Human skeletal muscle pyruvate dehydrogenase phosphatase activity and expression : the effect of aerobic capacity


Autoria(s): Love, Lorenzo Kenward.
Contribuinte(s)

Applied Health Sciences Program

Data(s)

16/02/2010

16/02/2010

16/02/2009

Resumo

Activation of pyruvate dehydrogenase (PDH), which converts pyruvate into acetyl-CoA, is accomplished by a pair of specific phosphatases (PDP 1 & 2). A cross-sectional study investigating the effect of aerobic capacity on PDP activity and expression found that: 1) PDP activity and PDP! protein expression were positively correlated with most aerobic capacity measures in males (n=lS), but not females (n=12); 2) only males showed a positive correlation between PDP activity and PDPl protein expression (r=0.47; p=O.05), indicating that the increase in PDP activity in males is largely explained by increased PDPl protein expression, but that females rely on another level for PDP activity regulation; and 3) PDP} and Ela protein expression increase in unison when expressed relative to the E2 core. These data suggest that with increased aerobic capacity there is an increased capacity for carbohydrate oxidation through PDH, via El a, and an increased ability to activate PDH, via PDP, when exercising maximally.

Identificador

http://hdl.handle.net/10464/2909

Idioma(s)

eng

Publicador

Brock University

Palavras-Chave #Dehydrogenases. #Striated muscle--Metabolism. #Exercise--Physiological aspects.
Tipo

Electronic Thesis or Dissertation