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Thromb Haemost 1998; 80(05): 836-839
DOI: 10.1055/s-0037-1615367
Review Article
Schattauer GmbH

Localization and Translocation of MMP-2 during Aggregation of Human Platelets

Grzegorz Sawicki
1   From the Departments of Pharmacology, Edmonton, Canada
,
Esmond J. Sanders
2   From the Departments of Physiology, University of Alberta, Edmonton, Canada
,
Eduardo Salas
3   Division of Research, Lacer SA, Barcelona, Spain
,
Mieczyslaw Wozniak
4   Department of Clinical Chemistry, Wroclaw University of Medicine, Wroclaw, Poland
,
Jose Rodrigo
5   Department of Comparative Neuroanatomy, Cajal Institute, Madrid, Spain
,
Marek W. Radomski
1   From the Departments of Pharmacology, Edmonton, Canada
3   Division of Research, Lacer SA, Barcelona, Spain
› Author Affiliations
Further Information

Publication History

Received 13 February 1998

Accepted after resubmission 24 July 1998

Publication Date:
07 December 2017 (online)

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Summary

We have previously shown that human platelets express matrix metalloproteinase-2 (MMP-2) and that the release of this enzyme during platelet activation mediates the ADP- and thromboxane-independent part of aggregation. We have now used immunogold electron microscopy, flow cytometry, Western blot analysis and zymography methods to study the ultrastructural localization of MMP-2 in human washed platelets. Platelet aggregation was stimulated by collagen and the MMP-2 immunoreactivity of platelets was followed during various stages of aggregation. In resting platelets, MMP-2 was randomly distributed in the platelet cytosol without detectable association with platelet granules. Platelet aggregation caused the translocation of MMP-2 from the cytosol to the extracellular space. During the early stages of aggregation, MMP-2 remained in close association with the platelet plasma membrane. We conclude that the interactions of MMP-2 with platelet surface membranes mediate the aggregatory response induced by this enzyme.

 

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