ArticleThe Biochemical journal1995
Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Dermal Pathology in Melasma: An Update Review.Clinical, cosmetic and investigational dermatology · 2022Review
- Mouse mast cell protease 4 suppresses scar formation after traumatic spinal cord injury.Scientific reports · 2019Article
- The emerging prominence of the cardiac mast cell as a potent mediator of adverse myocardial remodeling.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Article
- Influence of mast cells in drug-induced gingival overgrowth.Mediators of inflammation · 2013Article
- Cardiac mast cells: the centrepiece in adverse myocardial remodelling.Cardiovascular research · 2011Review
- Systemic mastocytosis with skeletal involvement: a case report and review of the literature.Clinical cases in mineral and bone metabolism : the official journal of the Italian Society of Osteoporosis, Mineral Metabolism, and Skeletal Diseases · 2009Article
- Up-regulation of matrix metalloproteinase-3 in the dorsal root ganglion of rats with paclitaxel-induced neuropathy.Cancer science · 2008Article
- Mast cells in rheumatoid arthritis.Clinical rheumatology · 2007Review
- Chymase-positive mast cells in small sized adenocarcinoma of the lung.Virchows Archiv : an international journal of pathology · 2003Article
- Tissue-specific expression of mast cell granule serine proteinases and their role in inflammation in the lung and gut.Immunology · 2002Review
- Rat mast cell protease-I enhances immunoglobulin E production by mouse B cells stimulated with interleukin-4.Immunology · 2001Article
- Conditional and targeted overexpression of vascular chymase causes hypertension in transgenic mice.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Effects of induced mast cell activation on prostaglandin E and metalloproteinase production by rheumatoid synovial tissue in vitro.Annals of the rheumatic diseases · 1998Article
- Cloning of the cDNAs for mast-cell chymases from the jejunum of Mongolian gerbils, Meriones unguiculatus, and their sequence similarities with chymases expressed in the connective-tissue mast cells of mice and rats.The Biochemical journal · 1996Article
- Release of the mucosal mast cell granule chymase, rat mast cell protease-II, during anaphylaxis is associated with the rapid development of paracellular permeability to macromolecules in rat jejunum.The Journal of experimental medicine · 1995Article
- Mast cells, cytokines, and metalloproteinases at the rheumatoid lesion: dual immunolocalisation studies.Annals of the rheumatic diseases · 1995Article
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5 authors.
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Abstract
Histological studies have previously demonstrated an association between mast-cell activation/degranulation and areas of connective-tissue lysis in vivo; in addition, mast-cell extracts have been shown to activate latent forms of collagenase and stromelysin. In the present study we have examined the potential roles of rat mast-cell proteinase (RMCP) I and RMCP II as activators of the precursors of matrix metalloproteinase (MMP)-1 (interstitial collagenase), MMP-2 (gelatinase A) and MMP-3 (stromelysin 1). Both RMCPs I and II activated proMMP-3 by converting the 57 kDa precursor into a 45 kDa polypeptide. The N-terminal amino acid of 45 kDa MMP-3 activated by RMCP II was identified as Phe83. By contrast, only RMCP II activated the 52 kDa proMMP-1 by converting it into a 41 kDa protein and generating the new N-termini, namely Gln80 and Val82. The collagenolytic activity which resulted from this cleavage was only 35% of the full activity, but this could not be augmented by subsequent treatment with MMP-3, the latter being a crucial enzyme for the generation of the fully active MMP-1 with Phe81 at the N-terminus, in conjunction with other serine proteinases. Thus RMCP II activates proMMP-1 via a mechanism different from that reported for the stepwise processing by combinations of other trypsin-like enzymes and MMP-3. ProMMP-2 (pro-gelatinase A) was not activated by either RMCP I or RMCP II, despite processing to smaller products.
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