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.
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Research Article|
April 15 1998
Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3
Susan COWELL;
Susan COWELL
1
*Department of Cell and Molecular Biology, Strangeways Research Laboratory, Worts' Causeway, Cambridge, CB1 4RN, U.K.
1To whom correspondence should be addressed.
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Vera KNÄUPER;
Vera KNÄUPER
2
*Department of Cell and Molecular Biology, Strangeways Research Laboratory, Worts' Causeway, Cambridge, CB1 4RN, U.K.
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Margaret L. STEWART;
Margaret L. STEWART
2
*Department of Cell and Molecular Biology, Strangeways Research Laboratory, Worts' Causeway, Cambridge, CB1 4RN, U.K.
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Marie-Pia D'ORTHO;
Marie-Pia D'ORTHO
†Unité INSERM U296, Faculté de Médicine de Créteil, 8 Avenue du Général Sarrail, F-94010 Créteil, France
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Heather STANTON;
Heather STANTON
2
*Department of Cell and Molecular Biology, Strangeways Research Laboratory, Worts' Causeway, Cambridge, CB1 4RN, U.K.
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Rosalind M. HEMBRY;
Rosalind M. HEMBRY
*Department of Cell and Molecular Biology, Strangeways Research Laboratory, Worts' Causeway, Cambridge, CB1 4RN, U.K.
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Carlos LÓPEZ-OTÍN;
Carlos LÓPEZ-OTÍN
‡Departmento de Bioquímica y Biología Molecular, Universidad de Oviedo, 33006 Oviedo, Spain
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John J. REYNOLDS;
John J. REYNOLDS
§Department of Orthodontics and Paediatric Dentistry, United Medical and Dental Schools of Guy's and St. Thomas's Hospital, Floor 22, Guy's Tower, London SE1 9RT, U.K.
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Gillian MURPHY
Gillian MURPHY
2
*Department of Cell and Molecular Biology, Strangeways Research Laboratory, Worts' Causeway, Cambridge, CB1 4RN, U.K.
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Publisher: Portland Press Ltd
Received:
November 14 1997
Revision Received:
December 01 1997
Accepted:
January 29 1998
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1998
1998
Biochem J (1998) 331 (2): 453–458.
Article history
Received:
November 14 1997
Revision Received:
December 01 1997
Accepted:
January 29 1998
Citation
Susan COWELL, Vera KNÄUPER, Margaret L. STEWART, Marie-Pia D'ORTHO, Heather STANTON, Rosalind M. HEMBRY, Carlos LÓPEZ-OTÍN, John J. REYNOLDS, Gillian MURPHY; Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3. Biochem J 15 April 1998; 331 (2): 453–458. doi: https://doi.org/10.1042/bj3310453
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