title: Seasonal changes in critical enzymes of lipogenesis and triacylglycerol synthesis in the marmot (Marmota flaviventris).
abstract: Fatty acid metabolism and triacylglycerol synthesis are critical processes for the survival of hibernating mammals that undergo a prolonged fasting period. Fatty acid synthase, fatty-acid-CoA ligase, diacylglycerol acyltransferase, and monoacylglycerol acyltransferase activities were measured in liver and in white and brown adipose tissue, in order to determine whether enzymes of lipogenesis and triacylglycerol synthesis vary seasonally during hibernation in the yellow-bellied marmot (Marmota flaviventris). Compared with mid-winter hibernation, fatty acid synthase activity was higher in all three tissues during early spring when marmots emerged from hibernation and in mid-summer when they were feeding, consistent with the synthesis of fatty acids from the carbohydrate-rich summer diet. Fatty-acid-CoA ligase and diacylglycerol acyltransferase activities were highest in summer in white adipose tissue when triacylglycerol synthesis would be expected to be high; diacylglycerol acyltransferase activity was also high in brown adipose tissue during spring and summer. In liver, however, diacylglycerol acyltransferase specific activity was highest during hibernation, suggesting that triacylglycerol synthesis may be prominent in liver in winter. Monoacylglycerol acyltransferase activity, which may aid in the retention of essential fatty-acids, was 80-fold higher in liver than in white or brown adipose tissue, but did not vary seasonally. Its dependence on palmitoyl-CoA suggests that a divalent cation might play a role in enzyme activation. The high hepatic diacylglycerol acyltransferase activity during hibernation suggests that the metabolism of very low density lipoprotein may be important in the movement of adipose fatty acids to brown adipose tissue and muscle during the rewarming that occurs periodically during hibernation.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Department of Nutrition, University of North Carolina at Chapel Hill 27599.
authors.forename: N
authors.initials: N
authors.lastname: Mostafa
authors.forename: D C
authors.initials: DC
authors.lastname: Everett
authors.forename: S C
authors.initials: SC
authors.lastname: Chou
authors.forename: P A
authors.initials: PA
authors.lastname: Kong
authors.forename: G L
authors.initials: GL
authors.lastname: Florant
authors.forename: R A
authors.initials: RA
authors.lastname: Coleman
mesh_terms: D000217:Acyltransferases / Q000378:metabolism; D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D003066:Coenzyme A Ligases / Q000378:metabolism; D064429:Fatty Acid Synthases / Q000378:metabolism; D006605:Hibernation / Q000502:physiology*; D008099:Liver / Q000201:enzymology* / Q000378:metabolism; D008392:Marmota / Q000378:metabolism*; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D012621:Seasons; D014280:Triglycerides / Q000096:biosynthesis*; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
chemical_list: D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D014280:Triglycerides; D000217:Acyltransferases; D064429:Fatty Acid Synthases; D003066:Coenzyme A Ligases; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase