Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Incubation of rat adipocytes with the same range of noradrenaline concentrations that stimulate lipolysis caused a rapid and stable decrease in the activity of fatty acyl-CoA synthetase. Corticotropin, glucagon and dibutyryl cyclic AMP also decreased the activity of the enzyme. The effect of noradrenaline was apparent over a wide range of concentrations for the three substrates of the enzyme. A novel fluorescence assay of fatty acyl-CoA synthetase using (1,N6-etheno)-CoA is described. The effect of noradrenaline was not abolished by inclusion of albumin in homogenization buffers, persisted through subcellular fractionation and isolation of microsomes (microsomal fractions) and even survived treatment of microsomes with Triton X-100. The effect of noradrenaline was rapidly reversed within cells by the subsequent addition of insulin or propranolol. The inclusion of fluoride in homogenization buffers did not alter the observed effect of noradrenaline. Additions of cyclic AMP-dependent protein kinase to adipocyte microsomes caused considerable phosphorylation of microsomal protein by [gamma-32P]ATP, but did not affect the activity of fatty acyl-CoA synthetase.
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PMID:Reversible inactivation by noradrenaline of long-chain fatty acyl-CoA synthetase in rat adipocytes. 388 97

Primary cultures of adult rat hepatocytes incubated (24-72 h) in Waymouth's 752/1 medium, exhibited a marked decline (80-90%) in their ability to incorporate 0.5 mM [1,3-14C]glycerol and 1.0 mM palmitate into glycerolipids. The specific activities of glycerol kinase and sn-glycerol-3-P acyltransferase also showed a time-dependent reduction (30-80%). Phosphatidate phosphohydrolase, diacylglycerol cholinephosphotransferase, and fatty acid-CoA ligase activities were unaffected. Insulin and/or glucagon (10(-8) to 10(-6) M) not only prevented these reductions in hepatocyte monolayer glycerolipid formation and enzyme activities but increased (2-5-fold) the level of these processes. Cycloheximide (1 microM) reduced the insulin- and glucagon-dependent increases in sn-glycerol-3-P acyltransferase and glycerol kinase activity and glycerolipid biosynthesis. There was an excellent correlation (r greater than 0.93) between changes in glycerol kinase and sn-glycerol-3-P acyltransferase activity and the capacity of hepatocyte monolayers to incorporate labeled glycerol into glycerolipids under all conditions studied. Therefore, insulin and glucagon may regulate hepatic glycerolipid biosynthesis in part by maintaining the liver cell's enzymatic rate of glycerolipid biosynthesis.
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PMID:Effects of chronic insulin and glucagon exposure on the biosynthesis of glycerolipids by cultured hepatocytes. 629 87