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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




Journal article


Experimental cell research

Publication Date





185 - 193


School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom.


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