Cited by 126Protease and Inhibitor MechanismsMast cells and histamineVeterinary Oncology Research

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Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase.

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Fang, K C, Raymond, W W, Lazarus, S C, Caughey, G H·1996·Journal of Clinical Investigation

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Abstract

Gelatinolytic metalloproteinases implicated in connective tissue remodeling and tumor invasion are secreted from several types of cells in the form of inactive zymogens. In this report, characterization of gelatinase activity secreted by the BR line of dog mastocytoma cells reveals a phorbol-inducible, approximately 92-kD, Ca2+ - and Zn2+ -dependent proenzyme cleaved over time to smaller, active forms. Incubation of cells with the general serine protease inhibitor, PMSF, prevented proenzyme cleavage and permitted its purification free of activation products. The NH2-terminal 13 amino acids of the purified mastocytoma progelatinase are 50-67% identical to those of human, mouse, and rabbit 92-kD progelatinase (gelatinase B; matrix metalloproteinase-9). Degranulation of mastocytoma cells using ionophore A23187 greatly accelerated proenzyme cleavage, suggesting that a serine protease present in secretory granules hydrolyzed the progelatinase to active fragments. To identify the activating protease, cells were coincubated with ionophore and a panel of selective serine protease inhibitors. Soybean trypsin inhibitor and succinyl-L-Ala-Ala-Pro-Phe-chloromethylketone, which inhibit mast cell chymase, prevented progelatinase activation. Inhibitors of tryptase and dog mast cell protease (dMCP)-3, i.e., aprotinin or bis(5-amidino-2-benzimidazolyl) methane (BABIM), did not. In further experiments using highly purified enzymes, mastocytoma cell chymase activated 92-kD progelatinase in the absence of other enzymes or cofactors; tryptase and dMCP-3, however, had no effect. These data demonstrate that dog mastocytoma cells secrete a metalloproteinase related to progelatinase B that is directly activated outside of the cell by exocytosed chymase, and provide the first demonstration of a cell that activates a matrix metalloproteinase it secretes by cosecreting an activating enzyme. In mastocytomas, this pathway may facilitate tumor invasion of surrounding tissues, and in normal mast cells, it could play a role in tissue remodeling and repair.

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Authors: Fang, K. C., Raymond, W. W., Lazarus, S. C., & Caughey, G. H.
Affiliations: University of California, San Francisco (US)
ORCID: Lazarus, S C
Caughey, G H
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 1996-04-01
Volume: 97
Issue: 7
Pages: 1589-1596
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci118583
PMC: PMC507221
OpenAlex: W1967763193
Cited by: 125
References: 40
Citations by year: 2025: 2 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 8 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 4 · 2014: 7 · 2013: 2 · 2012: 5
FWCI: 1.79
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Lung Association
National Institutes of Health (HL24136)
National Heart, Lung, and Blood Institute (F32HL009133, HL 24136, P01HL024136, HL 07185, HL09133)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Life Sciences › Immunology and Microbiology › Immunology › Mast cells and histamine
Health Sciences › Veterinary › Small Animals › Veterinary Oncology Research
Keywords: mastocytoma, chymase, MMP-9, serine protease, mast cell degranulation, tumor invasion, connective tissue remodeling, tryptase
MeSH terms: Amino Acid Sequence, Animals, Dogs, Enzyme Activation, Enzyme Inhibitors, Humans, Mast Cells, Molecular Sequence Data, Molecular Weight, Rabbits, Mast-Cell Sarcoma, Serine Endopeptidases, Tumor Cells, Cultured, Sequence Homology, Amino Acid, Gelatinases, Mice, Chymases

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Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase.

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