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Am J Physiol Heart Circ Physiol (January 20, 2006). doi:10.1152/ajpheart.01206.2005
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Submitted on November 15, 2005
Accepted on January 17, 2006

Activation of Cardiac AMP-activated Protein Kinase (AMPK) by LKB1 Expression or Chemical Hypoxia is Blunted by Increased Akt Activity

Carrie-Lynn M Soltys1, Suzanne Kovacic1, and Jason R. B. Dyck1*

1 Departments of Pediatrics and Pharmacology, University of Alberta, Edmonton, Alberta, Canada

* To whom correspondence should be addressed. E-mail: jason.dyck{at}ualberta.ca.

AMPK plays a major role in the regulation of cardiac energy substrate utilization and can be negatively regulated by Akt activation in the heart. It has recently been shown that Akt directly phosphorylates the {alpha} subunit of AMPK{alpha}1/{alpha}2 on serine 485/491 in vitro, and prevents the AMPKK, LKB1, from phosphorylating AMPK{alpha} at its primary activation site, threonine 172 (Horman et al. 2005; J Biol Chem, in press). In order to determine if this is also the case in the cardiac myocyte, neonatal rat cardiac myocytes (NRCM) were infected with a recombinant adenovirus expressing a constitutively active mutant of Akt1 (myrAkt1) followed by infection with or without the adenoviruses expressing the active LKB1 complex. Expression of myrAkt1 blunted LKB1-induced phosphorylation of AMPK{alpha} at threonine 172, which resulted in a dramatic decrease in phosphorylation of AMPK's target, acetyl CoA carboxylase and was associated with prior Akt1-dependent phosphorylation of AMPK{alpha}1/{alpha}2 at serine 485/491. To investigate whether Akt1 activation was also able to prevent other AMPKKs from phosphorylating AMPK{alpha}, we subjected NRCM to chemical hypoxia and show a marked increase in the phosphorylation of AMPK{alpha} at threonine 172, despite no change in LKB1 activity. NRCM expressing myrAkt1 demonstrated increased phosphorylation of AMPK{alpha}1/{alpha}2 at serine 485/491 and a complete inhibition of chemical hypoxia-induced phosphorylation of AMPK{alpha} at threonine 172. Taken together, our data show that activation of Akt1 is able to prevent activation of cardiac AMPK by LKB1 and at least one other AMPKK, likely by prior phosphorylation of AMPK{alpha}1/{alpha}2 at serine 485/491.




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