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首页> 外文期刊>Biological chemistry >Mast cell-dependent activation of pro matrix metalloprotease 2: a role for serglycin proteoglycan-dependent mast cell proteases
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Mast cell-dependent activation of pro matrix metalloprotease 2: a role for serglycin proteoglycan-dependent mast cell proteases

机译：肥大细胞依赖的基质金属蛋白酶的激活2：丝氨酸蛋白依赖蛋白聚糖的肥大细胞蛋白酶的作用

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摘要

The formation of active matrix metalloprotease-2 (MMP-2) requires the proteolytic processing of proMMP-2, a process that can occur through the formation of a ternary complex between proMMP-2, the tissue inhibitor of metalloprotease-2 and membrane type 1-MMP. However, other activation mechanisms have been suggested, and in this study we investigated whether mast cells (MCs) may play a role in the activation of proMMP-2. Murine peritoneal cells, a mixture of macrophages, lymphocytes and MCs, were cultured ex vivo. Addition of proMMP-2 to resting peritoneal cell cultures resulted in only slow conversion of proMMP-2 into the active enzyme. However, when MC degranulation was provoked using a calcium ionophore, proMMP-2 processing was markedly enhanced. When the peritoneal cell populations were depleted in MCs, proMMP-2 processing was abrogated, but was reconstituted when purified MCs were added to the depleted cultures. ProMMP-2 processing was sensitive to serine protease inhibitors, but not to inhibitors of other classes of proteases. Furthermore, proMMP-2 processing was completely abrogated in cells lacking serglycin, a proteoglycan that has previously been shown to mediate storage of a variety of MC serine proteases. Taken together, these results suggest a novel mode of proMMP-2 activation mediated by serglycin-dependent MC serine proteases.
机译：活性基质金属蛋白酶2（MMP-2）的形成需要proMMP-2的蛋白水解过程，该过程可以通过在proMMP-2，金属蛋白酶2的组织抑制剂和1型膜之间形成三元复合物而发生。 -MMP。但是，还提出了其他激活机制，在这项研究中，我们研究了肥大细胞（MC）是否可能在proMMP-2的激活中起作用。离体培养鼠腹膜细胞，巨噬细胞，淋巴细胞和MC的混合物。将proMMP-2添加到静止的腹膜细胞培养物中只会导致proMMP-2缓慢转化为活性酶。但是，当使用钙离子载体引起MC脱粒时，proMMP-2的加工显着增强。当腹膜细胞群中的MCs耗尽时，proMMP-2处理被取消，但是当将纯化的MCs添加到枯竭的培养物中时，proMMP-2的处理被重建。 ProMMP-2加工对丝氨酸蛋白酶抑制剂敏感，但对其他类别蛋白酶的抑制剂不敏感。此外，proMMP-2加工在缺乏血清甘油糖的细胞中被完全废除，该蛋白质以前被证明可以介导多种MC丝氨酸蛋白酶的存储。两者合计，这些结果表明proMMP-2激活的新型模式，由丝氨酸蛋白依赖性MC丝氨酸蛋白酶介导。

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