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Blood, 1 November 2000, Vol. 96, No. 9, pp. 3064-3069
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Platelet release of trimolecular complex components
MT1-MMP/TIMP2/MMP2: involvement in MMP2 activation and
platelet aggregation
Isabelle Kazes,
Ismaïl Elalamy,
Jean-Daniel Sraer,
Mohamed Hatmi, and
Geneviève Nguyen
From INSERM U489 and Association Claude Bernard, Tenon
Hospital, and Unité de Pharmacologie Cellulaire, Unité
Associée, Pasteur Institute INSERM U485, Paris, France.
Matrix metalloproteinase 2 (MMP2) has been reported to be
secreted by collagen-stimulated platelets, and active MMP2 has been shown to play a role in platelet aggregation. It has been demonstrated that MMP2 activation is dependent on the complex (membrane type 1 [MT1]-MMP/tissue inhibitor of MMP2 [TIMP2]) receptor and MMP2. We
have investigated human platelets as a possible source of MT1-MMP, and
we have studied its role in MMP2 activation and in platelet aggregation. Gelatin zymograms showed the existence of MMP2 at proforms
(68 kd) and activated-enzyme forms (62-59 kd) in supernatants of
resting and activated platelets, respectively. No gelatinolytic activity was associated with the platelet pellet after aggregation, suggesting a total release of MMP2 during cell activation. By Western
blot analysis in nonreduced conditions, MT1-MMP was found on resting
platelet membranes in 2 forms-the inactive 45-kd form and an apparent
89-kd form, which totally disappeared under reduced conditions. After
platelet degranulation, only the 45-kd form was detected. Reverse
transcription-polymerase chain reaction experiments showed the
expression in platelets of messenger RNA encoding for MMP2, MT1-MMP,
and TIMP2. Flow cytometry analysis showed that MT1-MMP, MMP2, and TIMP2
expressions were enhanced at the activated platelet surface. MMP
inhibitors, recombinant TIMP2, and synthetic BB94 inhibited
collagen-induced platelet aggregation in a concentration-dependent
manner, indicating the role of activated MT1-MMP in the modulation of
platelet function. In conclusion, our results demonstrate the
expression of the trimolecular complex components (MT1-MMP/TIMP2/MMP2)
by blood platelets as well as the ability of MMP inhibitors to modulate
the aggregating response.
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