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[纤连蛋白的蛋白水解潜能与细胞外基质的降解]

[Proteolytic potential of fibronectin and degradation of extracellular matrix].

作者信息

Keil-Dlouha V, Planchenault T, Imhoff J M, Emod I, Blondeau X, Lambert-Vidmar S

机构信息

Laboratoire de Chimie des Protéines, Institut Pasteur, Paris, France.

出版信息

Pathol Biol (Paris). 1990 Dec;38(10):993-8.

PMID:2290700
Abstract

Fibronectin is one of the major adhesive glycoproteins and bears interaction sites for both cell receptors and the extracellular matrix. Disappearance of fibronectin is the first step of cellular transformation in carcinogenesis. This phenomenon has been ascribed to increased proteolysis of fibronectin or of its cellular receptor. Results obtained during previous studies by the authors have shown that the fibronectin molecule has latent proteolytic activities which become apparent only after the action of other external proteases. Two proteinases, FN-gelatinase and FN-laminase, were identified in cathepsin D fibronectin digest. The acute activity of these two proteases is responsible for degradation of the extracellular matrix. Furthermore, the sequences and functions of both enzymes share a number of features with retroviral proteases.

摘要

纤连蛋白是主要的黏附糖蛋白之一,具有细胞受体和细胞外基质的相互作用位点。纤连蛋白的消失是致癌过程中细胞转化的第一步。这种现象被归因于纤连蛋白或其细胞受体的蛋白水解增加。作者先前研究获得的结果表明,纤连蛋白分子具有潜在的蛋白水解活性,只有在其他外部蛋白酶作用后才会显现出来。在组织蛋白酶D纤连蛋白消化物中鉴定出两种蛋白酶,即纤连蛋白-明胶酶和纤连蛋白-层粘连蛋白酶。这两种蛋白酶的急性活性负责细胞外基质的降解。此外,这两种酶的序列和功能与逆转录病毒蛋白酶有许多共同特征。

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