Suppression of hepatocyte fatty acid synthesis by albumin-bound linoleate involves depolymerization of acetyl-CoA carboxylase filaments.
Digitonin treatment of chick liver cells in monolayer culture results in plasma membrane perforations due to digitonin removal of membrane cholesterol. The amount and rate of acetyl-CoA carboxylase activity that escapes from the hepatocyte during digitonin treatment is positively related to the amount of protomeric carboxylase in the cells. Incubation of chick liver cells in culture with albumin-bound linoleate (60 min) caused a 3-fold increase in the amount of carboxylase activity released during exposure of cells to digitonin. Concomitant with the enhanced release of carboxylase activity was an 85% reduction in fatty acid synthesis induced by linoleate. Apparently, acute suppression of hepatocyte fatty acid synthesis by media free fatty acids resulted, in part, from a change in carboxylase conformation from the active polymeric state to the inactive protomeric form.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000818:Animals; D003994:Bucladesine / Q000494:pharmacology; D002462:Cell Membrane / Q000187:drug effects; D002645:Chickens; D004072:Digitonin / Q000494:pharmacology; D005227:Fatty Acids / Q000096:biosynthesis*; D008025:Ligases / Q000378:metabolism*; D008041:Linoleic Acids / Q000494:pharmacology*; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D046911:Macromolecular Substances; D008297:Male; D011487:Protein Conformation
D005227:Fatty Acids; D008041:Linoleic Acids; D046911:Macromolecular Substances; D003994:Bucladesine; D008025:Ligases; D000103:Acetyl-CoA Carboxylase; D004072:Digitonin