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Tyrosine kinase-mediated signal transduction pathways and the actions of polypeptide growth factors and G-protein-coupled agonists in smooth muscle

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Abstract

This synopsis focuses on the role that tyrosine kinase pathways may play in the actue regulation of smooth muscle contractility by receptor-kinase-activating growth factors, such as epidermal growth factor-urogastrone (EGF-URO) and by G-protein-coupled agonists, such as angiotensin-II. Growth factor-activated response paradigms that modulate smooth muscle contractility are summarized and the parallels between the actions of G-protein-coupled agonists and growth factors in these response systems are pointed out. A possible dynamic interplay between tyrosine kinase and tyrosine phosphatase activities to modulate tissue tension is also hypothesized. Finally, a model is proposed, wherein an intermediary tyrosine kinase pathway is suggested as a point of convergence for the regulation of smooth muscle contractility by agonists as diverse as EGF-URO and angiotensin-II.

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  1. Endocrine Research Group, Departments of Pharmacology & Therapeutics and Medicine, The University of Calgary, Faculty of Medicine, 3330 Hospital Drive N.W., T2N 4N1, Calgary, Alberta, Canada

    Morley D. Hollenberg

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Hollenberg, M.D. Tyrosine kinase-mediated signal transduction pathways and the actions of polypeptide growth factors and G-protein-coupled agonists in smooth muscle. Mol Cell Biochem 149, 77–85 (1995). https://doi.org/10.1007/BF01076566

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