Localization and translocation of MMP-2 during aggregation of human platelets.

Abstract:

: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.

journal_name

Thromb Haemost

authors

Sawicki G,Sanders EJ,Salas E,Wozniak M,Rodrigo J,Radomski MW

subject

Has Abstract

pub_date

1998-11-01 00:00:00

pages

836-9

issue

5

eissn

0340-6245

issn

2567-689X

pii

98110836

journal_volume

80

pub_type

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