Activation of myocardial cAMP-dependent protein kinase by lysoplasmenylcholine

FEBS Letters
S D Williams, D A Ford

Abstract

Plasmalogen-specific, calcium-independent phospholipase A2 (iPLA2) is activated during myocardial ischemia. Accordingly, we have assessed the activation of myocardial protein kinases by the iPLA2 product, lysoplasmenylcholine. Lysoplasmenylcholine-activated protein kinase activity from heart cytosol fractionated on a DE-52 column was identified as cAMP-dependent protein kinase (PKA) based on the following: (1) protein kinase activity stimulated by cAMP and lysoplasmenylcholine co-eluted on sequential chromatographic steps; (2) lysoplasmenylcholine-activated protein kinase activity was inhibited by the PKA inhibitor, PKI; and (3) the unprimed PKA form generated from the primed form of PKA was activated by cAMP and lysoplasmenylcholine. These results demonstrate a novel mechanism for PKA activation by lysoplasmenylcholine.

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Citations

Jan 22, 2008·Cardiovascular Drugs and Therapy·E MaraisA Lochner
May 29, 2004·Biochimica Et Biophysica Acta·Pedro BritesRonald J A Wanders
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Jun 19, 2001·American Journal of Physiology. Heart and Circulatory Physiology·S D Williams, D A Ford
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Aug 31, 2020·Neurobiology of Disease·Fabian DorningerJohannes Berger

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