Effects of High Carbohydrate and High Fat Diets on Rat Adipose Tissue Pyruvate Dehydrogenase Responses to Concanavalin A and Spermine*

Endocrinology ◽  
1982 ◽  
Vol 111 (5) ◽  
pp. 1491-1497 ◽  
Author(s):  
NAJMA BEGUM ◽  
HELEN M. TEPPERMAN ◽  
JAY TEPPERMAN
1964 ◽  
Vol 206 (3) ◽  
pp. 603-609 ◽  
Author(s):  
Adawia A. Alousi ◽  
Samuel Mallov

Rats were fasted for several days, placed on diets high in carbohydrate, fat, or containing iodinated casein so as to produce hyperthyroidism, or were chronically injected with epinephrine. Lipoprotein lipase (LPL) activities of homogenates of the hearts of these animals were determined. Significant increases in LPL activity occurred in thyrotoxic animals, in rats receiving epinephrine injections chronically, or after prolonged fasting, while significant lowering of cardiac LPL activity was observed in rats on the high-carbohydrate or high-fat diets. Single doses of fat or single injections of epinephrine had no effect. Addition of epinephrine or of triiodothyronine to heart slices or homogenates in vitro caused no LPL increases. It is postulated that adaptive changes in cardiac LPL activity may occur in response to altered needs for utilization of fatty acids by the heart. Microsomal fractions of heart cells had the highest specific LPL activities, suggesting synthesis of the enzyme by these cellular components, or activity of the enzyme at the endoplasmic reticulum.


1987 ◽  
Vol 117 (6) ◽  
pp. 1115-1120 ◽  
Author(s):  
Colleen K. Grogan ◽  
Hye-Kyung Kim ◽  
Dale R. Romsos

Metabolism ◽  
1984 ◽  
Vol 33 (11) ◽  
pp. 1003-1010 ◽  
Author(s):  
Paul D. Thompson ◽  
Eileen M. Cullinane ◽  
Ruth Eshleman ◽  
Mark A. Kantor ◽  
Peter N. Herbert

1991 ◽  
Vol 72 (2) ◽  
pp. 432-437 ◽  
Author(s):  
MARK BORKMAN ◽  
LESLEY V. CAMPBELL ◽  
DONALD J. CHISHOLM ◽  
LEONARD H. STORLIEN

2019 ◽  
Vol 60 (6) ◽  
pp. 1112-1120 ◽  
Author(s):  
Chandramohan Chitraju ◽  
Tobias C. Walther ◽  
Robert V. Farese

Mammals store metabolic energy as triacylglycerols (TGs) in adipose tissue. TG synthesis is catalyzed by the evolutionarily unrelated acyl-CoA:diacylglycerol acyltransferase (DGAT) enzymes DGAT1 and DGAT2, which catalyze the same reaction and account for nearly all TG synthesis. The reasons for their convergent evolution to synthesize TGs remain unclear. Mice lacking DGAT1 are viable with reduced fat stores of TGs, whereas DGAT2 KO mice die postnatally just after birth with >90% reduction of TGs, suggesting that DGAT2 is the predominant enzyme for TG storage. To better understand the functional differences between the DGATs, we studied mice fed chow or high-fat diets lacking either enzyme in adipose tissue. Unexpectedly, mice lacking DGAT2 in adipocytes have normal TG storage and glucose metabolism on regular or high-fat diets, indicating DGAT2 is not essential for fat storage. In contrast, mice lacking DGAT1 in adipocytes have normal TG storage on a chow diet but moderately decreased body fat accompanied by glucose intolerance when challenged with a high-fat diet. The latter changes were associated with the activation of ER stress pathways. We conclude that DGAT1 and DGAT2 can largely compensate for each other for TG storage but that DGAT1 uniquely has an important role in protecting the ER from the lipotoxic effects of high-fat diets.


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