title: Characterization of lipolytic inhibitor G(0)/G(1) switch gene-2 protein (G0S2) expression in male Sprague-Dawley rat skeletal muscle compared to relative content of adipose triglyceride lipase (ATGL) and comparitive gene identification-58 (CGI-58).
abstract: The rate-limiting enzyme in lipolysis, adipose triglyceride lipase (ATGL), is activated by comparative gene identification-58 (CGI-58) and inhibited by the G(0)/G(1) switch gene-2 (G0S2) protein. It is speculated that inhibition of ATGL is through a dose dependent manner of relative G0S2 protein content. There is little work examining G0S2 expression in lipolytic tissues, and the relative expression across oxidative tissues such as skeletal muscle has not yet been described. Three muscles, soleus (SOL), red gastrocnemius (RG), and white gastrocnemius (WG) were excised from 57-day old male Sprague-Dawley rats (n = 9). QRT-PCR was used for mRNA analysis, and western blotting was conducted to determine protein content. ATGL and G0S2 protein content were both greatest in the lipolytic SOL, with the least amount of both ATGL and G0S2 protein content found in the WG. CGI-58 protein content however did not mirror ATGL and G0S2 protein content, since the RG had the greatest CGI-58 protein content when compared to the SOL and WG. When comparing our tissues based on CGI-58-to-ATGL ratio and G0S2-to-ATGL ratio, it was discovered that contrary to oxidative demand, the glycolytic WG had the greatest activator CGI-58-to-ATGL ratio with the oxidative SOL having the least, and no differences in G0S2-to-ATGL across the three muscle types. These data suggest that the content of G0S2 relative to the lipase in skeletal muscle would not predict lipolytic potential.
authors: Department of Kinesiology, Centre for Bone and Muscle Health, Brock University, 500 Glenridge Ave, St Catharines, Ontario, Canada.
authors: Patrick C
authors: PC
authors: Turnbull
authors: Department of Kinesiology, Centre for Bone and Muscle Health, Brock University, 500 Glenridge Ave, St Catharines, Ontario, Canada.
authors: Sofhia V
authors: SV
authors: Ramos
authors: Department of Kinesiology, Centre for Bone and Muscle Health, Brock University, 500 Glenridge Ave, St Catharines, Ontario, Canada.
authors: Rebecca E K
authors: RE
authors: MacPherson
authors: Department of Kinesiology, Centre for Bone and Muscle Health, Brock University, 500 Glenridge Ave, St Catharines, Ontario, Canada.
authors: Brian D
authors: BD
authors: Roy
authors: Department of Kinesiology, Centre for Bone and Muscle Health, Brock University, 500 Glenridge Ave, St Catharines, Ontario, Canada.
authors: Sandra J
authors: SJ
authors: Peters
mesh_terms: D000217:Acyltransferases / Q000235:genetics*; D000818:Animals; D018797:Cell Cycle Proteins / Q000235:genetics*; D002950:Citrate (si)-Synthase / Q000235:genetics / Q000378:metabolism; D004789:Enzyme Activation; D020869:Gene Expression Profiling; D005786:Gene Expression Regulation; D008049:Lipase / Q000235:genetics*; D008297:Male; D018482:Muscle, Skeletal / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D059467:Transcriptome
chemical_list: C520594:Abhd5 protein, rat; D018797:Cell Cycle Proteins; C586945:G0S2 protein, rat; D012333:RNA, Messenger; D000217:Acyltransferases; D002950:Citrate (si)-Synthase; D008049:Lipase; C571275:PNPLA2 protein, rat