软骨基质转换中基质溶解素/转蛋白的基本结构和功能。

S M Wilhelm, D Wunderlich, C A Maniglia, A Z Eisen, G I Goldberg
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引用次数: 0

摘要

Stromelysin/Transin是基质金属蛋白酶基因家族的成员。该金属蛋白酶作为预前酶合成,预测大小为53,977 Da,包含17个氨基酸的信号肽。促泌素由正常细胞和转化细胞分泌,在60和58 kda的NaDodSO4凝胶上有两种明显的分子质量。较小的60 kda物种含有n -连接的低聚糖。Stromelysin由三个结构域组成,氨基末端前肽(s)结构域包含三碱基氨基酸序列RRK,这在胰蛋白酶样丝氨酸蛋白酶对该酶原的蛋白水解激活中起重要作用。第二结构域由含有锌结合位点的催化结构域组成。羧基末端血凝素结构域没有已知的功能,可以在不损失酶活性的情况下去除。基质溶酶具有广泛的底物特异性,包括蛋白聚糖、酪蛋白、纤维连接蛋白、层粘连蛋白、天然IV型和IX型胶原和明胶,但不包括I型胶原。在胰蛋白酶或纤溶酶存在的情况下,这种酶的催化量也可以充分激活间质成纤维细胞胶原酶。我们已经开发了一组抗基质溶酶的单克隆抗体,这将有助于组织中各种酶的组织定位。此外,我们已经证明,人il -1 (α)或rTNF (α)可以刺激该酶在培养的牛关节软骨中的表达至少10倍。基于western blot分析,在细胞因子处理培养的培养基或软骨基质室中,酶原形式是检测到的主要酶种。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Primary structure and function of stromelysin/transin in cartilage matrix turnover.

Stromelysin/Transin is a member of the matrix metalloprotease gene family. This metalloprotease is synthesized as a preproenzyme with a predicted size of 53,977 Da including a 17 amino acid signal peptide. Prostromelysin is secreted from normal and transformed cells in two forms with apparent molecular masses on NaDodSO4 gels of 60 and 58-kDa. The minor 60-kDa species contains N-linked oligosaccharide(s). Stromelysin consists of three domains the amino terminal propeptide(s) domain contains the tribasic amino acid sequence RRK which is important in the proteolytic activation of this zymogen by trypsin-like serine proteases. The second domain consists of the catalytic domain which contains the zinc binding site. The carboxyl-terminal hemopexin domain has no known function and can be removed without a loss of enzymatic activity. Stromelysin has a broad range of substrate specificity including proteoglycans, casein, fibronectin, laminin, native type IV and IX collagen and gelatin but not type I collagen. In the presence of trypsin or plasmin, catalytic amounts of this enzyme can also fully activate interstitial fibroblast collagenase. We have developed a panel of monoclonal antibodies against stromelysin which will be useful for the tissue localization of the various species of this enzyme in tissues. In addition, we have demonstrated that either human rIL-1 (alpha) or rTNF (alpha) can stimulate the expression of this enzyme in cultured bovine articular cartilage at least 10-fold. Based on western blot analysis, the zymogen form of the enzyme was the major enzyme species detected in either the media or cartilage matrix compartments of cytokine treated cultures.

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