Research article - Peer-reviewed, 2003
Human mast cell beta-tryptase is a gelatinase
Fajardo I, Pejler GAbstract
Remodeling of extracellular matrix is an important component in a variety of inflammatory disorders as well as in normal physiological processes such as wound healing and angiogenesis. Previous investigations have identified the various matrix metalloproteases, e.g., gelatinases A and B, as key players in the degradation of extracellular matrix under such conditions. Here we show that an additional enzyme, human mast cell beta-tryptase, has potent gelatin-degrading properties, indicating a potential contribution of this protease to matrix degradation. Human beta-tryptase was shown to degrade gelatin both in solution and during gelatin zymographic analysis. Further, beta-tryptase was shown to degrade partially denatured collagen type 1. beta-Tryptase bound strongly to gelatin, forming high molecular weight complexes that were stable during SDS-PAGE. Mast cells store large amounts of preformed, active tryptase in their secretory granules. Considering the location of mast cells in connective tissues and the recently recognized role of mast cells in disorders in which connective tissue degradation is a key event, e.g., rheumatoid arthritis, it is thus likely that tryptase may contribute to extracellular matrix-degrading processes in vivoPublished in
Journal of Immunology2003, volume: 171, number: 3, pages: 1493-1499
Publisher: AMER ASSOC IMMUNOLOGISTS
Authors' information
Swedish University of Agricultural Sciences, Department of Molecular Biosciences
Fajardo, I
Publication Identifiers
DOI: https://doi.org/10.4049/jimmunol.171.3.1493
URI (permanent link to this page)
https://res.slu.se/id/publ/1091