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Molecular and Cellular Biochemistry

, Volume 176, Issue 1–2, pp 47–51 | Cite as

Smooth muscle contractility and protein tyrosine phosphorylation

  • Ashok K. Srivastava
  • Jean St-Louis
Article

Abstract

During the last 5 years several studies have documented an involvement of protein tyrosine kinases (PTKs) in smooth muscle contraction and Ca2+mobilization. Most of these studies have utilized highly selective inhibitors of PTKs, genistein and tyrphostin and have shown that these inhibitors attenuated smooth muscle contraction induced by growth factors - epidermal growth factor (EGF) and platelet derived growth factor (PDGF) and several vasoactive peptides. It has also been demonstrated that inhibitors of protein tyrosine phosphatases (PTPases) such as vanadate and pervanadate mimic growth factors and vasoactive peptides in causing the contraction of smooth muscle. In this brief review, we have summarized some of the recent observations suggesting a possible link between protein tyrosine phosphorylation pathway and smooth muscle contraction.

tyrosine kinases growth factors vanadate 

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Copyright information

© Kluwer Academic Publishers 1997

Authors and Affiliations

  • Ashok K. Srivastava
    • 1
  • Jean St-Louis
    • 2
  1. 1.Research Center, Hôtel-Dieu de Montréal, Department of MedicineUniversity of MontréalMontréalCanada
  2. 2.Research Center, St. Justine Hospital, Department of Obstetrics and GynecologyUniversity of MontréalMontréalCanada

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