrometry and immunodetection. Among 337 proteins identified, 144 were previously detected in LD proteomes; 44 were confirmed by microscopy. Testicular LDs contained multiple Rab GTPases, chaperones, and proteins involved in glucuronidation, ubiquination and transport, many known to modulate LD formation and LD-related cellular functions. In particular, testicular LDs contained many members of both the perilipin family and classical lipase/esterase superfamily assembled predominately in adipocyte LDs. Thus, testicular LDs might be regulated similar to adipocyte LDs. Remarkably, testicular LDs contained a large number of classical enzymes for biosynthesis and metabolism of cholesterol and hormonal steroids, so steroidogenic reactions might occur on testicular LDs or the steroidogenic enzymes and products could be transferred through testicular LDs. These characteristics differ from the LDs in most other types of cells, so testicular LDs could be an active organelle functionally involved in steroidogenesis.
authors.affiliation: Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
authors.forename: Weiyi
authors.initials: W
authors.lastname: Wang
authors.affiliation: Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
authors.forename: Suning
authors.initials: S
authors.lastname: Wei
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
authors.forename: Linghai
authors.initials: L
authors.lastname: Li
authors.affiliation: Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
authors.forename: Xueying
authors.initials: X
authors.lastname: Su
authors.affiliation: Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
authors.forename: Congkuo
authors.initials: C
authors.lastname: Du
authors.affiliation: Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
authors.forename: Fengjuan
authors.initials: F
authors.lastname: Li
authors.affiliation: Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
authors.forename: Bin
authors.initials: B
authors.lastname: Geng
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
authors.forename: Pingsheng
authors.initials: P
authors.lastname: Liu
authors.affiliation: Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Peking University, Beijing 100191, China.
authors.forename: Guoheng
authors.initials: G
authors.lastname: Xu
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D004950:Esterases / Q000378:metabolism; D007985:Leydig Cells / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism; D066292:Lipid Droplets / Q000378:metabolism*; D050356:Lipid Metabolism / Q000502:physiology; D008055:Lipids; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D000070778:Perilipin-1; D010750:Phosphoproteins / Q000378:metabolism; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics / Q000379:methods; D013256:Steroids / Q000378:metabolism; D020691:rab GTP-Binding Proteins / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D008055:Lipids; D000070778:Perilipin-1; D010750:Phosphoproteins; D020543:Proteome; D013256:Steroids; D004950:Esterases; D008049:Lipase; D020691:rab GTP-Binding Proteins