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Am J Physiol Endocrinol Metab (June 4, 2002). doi:10.1152/ajpendo.00133.2002
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Articles in PresS, published online ahead of print June 4, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00133.2002
Submitted on March 26, 2002
Accepted on June 3, 2002

Insulin increases branched chain {alpha}-ketoacid dehydrogenase kinase expression in Clone 9 rat cells

Mary M. Nellis1, Christopher B. Doering1, Andrea Kasinski1, and Dean J. Danner1*

1 Deaprtment of Genetics and Graduate Program in Nutrition and Health Sciences, Emory University School of Medicine, Atlanta, GA, USA

* To whom correspondence should be addressed. E-mail: ddanner{at}emory.edu.

The branched chain amino acids [BCAA] are committed to catabolism by the activity of the branched chain {alpha}-ketoacid dehydrogenase [BCKD] complex. BCKD activity is regulated through the action of the complex-specific BCKD-kinase that phosphorylates two serine residues in the E1{alpha} subunit. Greater BCKD-kinase expression levels result in a lower activity-state of BCKD and thus a decreased rate of BCAA catabolism. Activity-state varies among tissues and can be altered by diet, exercise, hormones, and disease-state. Within individual tissues the concentration of BCKD-kinase reflects the activity-state of the BCKD complex. Here we investigated the effects of insulin, an important regulator of hepatic metabolic enzymes, on BCKD-kinase expression in Clone 9 rat cells. Insulin effected a 2-fold increase in message levels and a 2-fold increase in BCKD-kinase protein levels. The response was completely blocked by treatment with LY294002 and partially blocked by rapamycin, thus demonstrating a dependence on PI-3 kinase and mTOR function respectively. These studies suggest that insulin acts to regulate BCAA catabolism through stimulation of BCKD-kinase expression.




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