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Inhibition of SERPINE1 Function Attenuates Wound Closure in Response to Tissue Injury: A Role for PAI-1 in Re-Epithelialization and Granulation Tissue Formation

Center for Cell Biology & Cancer Research, Albany Medical College, Albany, New York, NY 12208, USA
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Academic Editor: Robin Muise-Helmericks
J. Dev. Biol. 2015, 3(1), 11-24; https://doi.org/10.3390/jdb3010011
Received: 13 January 2015 / Revised: 10 February 2015 / Accepted: 12 February 2015 / Published: 2 March 2015
(This article belongs to the Special Issue Wound Healing and Tissue Regeneration)
Plasminogen activator inhibitor-1 (PAI-1; SERPINE1) is a prominent member of the serine protease inhibitor superfamily (SERPIN) and a causative factor of multi-organ fibrosis as well as a key regulator of the tissue repair program. PAI-1 attenuates pericellular proteolysis by inhibiting the catalytic activity of both urokinase and tissue-type protease activators (uPA and tPA) effectively modulating, thereby, plasmin-mediated fibrinolysis and the overall pericellular proteolytic cascade. PAI-1 also impacts cellular responses to tissue injury and stress situations (growth, survival, migration) by titering the locale and temporal activation of multimeric cell-surface signaling complexes. This review will describe PAI-1 structure and function and detail the role of PAI-1 in the tissue repair program with an emphasis on cutaneous wound healing. View Full-Text
Keywords: SERPINE1; PAI-1; migration; proliferation; pericellular proteolysis; tiplaxtinin; fibrosis; TGF-β; wound healing; apoptosis SERPINE1; PAI-1; migration; proliferation; pericellular proteolysis; tiplaxtinin; fibrosis; TGF-β; wound healing; apoptosis
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Simone, T.M.; Higgins, P.J. Inhibition of SERPINE1 Function Attenuates Wound Closure in Response to Tissue Injury: A Role for PAI-1 in Re-Epithelialization and Granulation Tissue Formation. J. Dev. Biol. 2015, 3, 11-24.

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