Reorganization of myosin in surface-activated spreading platelets.
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.
D001792:Blood Platelets / Q000648:ultrastructure*; D003599:Cytoskeleton / Q000648:ultrastructure; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins; D005455:Fluorescent Antibody Technique; D005456:Fluorescent Dyes; D006801:Humans; D008854:Microscopy, Electron; D009218:Myosins / Q000097:blood* / Q000302:isolation & purification; D010974:Platelet Aggregation; D013861:Thiocyanates
D005452:Fluoresceins; D005456:Fluorescent Dyes; D013861:Thiocyanates; D009218:Myosins; D016650:Fluorescein-5-isothiocyanate