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Articles in PresS, published online ahead of print August 22, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00474.2002
Submitted on June 6, 2002
Accepted on August 14, 2002
1 Physiology, University of South Alabama, Mobile, AL, USA
2 Physiology, University of South Alabama, Mobile, AL, USA; Medicine, University of South Alabama, Mobile, AL, USA
* To whom correspondence should be addressed. E-mail: mcohen{at}usouthal.edu.
Adenosine and acetylcholine (ACh) trigger preconditioning through different signaling pathways. We tested whether either could activate myocardial phosphatidylinositol (PI3)-kinase, a putative signaling protein in ischemic preconditioning. We used phosphorylation of Akt, a downstream target of PI3-kinase, as a reporter. Exposure of isolated rabbit hearts to ACh increased Akt phosphorylation 2.62 ± 0.33-fold (p=0.001), while adenosine caused a significantly smaller increase (1.52 ± 0.08-fold). ACh-induced activation of Akt was abolished by the tyrosine kinase blocker genistein indicating at least one tyrosine kinase between the muscarinic receptor and Akt. ACh-induced Akt activation was blocked by the Src tyrosine kinase inhibitor PP2 and by AG1478, an epidermal growth factor receptor (EGFR) inhibitor, suggesting phosphorylation of a receptor tyrosine kinase in a Src tyrosine kinase-dependent manner. ACh caused tyrosine phosphorylation of the EGFR which could be blocked by PP2 supporting this receptor hypothesis. AG1478 failed to block ACh's cardioprotection, however, suggesting that other receptor tyrosine kinases may be involved. Therefore, Gi protein-coupled receptors can activate PI3-kinase/Akt through transactivation of receptor tyrosine kinases in a Src tyrosine kinase-dependent manner.
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