Regulation of PDH activity and isoform expression: diet and exercise.
During exercise in human skeletal muscle, the proportion of carbohydrate derived acetyl-CoA is determined at least in part by the activity of the PDH (pyruvate dehydrogenase) complex. Inhibition of the complex is achieved through reversible phosphorylation of the E1 subunit by a family of PDH kinase isoforms (PDK1-4) while dephosphorylation and activation of the complex is catalysed by a pair of intrinsic PDH phosphatases (PDP1 and 2). In general, the relative activity of the kinases and phosphatases is determined by a host of intramitochondrial effectors which signal energy charge, substrate and product accumulation, muscle contraction and nutritional status. This review focuses on advances in our understanding in human skeletal muscle of the regulatory signals and changes in gene expression which are important during acute exercise and exercise training, as well as in prolonged situations of altered nutritional status.
Peters
S J
SJ
Faculty of Applied Health Sciences, Brock University, St Catharines, Ontario, Canada L2S 3A1. sandra.peters@brocku.ca
D002384:Catalysis; D004032:Diet; D015444:Exercise; D006019:Glycolysis; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*; D019289:Pyruvic Acid / Q000378:metabolism
D007527:Isoenzymes; D011768:Pyruvate Dehydrogenase Complex; D019289:Pyruvic Acid