Vascular smooth muscle contractile elements cellular regulation

James T. Stull, Patricia J. Gallagher, B. Paul Herring, Kristine E. Kamm

Research output: Contribution to journalReview articlepeer-review

77 Scopus citations

Abstract

For many years the simple view was held that contractile force in smooth muscle was proportional to cytosolic Ca2+ concentrations ([Ca2+],). With the discovery that phosphorylation of myosin light chain by Ca2VcaImodulin-dependent myosin light chain kinase initiated contraction, regulation of the contractile elements developed more complex properties. Molecular and biochemical investigations have identified important domains of myosin light chain kinase: light chain binding sites, catalytic core, pseudosubstrate prototope, and calmodulin-binding domain. New protein phosphatase inhibitors such as okadaic acid and calyculin A should help In the identification of the physiologically important phosphatase and potential modes of regulation. The proposal of an attached, dephosphorylated myosin cross bridge (latch bridge) that can maintain force has evoked considerable controversy about the detailed functions of the myosin phosphorylation system. The latch bridge has been defined by a model based on physiological properties but has not been identified biochemically. Thin-filament proteins have been proposed as secondary sites of regulation of contractile elements, but additional studies are needed to establish physiological roles. Changes in the Ca2+ sensitivity of smooth muscle contractile elements with different modes of cellular stimulation may be related to inactivation of myosin light chain kinase or activation of protein phosphatase activities. Thus, contractile elements in smooth muscle cells are not dependent solely on [Ca2+] but use additional regulatory mechanisms. The immediate challenge is to define their relative importance and to describe molecular-biochemical properties that provide insights into proposed physiological functions.

Original languageEnglish (US)
Pages (from-to)723-732
Number of pages10
JournalHypertension
Volume17
Issue number6
DOIs
StatePublished - Jun 1991

Keywords

  • Calcium
  • Calmodulin
  • Contractile proteins
  • Myosin
  • Myosin light-chain kinase
  • Phosphorylation
  • Vascular smooth muscle

ASJC Scopus subject areas

  • Internal Medicine

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