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Mouse T-cell associated serine proteinase 1 degrades collagen type IV: a structural basis for the migration of lymphocytes through vascular basement membranes.

机译:小鼠T细胞相关的丝氨酸蛋白酶1降解IV型胶原蛋白:淋巴细胞通过血管基底膜迁移的结构基础。

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摘要

We show that CD8+ T-lymphocyte lines perferentially attach to collagen type IV and that mouse T-cell specific serine proteinase 1 (MTSP-1) preferentially degrades native basement membrane collagen type IV. In contrast, the interstitial collagen types I, II, III, V and VI appear not to be affected. The data reveal that MTSP-1 predominantly cleaves the alpha 2(IV) chain, which is found in the native triple helical structure of type IV collagen in a ratio of alpha 1(IV): alpha 2(IV) = 2:1 into small peptides. The cleavage of the alpha 2(IV) chain within the native collagen type IV molecules most likely results not only in a destabilization of single molecules but of the entire collagenous basement membrane scaffold at the site of MTSP-1 secretion.
机译:我们表明,CD8 + T淋巴细胞系与四型胶原蛋白完美结合,并且小鼠T细胞特异性丝氨酸蛋白酶1(MTSP-1)优先降解了天然基底膜四型胶原蛋白。相反,间质胶原蛋白I,II,III,V和VI似乎没有受到影响。数据显示,MTSP-1主要切割α2(IV)链,该链以α1(IV):α2(IV)= 2:1的比例存在于IV型胶原的天然三螺旋结构中。小肽。天然IV型胶原分子中的α2(IV)链断裂最可能不仅导致单个分子的不稳定,而且导致MTSP-1分泌部位的整个胶原基底膜支架的不稳定。

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