Insulin stimulates fatty acid acylation of adipocyte proteins.
Isolated rat adipocytes were incubated with [3H]palmitate in the presence or absence of insulin. Insulin caused marked (20-fold), rapid (T1/2 approximately 15 min), and concentration-dependent labeling of an 80 kilodalton protein. The insulin concentration producing half-maximal labeling was 0.4 ng/ml. The label was removed from the protein by treatment with hydroxylamine indicating the fatty acid was linked to the protein via an oxyester bond. Label removed from the protein co-eluted with palmitate standard by high-performance liquid chromatography. In summary, adipocyte proteins are subject to acylation by exogenous long-chain fatty acids and this process is stimulated by insulin.
Jochen
A
A
Department of Medicine, Medical College of Wisconsin, Zablocki Veterans Administration Hospital, Milwaukee 53295.
Hays
J
J
Lianos
E
E
Hager
S
S
D000215:Acylation; D000273:Adipose Tissue / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005227:Fatty Acids / Q000378:metabolism*; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D007328:Insulin / Q000494:pharmacology*; D008297:Male; D010168:Palmitates / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D005227:Fatty Acids; D006898:Hydroxylamines; D007328:Insulin; D010168:Palmitates; D011506:Proteins; D019811:Hydroxylamine