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Immunocytochemical studies demonstrate that annexin V relocates to the plasma membranes of intact stimulated blood platelets. Anti-annexin V antibodies label the cytoplasmic side of the substrate-adherent plasma membrane of mechanically unroofed, glass-activated platelets and colocalize with actin. In addition, crosslinking experiments using detergent-solubilized membranes of activated platelets have identified an 85-kDa complex containing annexin V. The 85-kDa complex is also recognized by antibodies against actin, suggesting that annexin V interacts with actin. In addition, annexin V was found to associate with filamentous actin in the presence of millimolar Ca(2+). Annexin V was also shown by immunofluorescence microscopy to be associated with platelet cytoskeletons, colocalizing with actin in the presence of micromolar Ca(2+). These findings provide the first evidence for annexin V binding to the plasma membrane and to the actin-based cytoskeleton in activated platelets and indicate that annexin V may function in both cytoskeletal and membrane domains.

Original publication

DOI

10.1006/excr.1999.4553

Type

Journal article

Journal

Exp Cell Res

Publication Date

25/08/1999

Volume

251

Pages

185 - 193

Keywords

Actin Cytoskeleton, Actins, Annexin A5, Blood Platelets, Calcium, Cell Adhesion, Cell Membrane, Cell Size, Cross-Linking Reagents, Cytochalasins, Cytoskeleton, Egtazic Acid, Fixatives, Fluorescent Antibody Technique, Glass, Humans, Molecular Weight, Platelet Activation, Protein Binding, Pseudopodia