Reorganization of myosin in surface-activated spreading platelets

https://doi.org/10.1016/S0889-1605(86)80016-7Get rights and content

To study the localization of myosin in platelets, we utilized polyclonal antibody to heavy chain of platelet myosin. Both immunofluorescence and indirect immunogold staining techniques were employed. (1) In the unactivated platelets, myosin was distributed homogeneously throughout the cytosol. The cytosolic myosin was removed after platelets were treated with Triton X-100. The association of myosin with actin microfilaments in unactivated platelets was minimal. (2) In the surface-activated platelets, myosin was unextractable by Triton X-100. The myosin antibody heavily decorated the actin cable-networks which characterized the activated platelets. (3) In the Triton-unextractable cytoskeleton of both unactivated and activated platelets, we found fine fibrils (about 1-nm wide) that were often associated with immunogolds. These fibrils were similar to purified myosin molecules observed in rotary-shadowed metal replicas and ultrathin sections. These results indicate that cytosolic myosin becomes associated with actin cable-networks after the activation of platelets.

References (42)

  • BehnkeO. et al.

    J. Ultrastruct. Res.

    (1971)
  • Bettex-GallandM. et al.

    Biochim. Biophys. Acta

    (1961)
  • CarrollR.C. et al.

    Cell

    (1982)
  • DanielJ.L. et al.

    J. Biol. Chem.

    (1984)
  • FeinsteinM.B. et al.

    Biochem. Biophys. Res. Commun.

    (1983)
  • HaslamR.J. et al.

    Biochem. Biophys. Res. Commun.

    (1977)
  • JenningsL.K. et al.

    J. Biol. Chem.

    (1981)
  • KarlssonR. et al.

    Exp. Cell Res.

    (1985)
  • OnjiT. et al.

    Biochem. Biophys. Res. Commun.

    (1982)
  • OnjiT. et al.

    Biochem. Biophys. Res. Commun.

    (1985)
  • OnjiT. et al.

    Biochem. Biophys. Res. Commun.

    (1987)
  • PainterR.G. et al.

    Exp. Cell Res.

    (1984)
  • TanakaK. et al.

    J. Ultrastruct. Res.

    (1984)
  • TylerJ.M. et al.

    J. Ultrastruct. Res.

    (1980)
  • AdelsteinR.S. et al.

    Thromb. Haemostasis

    (1978)
  • ArmbrusterB.L. et al.

    J. Histochem. Cytochem.

    (1983)
  • BooyseF.M. et al.

    J. Histochem. Cytochem.

    (1971)
  • CohenI.

    Methods Achiev. Exp. Pathol.

    (1979)
  • CarlssonL. et al.
  • DanielJ.L. et al.

    Thromb. Haemostasis

    (1977)
  • DebusE. et al.

    Eur. J. Cell Biol.

    (1981)
  • Cited by (15)

    • Differential expression of wild-type and mutant NMMHC-IIA polypeptides in blood cells suggests cell-specific regulation mechanisms in MYH9 disorders

      2008, Blood
      Citation Excerpt :

      Upon contact with a glass surface, platelets change from a discoid to a spherical shape, extend filopodia, and spread with large sheetlike lamellipodia. Myosin becomes associated with actin and comigrates to the front of the lamellipodia, and associates with the granulomere zone.24-26 Biochemical analyses have also shown that activation increases the myosin content in the cytoskeleton.27,28

    View all citing articles on Scopus
    View full text