The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase.
Open accessAbstract
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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“Moreover, MC tryptases and chymases have been shown to activate the precursors of MMP2 [12], MMP9 [13], collagenase and stromelysin [14].”
From Estradiol and Progesterone Regulate the Migration of Mast Cells from the Periphery to the Uterus and Induce Their Maturation and Degranulation (2010) · cites this paper as [13]
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Cites
A matrix metalloproteinase expressed on the surface of invasive tumour cells
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Metalloproteinases and their inhibitors in matrix remodeling
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Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
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Tissue Inhibitor of Metalloproteinase (TIMP-2)
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Furin-dependent intracellular activation of the human stromelysin-3 zymogen
Pei, D., & Weiss, S. J. (1995) · Nature · doi:10.1038/375244a0 · Cited by 629
Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase.
Hibbs, M. S., Hasty, K. A., Seyer, J. M., Kang, A. H., & Mainardi, C. L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89580-1 · Cited by 613
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Mast cell secretory granules: armed for battle
Wernersson, S., & Pejler, G. (2014) · Nature reviews. Immunology · doi:10.1038/nri3690 · Cited by 968
Inflammatory mast cells up-regulate angiogenesis during squamous epithelial carcinogenesis
Coussens, L. M., Raymond, W. W., Bergers, G., Laig-Webster, M., Behrendtsen, O., Werb, Z., Caughey, G. H., & Hanahan, D. (1999) · Genes & Development · doi:10.1101/gad.13.11.1382 · Cited by 946
Self-citationBiochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9)
den Steen, P. E. V., Dubois, B., Nelissen, I., Rudd, P., Dwek, R., & Opdenakker, G. (2002) · Critical reviews in biochemistry and molecular biology · doi:10.1080/10409230290771546 · Cited by 948
da Silva, E. Z. M., Jamur, M. C., & Oliver, C. (2014) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155414545334 · Cited by 645
Mast cell tryptases and chymases in inflammation and host defense.
Caughey, G. H. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00509.x · Cited by 442
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Metadata
- Authors
- Fang, K. C., Raymond, W. W., Lazarus, S. C., & Caughey, G. H.
- Affiliations
- University of California, San Francisco (US)
- Venue
- Journal of Clinical Investigation
- Published
- 1996-04-01
- Volume
- 97
- Issue
- 7
- Pages
- 1589-1596
- ISSN
- 0021-9738 (ISSN-L)
- 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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