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Purinergic activation of a tyrosine kinase‐dependent pathway in cardiac cells
Author(s) -
Pucéat Michel
Publication year - 1998
Publication title -
drug development research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.582
H-Index - 60
eISSN - 1098-2299
pISSN - 0272-4391
DOI - 10.1002/(sici)1098-2299(199811/12)45:3/4<427::aid-ddr44>3.0.co;2-o
Subject(s) - fyn , purinergic receptor , proto oncogene tyrosine protein kinase src , tyrosine kinase , microbiology and biotechnology , phosphorylation , tyrosine phosphorylation , tyrosine protein kinase csk , kinase , biology , tyrosine , signal transduction , receptor tyrosine kinase , chemistry , biochemistry , sh2 domain , extracellular
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 PLCγ, the major PLC isoform in heart, and AE1, the predominant cardiac Cl/HCO 3 exchanger. Tyrosine kinase‐mediated phosphorylation of PLCγ 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. Drug Dev. Res. 45:427–433, 1998. © 1998 Wiley‐Liss, Inc.