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Purinergic activation of a tyrosine kinase-dependent pathway in cardiac cells

✍ Scribed by Michel Pucéat

Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
163 KB
Volume
45
Category
Article
ISSN
0272-4391

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✦ Synopsis

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 pp60 c-src , p59 c-fyn , Csk, FAK, and Tec. Purinergic stimulation of cardiomyocytes increases the activity of pp60 c-src and p59 c-fyn and induces phosphorylation of FAK. This signaling pathway leads to phosphorylation of many proteins, including PLCg, the major PLC isoform in heart, and AE1, the predominant cardiac Cl/HCO 3 exchanger. Tyrosine kinase-mediated phosphorylation of PLCg and AE1 allows the cardiomyocyte to regulate both its Ca 2+ 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.

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