A major role for the rho-associated coiled coil forming protein kinase in G-protein-mediated Ca2+ sensitization through inhibition of myosin phosphatase in rabbit trachea

Br J Pharmacol. 1999 Oct;128(4):925-33. doi: 10.1038/sj.bjp.0702864.

Abstract

1 G protein-mediated Ca2+ sensitization of airway smooth muscle contraction was investigated with respect to the relative importance of Rho-associated coiled coil forming protein kinase (ROCK) and protein kinase C (PKC). We examined the effects of Y-27632, a ROCK inhibitor, and GF 109203X, a PKC inhibitor, on guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS)-induced contraction in alpha-toxin- or beta-escin-permeabilized rabbit trachea. 2 Although pre-treatment with Y-27632 dose-dependently inhibited GTPgammaS (10 microM)-induced Ca2+ sensitization of alpha-toxin-permeabilized trachea, a Y-27632-insensitive component (approximately 16% of the maximum contraction) was retained during the early phase of the GTPgammaS response in the presence of Y-27632 (100 microM). 3 GF 109203X (5 microM) abolished 1 microM 4beta-phorbol 12, 13-dibutyrate (PDBu)-induced, but only partially inhibited the GTPgammaS-induced Ca2+ sensitization. A combination of Y-27632 (100 microM) and GF 109203X (5 microM) totally abolished the GTPgammaS response. 4 GTPgammaS caused only a small contraction in the absence of Ca2+. Wortmannin (30 microM), a myosin light chain kinase (MLCK) inhibitor, completely inhibited Ca2+-induced contraction. ATP-triggered contraction of the strip which had been treated with calyculin A (1 microM), a phosphatase inhibitor, in rigor solutions was markedly slowed by worthmannin (30 microM), but not by Y-27632 (100 microM), in the presence of GTPgammaS and Ca2+. 5 GTPgammaS, but not PDBu, contracted the beta-escin-permeabilized trachea in the absence of Ca2+, but the presence of Ca2+-independent MLCK. 6 We conclude that ROCK plays a primary role in G-protein-mediated Ca2+ sensitization, which requires MLCK activity, with minor contribution of PKC to the early phase of contraction, and PDBu utilizes conventional PKC(s) in airway smooth muscle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amides / pharmacology
  • Animals
  • Calcium / metabolism*
  • Enzyme Inhibitors / pharmacology
  • GTP-Binding Proteins / physiology*
  • Guanosine 5'-O-(3-Thiotriphosphate) / metabolism
  • Indoles / pharmacology
  • Intracellular Signaling Peptides and Proteins
  • Maleimides / pharmacology
  • Myosin-Light-Chain Phosphatase
  • Phorbol 12,13-Dibutyrate / pharmacology
  • Phosphoprotein Phosphatases / antagonists & inhibitors*
  • Protein Serine-Threonine Kinases / antagonists & inhibitors
  • Protein Serine-Threonine Kinases / physiology*
  • Pyridines / pharmacology
  • Rabbits
  • Trachea / drug effects
  • Trachea / enzymology
  • Trachea / metabolism*
  • rho-Associated Kinases

Substances

  • Amides
  • Enzyme Inhibitors
  • Indoles
  • Intracellular Signaling Peptides and Proteins
  • Maleimides
  • Pyridines
  • Y 27632
  • Phorbol 12,13-Dibutyrate
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • Protein Serine-Threonine Kinases
  • rho-Associated Kinases
  • Phosphoprotein Phosphatases
  • Myosin-Light-Chain Phosphatase
  • GTP-Binding Proteins
  • bisindolylmaleimide I
  • Calcium