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1 Centre for Physical Activity and Nutrition, School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria 3125, Australia
2 St Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia
3 CSIRO Health Sciences and Nutrition, Parkville, 3052, Australia
To investigate the effect of exercise on protein kinase C (PKC) activity and localization in human skeletal muscle, eight healthy men performed cycle ergometer exercise for 40 min at 76 ± 1% the peak pulmonary O2 uptake 
, with muscle samples obtained at rest and after 5 and 40 min of exercise. PKC expression, phosphorylation and activities were examined by immunoblotting and in vitro kinase assays of fractionated and whole tissue preparations. In response to exercise, total PKC activity was slightly higher at 40 min in an enriched membrane fraction, and using a pSer-PKC-substrate motif antibody it was revealed that exercise increased the serine phosphorylation of a 
50 kDa protein. There were no changes in conventional PKC (cPKC) or PKC
activities; however, atypical PKC (aPKC) activity was 70% higher at 5 and 40 min, and aPKC expression and Thr410/403 phosphorylation were unaltered by exercise. There were no effects of exercise on the abundance of PKC
, PKC
, PKC and aPKC within cytosolic or enriched membrane fractions of skeletal muscle. These data indicate that aPKC, but not cPKC or PKC, are activated by exercise in contracting muscle suggesting a potential role for aPKC in the regulation of skeletal muscle function and metabolism during exercise in humans.
(Received 14 September 2004;
accepted after revision 4 October 2004;
first published online 7 October 2004)
Corresponding author M. Hargreaves: School of Exercise and Nutrition Sciences, Deakin University, Burwood, Victoria 3125, Australia. Email: mark.hargreaves{at}deakin.edu.au
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