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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Mast cell-dependent activation of pro matrix metalloprotease 2: a role for serglycin proteoglycan-dependent mast cell proteases

Anders Lundequist
  • Swedish University of Agricultural Sciences, Department of Molecular Biosciences, The Biomedical Center, P.O. Box 575, S-751 23 Uppsala, Sweden
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Magnus Åbrink
  • Swedish University of Agricultural Sciences, Department of Molecular Biosciences, The Biomedical Center, P.O. Box 575, S-751 23 Uppsala, Sweden
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Gunnar Pejler
  • Swedish University of Agricultural Sciences, Department of Molecular Biosciences, The Biomedical Center, P.O. Box 575, S-751 23 Uppsala, Sweden
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.189

Abstract

The formation of active matrix metalloprotease-2 (MMP-2) requires the proteolytic processing of proMMP-2, a process that can occur through the formation of a ternary complex between proMMP-2, the tissue inhibitor of metalloprotease-2 and membrane type 1-MMP. However, other activation mechanisms have been suggested, and in this study we investigated whether mast cells (MCs) may play a role in the activation of proMMP-2. Murine peritoneal cells, a mixture of macrophages, lymphocytes and MCs, were cultured ex vivo. Addition of proMMP-2 to resting peritoneal cell cultures resulted in only slow conversion of proMMP-2 into the active enzyme. However, when MC degranulation was provoked using a calcium ionophore, proMMP-2 processing was markedly enhanced. When the peritoneal cell populations were depleted in MCs, proMMP-2 processing was abrogated, but was reconstituted when purified MCs were added to the depleted cultures. ProMMP-2 processing was sensitive to serine protease inhibitors, but not to inhibitors of other classes of proteases. Furthermore, proMMP-2 processing was completely abrogated in cells lacking serglycin, a proteoglycan that has previously been shown to mediate storage of a variety of MC serine proteases. Taken together, these results suggest a novel mode of proMMP-2 activation mediated by serglycin-dependent MC serine proteases.

Keywords: chymase; mast cells; matrix metalloprotease; proteoglycan; serglycin

About the article

Corresponding author


Received: March 31, 2006

Accepted: May 31, 2006

Published Online: 2006-11-02

Published in Print: 2006-10-01


Citation Information: Biological Chemistry, Volume 387, Issue 10/11, Pages 1513–1519, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.189.

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