By Han A. A. van Heugten, Yvonne E. G. Eskildsen-Helmond, Henriette W. de Jonge (auth.), Jos M. J. Lamers, Pieter D. Verdouw (eds.)
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Extra resources for Biochemistry of Signal Transduction in Myocardium
Protein kinase C isozymes are responsible for phosphorylation of specific cardiac substrate proteins that may be involved in regulation of cardiac contractility, hypertrophic growth, gene expression, ischemic preconditioning and electrophysiological changes. The initial product of phospholipase D, phosphatidic acid, may also have a second messenger role. As in other tissues, the question how the activity of phospholipase D is controlled by agonists in myocardium is controversial. Agonists, such as endothelin-l, atrial natriuretic factor and angiotensin II that are shown to activate phospholipase D, also potently stimulate phospholipase C-~ in myocardium.
Interestingly, in the platelet the effects of cGK on Ca are mimicked by cAK, suggesting that both protein kinases share a common target. Indeed, a proline-rich, microfilament- and focal adhesion-associated protein termed VASP was shown to be phosphorylated in vivo by both cGK and cAK and may serve as a convergence point for the cAMP and cGMP pathway in platelets [59,60]. The recent identification ofVASP in a variety of other cell types, including cardiomyocytes, where it was found in association with the intercalating discs , and in endothelial cells , suggests a more general role of this protein in cyclic nucleotide-regulated processes.
I'2' allowed receptors that normally couple to the latter, to couple to a q . Other mutagenesis studies indicated the importance of the C-terminus in regulating GDP affinity . Since receptor affects this affinity by binding to the C-terminus, it probably induces a conformational change in this region that allows the release ofGDP. Nevertheless, other regions in close proximity to the C-terminus, including the N-terminus , may also interact with receptor. Interaction with f3r dimer The N-terminus is the region of the a subunit essential for binding of the ~y subunit, and was -like the adjacent C-terminus - disordered in the crystals [10, 11].