Human mast cell β-tryptase is a gelatinase
Human mast cell β-tryptase is a gelatinase
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DOI：
10.4049/jimmunol.171.3.1493
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发表时间：
2003-08-01
影响因子：
4.4
通讯作者：
Pejler, G
中科院分区：
文献类型：
--
作者：
Fajardo, I;Pejler, G
细胞外基质的重塑是多种炎症疾病以及伤口愈合和血管生成等正常生理过程的重要组成部分。先前的研究已经确定了各种基质金属蛋白酶，例如明胶酶A和B，是在这种条件下细胞外基质降解的关键参与者。在这里，我们发现了一种额外的酶，人类肥大细胞β -胰蛋白酶，具有有效的明胶降解特性，表明这种蛋白酶对基质降解的潜在贡献。人β -胰蛋白酶在溶液和明胶酶谱分析中都能降解明胶。此外，β -胰蛋白酶被证明可以降解部分变性的1型胶原蛋白。β -胰蛋白酶与明胶结合强烈，形成高分子量复合物，在SDS-PAGE期间稳定。肥大细胞在其分泌颗粒中储存大量预先形成的活性胰蛋白酶。考虑到肥大细胞在结缔组织中的位置，以及最近认识到肥大细胞在结缔组织降解为关键事件的疾病（如类风湿关节炎）中的作用，因此胰蛋白酶可能有助于体内细胞外基质降解过程。
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 vivo.