Pardo A, Ramirez R, Gutierrez-Kobeh L, Mendoza F, Bauer E, Selman M
Facultad de Ciencias, Universidad Nacional Autonoma de Mexico, D.F.
Connect Tissue Res. 1991;26(4):259-69. doi: 10.3109/03008209109152443.
Activation of procollagenase constitutes a crucial event in collagenolytic activity regulation. In this study we have purified by DEAE-cellulose, Ultrogel AcA-44, and zinc chelate sepharose chromatographies, a procollagenase-activator from the culture medium of the guinea pig carrageenin granuloma model. On SDS-PAGE, the activator migrates as a principal band of Mr approximately 44,000. The molecule activates procollagenase from human lung fibroblasts in a concentration dependent manner and an enhancement of collagenase activity of trypsin-treated crude culture medium was observed. A loss of about 50% of its activity occurs after heating. In addition, this activator degrades gelatin and casein. All these data suggest that this procollagenase-activator might be stromelysin. The activator was found in both phases of the granuloma, at 7 days when collagen is actively deposited and an important proportion of the collagenolytic activity remains in latent form; and at 14 days, when this enzymatic activity is fully expressed.
前胶原酶的激活是胶原分解活性调节中的一个关键事件。在本研究中，我们通过DEAE - 纤维素、Ultrogel AcA - 44和锌螯合琼脂糖层析，从豚鼠角叉菜胶肉芽肿模型的培养基中纯化了一种前胶原酶激活剂。在SDS - PAGE上，该激活剂迁移为一条主要条带，Mr约为44,000。该分子以浓度依赖的方式激活人肺成纤维细胞中的前胶原酶，并观察到胰蛋白酶处理的粗培养基中胶原酶活性增强。加热后其活性丧失约50%。此外，这种激活剂可降解明胶和酪蛋白。所有这些数据表明，这种前胶原酶激活剂可能是基质溶素。在肉芽肿的两个阶段均发现了该激活剂，一个阶段是在第7天，此时胶原正在积极沉积，且很大一部分胶原分解活性仍处于潜伏形式；另一个阶段是在第14天，此时这种酶活性已完全表达。
