STROMELYSIN IS AN ACTIVATOR OF PROCOLLAGENASE - A STUDY WITH NATURAL AND RECOMBINANT ENZYMES
STROMELYSIN IS AN ACTIVATOR OF PROCOLLAGENASE - A STUDY WITH NATURAL AND RECOMBINANT ENZYMES
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DOI：
10.1042/bj2480265
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发表时间：
1987-11-15
影响因子：
4.1
通讯作者：
DOCHERTY, AJP
中科院分区：
文献类型：
--
作者：
MURPHY, G;COCKETT, MI;DOCHERTY, AJP
从人牙龈成纤维细胞中纯化潜在形式的基质溶解素和胶原酶。这些潜在的酶原经历了一系列的小减少，在激活后，与4-aminophenylmercuric醋酸或胰蛋白酶处理的先生。在重组前基质溶解素或前胶原酶的相同治疗后，观察到类似的移位和活化动力学。前基质溶解素表现出激活和Mr下降之间的滞后，这表明初始激活的构象变化。胶原酶的活性增强了12倍，无论是天然或重组基质溶解素在胰蛋白酶或4-氨基苯汞乙酸的存在下。基质分解素引起前胶原酶的Mr进一步明显降低。由于这些重要的结缔组织降解酶通常由细胞协同产生，因此提出了一种级联机制，其中胶原酶被基质溶解素激活。
The latent forms of stromelysin and collagenase from human gingival fibroblasts were purified to homogeneity. These latent proenzymes underwent serial small reductions in Mr upon activation by treatment with either 4-aminophenylmercuric acetate or trypsin. Similar shifts in Mr and activation kinetics were observed upon identical treatments of either recombinant prostromelysin or procollagenase. Prostromelysin showed a lag between activation and Mr fall, suggesting an initial activation by conformational change. Collagenase activity was enhanced up to 12-fold by either natural or recombinant stromelysin in the presence of trypsin or 4-aminophenylmercuric acetate. Stromelysin caused a further apparent decrease in the Mr of procollagenase. Since these important connective-tissue-degrading enzymes are usually co-ordinately produced by cells, a cascade mechanism is proposed in which collagenase is activated by stromelysin.