Phospholipases of plasmic membranes of adipose tissue. Possible intermediaries for insulin action.
In the present investigation we have shown that cytoplasmic membranes of adipocytes contain A1 and A2 phospholipase activities which are optimal in a buffer with 5 mM Ca2+ (pH 8.5). Insulin enhances these activities within phosphatidylethanolamine. Insulin increases also the amount of free fatty acids in membranes. Rodbell and Blecher have already shown an insulin-like action of phospholipases towards the uptake of glucose and amino-acids by adipocytes. Shier and Asakawa have recently described that lysolecithin and unsaturated fatty acids can change nucleotide-cyclase activities of cytoplasmic membranes towards GTP and ATP; lysolecithins and Triton X 100 seem to react in an identical way. Results from these studies give new suggestions on insulin action; phospholipase activation changes membrane physiochemical properties inducing an increase of glucose carrier mobility and leading the membrane cyclase enzyme (s) towards GMP cyclic synthesis.
D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology*; D005230:Fatty Acids, Nonesterified / Q000032:analysis; D007328:Insulin / Q000494:pharmacology*; D008563:Membrane Lipids / Q000032:analysis; D010740:Phospholipases / Q000378:metabolism*; D013379:Substrate Specificity
D005230:Fatty Acids, Nonesterified; D007328:Insulin; D008563:Membrane Lipids; D010740:Phospholipases