Thrombin-induced activation of RhoA in platelet shape change

S. L. Bodie, Isobel Ford, Michael Greaves, Graeme Fleming Nixon

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


Thrombin-induced activation of RhoA and its involvement in the regulation of myosin II light chain(20) phosphorylation (MLC-P) in alpha -toxin permeabilized platelets was investigated. Permeabilized platelets, expressing normal levels of P-selectin, displayed a Ca2+-dependent increase in shape change and MLC-P. Thrombin activated RhoA as measured by a rhotekin-binding assay within 30 s of stimulation under conditions of constant [Ca2+](i). Under the same conditions and timecourse, thrombin or GTP gammaS induced an increase in MLC-P and platelet shape change which was not dependent on an increase in [Ca2+](i). The thrombin- and GTP gammaS-induced MLC-P in constant [Ca2+](i) was inhibited by the addition of Y27632, a Rho-kinase inhibitor. This study directly demonstrates that thrombin can activate RhoA in platelets in a timecourse compatible with a role in increasing MLC-P and shape change (not involving an increase in [Ca2+](i)). This is also Rho-kinase-dependent. (C) 2001 Academic Press.

Original languageEnglish
Pages (from-to)71-76
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2001


  • rho
  • rho-kinase
  • platelet shape change
  • thrombin
  • myosin light chain phosphorylation
  • myosin light-chain
  • binding protein-RHO
  • smooth-muscle
  • kinase
  • phosphorylation
  • phosphatase
  • calcium
  • pathway
  • cytoskeleton
  • secretion


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