Abstract

The spectrum of proteinases and the dynamics of proteinase activity in the ambulacrum structures were studied by quantitative gel zymography in the holothurians Eupentacta fraudatrix and Cucumaria japonica under normal conditions and after transverse cutting of the ambulacrum. Proteinases with gelatinolytic activity were detected only in E. fraudatrix; the species had two pools of proteinases. The high-molecular-weight pool was represented by only one (132 kDa) or two (132 and more than 250 kDa) proteins; the low-molecular-weight pool included two proteins with molecular weights of 53 and 47 kDa. In their ability to lyse gelatin, but not casein, and in their sensitivity to inhibitors of different classes of enzymes, gelatinases of E. fraudatrix are similar to vertebrate matrix metalloproteinases. It was shown that the activity of proteinases increased after injury to the animal and that GM6001, a selective inhibitor of metalloproteinases, blocks the proteinase activity. It was suggested that proteinases with gelatinolytic activity are a key factor of regeneration in holothurians.

中文翻译：

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具有明胶酶活性的蛋白酶及其在Holothurians Eupentacta欺诈家（D'yakonov and Baranova，1958）和Cucumaria japonica（Semper，1868）中的球囊再生中的作用（Echinodermata：Holothuroidea）

摘要

通过定量凝胶酶谱分析法，在正常条件下和横切后，对湖豚草中的真叶假单胞菌和黄瓜进行了定量的酶谱分析，研究了球菌结构中的蛋白酶谱和蛋白酶活性的动态。具有明胶分解活性的蛋白酶仅在大肠杆菌中检出; 该物种有两个蛋白酶池。高分子量库仅由一种（132 kDa）或两种（132和250 kDa以上）蛋白代表；低分子量库包含两种分子量分别为53和47 kDa的蛋白质。大肠杆菌的明胶酶裂解明胶而不是酪蛋白的能力以及对不同酶抑制剂的敏感性与脊椎动物基质金属蛋白酶相似。结果表明，对动物的伤害后，蛋白酶的活性增加了，金属蛋白酶的选择性抑制剂GM6001阻止了蛋白酶的活性。有人提出具有明胶分解活性的蛋白酶是全人类再生的关键因素。