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Matrix Metalloproteinase-10 Effectively Reduces Infarct Size in Experimental Stroke by Enhancing Fibrinolysis via a Thrombin-Activatable Fibrinolysis Inhibitor–Mediated Mechanism
Author(s) -
Josune Orbe,
Jaione Barrenetxe,
José Antonio Rodríguez,
Denis Vivien,
Cyrille Orset,
William C. Parks,
Timothy P. Birkland,
Rosario Serrano,
Ana Purroy,
Sara Martínez de Lizarrondo,
Eduardo AnglésCano,
José A. Páramo
Publication year - 2011
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/circulationaha.111.047100
Subject(s) - fibrinolysis , plasmin , medicine , fibrin , thrombin , tissue plasminogen activator , matrix metalloproteinase , plasminogen activator , pharmacology , plasminogen activator inhibitor 1 , in vivo , immunology , chemistry , biochemistry , platelet , biology , enzyme , microbiology and biotechnology
The fibrinolytic and matrix metalloproteinase (MMP) systems cooperate in thrombus dissolution and extracellular matrix proteolysis. The plasminogen/plasmin system activates MMPs, and some MMPs have been involved in the dissolution of fibrin by targeting fibrin(ogen) directly or by collaborating with plasmin. MMP-10 has been implicated in inflammatory/thrombotic processes and vascular integrity, but whether MMP-10 could have a profibrinolytic effect and represent a promising thrombolytic agent is unknown.

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