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1 Department of Physiology and Developmental Biology, Brigham Young University, Provo, Utah, USA
* To whom correspondence should be addressed. E-mail: william_winder{at}byu.edu.
This study was designed to examine activity of AMP-activated protein kinase kinase (AMPKK) in muscles from non-trained and endurance trained rats. Rats were trained 5 days/wk, 2 hr/d for 8 wks at a final intensity of 32 m/min up a 15% grade with 30 second sprints at 53 m/min every 10 min. Gastrocnemius muscles were stimulated in situ in trained and non-trained rats for 5 min at frequencies of 0.4/sec and 1/sec. Gastrocnemius LKB1 protein, a putative component of the AMPKK complex (LKB1, STRAD, and MO25), increased approximately 2-fold in response to training. Phosphorylation of AMPK determined by western blot and AMPK activity of immunoprecipitates (both isoforms) were increased at both stimulation rates in both trained and non-trained muscles. AMPKK activity was 73% lower in resuspended polyethylene glycol precipitates of muscle extracts from the trained compared to non-trained rats. AMPKK activity did not increase in either trained or non-trained in response to electrical stimulation even though phospho-AMPK did increase. These results suggest that AMPKK is activated during electrical stimulation of both trained and non-trained muscle by mechanisms other than covalent modification.
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