Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: Associated activation of gelatinase A, gelatinase B and collagenase 3

Cowell, Susan, Knauper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Stewart, Margaret L., D'ortho, Marie-Pia, Stanton, Heather, Hembrey, Rosalind M., López-Otín, Carlos, Reynolds, John J. and Murphy, Gillian 1998. Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: Associated activation of gelatinase A, gelatinase B and collagenase 3. Biochemical Journal 331 (2) , pp. 453-458. 10.1042/bj3310453

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Abstract

SW1353 chondrosarcoma cells cultured in the presence of interleukin-1, concanavalin A or PMA secreted procollagenase 3 (matrix metalloproteinase-13). The enzyme was detected in the culture medium by Western blotting using a specific polyclonal antibody raised against recombinant human procollagenase 3. Oncostatin M enhanced the interleukin-1-induced production of procollagenase 3, whereas interleukin-4 decreased procollagenase 3 synthesis. The enzyme was latent except when the cells had been treated with concanavalin A, when a processed form of 48 kDa, which corresponds to the active form, was found in the culture medium and collagenolytic activity was detected by degradation of 14C-labelled type I collagen. The concanavalin A-induced activation of procollagenase 3 coincided with the processing of progelatinase A (matrix metalloproteinase-2) by the cells, as measured by gelatin zymography. In addition, progelatinase B (matrix metalloproteinase-9) was activated when gelatinase A and collagenase 3 were in their active forms. Concanavalin A treatment of SW1353 cells increased the amount of membrane-type-1 matrix metalloproteinase protein in the cell membranes, suggesting that this membrane-bound enzyme participates in an activation cascade involving collagenase 3 and the gelatinases. This cascade was effectively inhibited by tissue inhibitors of metalloproteinases-2 and -3. Tissue inhibitor of metalloproteinases-1, which is a much weaker inhibitor of membrane-type 1 matrix metalloproteinase than tissue inhibitors of metalloproteinases-2 and -3 [Will, Atkinson, Butler, Smith and Murphy (1996) J. Biol. Chem. 271, 17119–17123], was a weaker inhibitor of the activation cascade.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Portland Press
ISSN:	0264-6021
Date of Acceptance:	29 January 1998
Last Modified:	18 Sep 2023 09:56
URI:	https://orca.cardiff.ac.uk/id/eprint/161591

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