Identification of a novel, actin-rich structure, the actin nodule, in the early stages of platelet spreading

J Thromb Haemost. 2008 Nov;6(11):1944-52. doi: 10.1111/j.1538-7836.2008.03141.x. Epub 2008 Aug 28.

Abstract

Background: During platelet spreading, the actin cytoskeleton undergoes marked changes, forming filopodia, lamellipodia and stress fibres. In the present study, we report the identification of a novel actin-rich structure, termed an actin nodule, which appears prior to lamellipodia and stress fibre formation.

Methods: Platelet spreading was monitored using human platelets and mouse GFP-actin platelets using real-time and end-point DIC, and fluorescent and electron microscopy (EM).

Results: We identified a small, novel actin structure, the actin nodule, in the early stages of adhesion and spreading, which we hypothesize to be a precursor of lamellipodia and stress fibres. Nodule formation shows an inverse correlation to Rho kinase and myosin-II activity, is independent of PI3-kinase, but dependent on Src kinase activity. Actin nodules contain multiple proteins, including Arp2/3, Fyn, Rac, and beta1- and beta3- integrins, but not Src. EM analysis revealed that actin filaments extend in all directions from the nodules. Actin nodules are present on multiple matrices, including fibrinogen, laminin and VWF + botrocetin.

Conclusion: This work identifies a novel platelet actin structure, which we propose is a precursor to both lamellipodia and stress fibres and acts to drive platelet spreading.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Actins / ultrastructure*
  • Animals
  • Blood Platelets / cytology
  • Blood Platelets / ultrastructure*
  • Cell Shape
  • Cytoskeleton
  • Humans
  • Mice
  • Microscopy, Electron
  • Platelet Adhesiveness
  • Pseudopodia
  • Stress Fibers

Substances

  • Actins