Abstract
This overview focuses on the role of cytosoluble tyrosine kinases in the purinergic regulation of cardiac function. Cardiac cells express many cytosolic tyrosine kinases, including pp60c-src, p59c-fyn, Csk, FAK, and Tec. Purinergic stimulation of cardiomyocytes increases the activity of pp60c-src and p59c-fyn and induces phosphorylation of FAK. This signaling pathway leads to phosphorylation of many proteins, including PLCγ, the major PLC isoform in heart, and AE1, the predominant cardiac Cl/HCO3 exchanger. Tyrosine kinase-mediated phosphorylation of PLCγ and AE1 allows the cardiomyocyte to regulate both its Ca2+ and H+ homeostasis, respectively. The existence of other cardiac intracellular substrates of tyrosine kinases, targets of the purinergic stimulation as well as the physiological relevance of this signaling pathway, is discussed. Drug Dev. Res. 45:427–433, 1998. © 1998 Wiley-Liss, Inc.
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