Preliminary characterization of a heat-stable protein from rat adipose tissue whose phosphorylation is stimulated by insulin.
Exposure of 32P-labelled isolated rat adipocytes or epididymal fat-pads to insulin resulted in an increase in the phosphorylation of a heat-stable acid-soluble protein of Mr 22 000. The phosphorylation of this protein was unaffected by isoprenaline (isoproterenol) in intact cells, nor was its phosphorylation catalysed by exposure in vitro to the cyclic AMP-dependent protein kinase or smooth-muscle myosin light-chain kinase. The properties of the Mr-22 000 protein include: heat-stability; solubility in 1% trichloroacetic acid; pI 4.9; elution at apparent Mr 37 500 on gel filtration; and it contains both phosphoserine and phosphothreonine. It can be distinguished from the heat-stable phosphatase inhibitor 1 of adipose tissue (inhibitor 1A) and the phosphorylated form of adipose-tissue myosin light chain by several criteria. Its identity, and the possible functional significance of the insulin-stimulated phosphorylation, remain problems for future study.
D000273:Adipose Tissue / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D002474:Cell-Free System; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D066298:In Vitro Techniques; D007328:Insulin / Q000494:pharmacology*; D008297:Male; D009218:Myosins / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains
D007328:Insulin; D010750:Phosphoproteins; D009218:Myosins