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Thromb Haemost 2002; 88(02): 315-320
DOI: 10.1055/s-0037-1613204
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Intracellular Factor XIII Crosslinks Platelet Cytoskeletal Elements upon Platelet Activation

Katherine Serrano
1   Departments of Biochemistry and Molecular Biology, Canada
3   Departments of Canadian Blood Services, Vancouver, BC, Canada
,
Dana V. Devine
1   Departments of Biochemistry and Molecular Biology, Canada
2   Departments of Pathology and Laboratory Medicine, University of British Columbia, Canada
3   Departments of Canadian Blood Services, Vancouver, BC, Canada
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Publikationsverlauf

Received 08. Januar 2002

Accepted after revision 11. April 2002

Publikationsdatum:
07. Dezember 2017 (online)

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Summary

The platelet cytoplasm contains approximately half of the factor XIII (FXIII) transglutaminase content circulating in blood, yet the function of cytoplasmic FXIII is poorly understood. This study investigated functions of platelet FXIII in internal platelet processes by studying the interactions of FXIII with platelet cytoskeletal proteins. FXIII was present in cytoskeletal fractions of platelet lysate separated by centrifugation. When cytoskeletal fractions were immobilized on nitrocellulose membranes, thrombin-activated rFXIII (rFXIIIa*) or calcium iontreated rFXIII (rFXIIIa°) bound to some of these proteins, whereas untreated rFXIII did not. Utilizing fluorescence microscopy, an actin polymerization-dependent transient translocation of FXIII from a diffuse homogeneous distribution throughout the cytoplasm to the platelet periphery was observed upon platelet activation, suggesting an association with cytoskeletal proteins. Transglutaminase activity increased in cytoskeletal fractions of activated versus non-activated platelets. Immunoblotting analysis of platelet cytoskeletal fractions identified filamin and vinculin as being crosslinked upon platelet activation.

Keywords

Platelet activation - factor XIII - filamin - vinculin - crosslinking
 

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