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Papers In Press, published online ahead of print June 4, 2004
Biochemistry Dept., University of Wisconsin-Madison, Madison, WI 53706
Corresponding Author: ntambi{at}biochem.wisc.edu
Stearoyl-CoA desaturase catalyzes the rate-limiting step in the biosynthesis of monounsaturated fatty acids, which are required for normal rates of synthesis of triglycerides, cholesterol esters and phospholipids. Mice with a targeted disruption of the stearoyl-CoA desaturase 1 (SCD1) isoform are protected against diet and leptin deficiency-induced adiposity, have increased energy expenditure and have up regulated expression of hepatic genes encoding enzymes of fatty acid b-oxidation. Because peroxisome proliferator-activated receptor-a (PPARa) is a key transcription factor that induces the transcription of b-fatty acid oxidation and thermogenic genes, we hypothesized that the increased fatty acid oxidation observed in SCD1 deficiency is dependent on activation of the PPAR-a pathway. Here we show that mice nullizygous for SCD1 and PPAR-a are still protected against adiposity, have increased energy expenditure and maintain high expression of PPARa-target genes in liver and brown adipose tissue. The SCD deficiency rescued hepatic steatosis of the PPARa-/- mice. The SCD mutation increased the phosphorylation of both AMP-activated protein kinase and acetyl-CoA carboxylase thereby increasing CPT activity and stimulating the oxidation of liver palmitoyl-CoA in the PPARa null mice. The findings indicate that the reduced adiposity, reduced liver steatosis, increased energy expenditure and increased expression of PPARa-target genes associated with SCD1 deficiency are independent of activation of the PPAR-a pathway.
J. Biol. Chem, 10.1074/jbc.M405327200
Submitted on May 12, 2004
Revised on June 4, 2004
Accepted on June 4, 2004
Reduced adiposity and liver steatosis by stearoyl-CoA desaturase deficiency are independent of peroxisome proliferator-activated receptor-a
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