兔成纤维细胞和粒细胞的蛋白聚糖降解酶
Proteoglycan-degrading enzymes of rabbit fibroblasts and granulocytes.
作者信息
Werb Z, Dingle J T, Reynolds J J, Barrett A J
出版信息
Biochem J. 1978 Sep 1;173(3):949-58. doi: 10.1042/bj1730949.
Abstract
A neutral proteinase secreted by rabbit synovial fibroblasts in parallel with specific collagenase was partially purified by ion-exchange chromatography. At pH 7.6 this proteinase degraded 35S-labelled bovine nasal proteoglycan and azo-casein. The enzymic activity was inhibited by EDTA, 1,10-phenanthroline and serum, whereas di-isopropyl phosphorofluoridate and soya-bean trypsin inhibitor had little effect. By gel filtration the apparent mol.wt. of the enzyme was 25000. The fibroblast neutral proteinase was compared with the proteoglycan-degrading neutral proteinases of rabbit polymorphonuclear-leucocyte granules. Two distinct activities were found in the granules: one was inhibited by soya-bean trypsin inhibitor and the other by EDTA. The proteoglycan-degrading proteinases of rabbit fibroblasts and polymorphonuclear leucocytes at acid pH also were examined. Both cathepsin D and a thiol-dependent proteinase contributed to the degradation of proteoglycan at pH 4.5.
摘要
兔滑膜成纤维细胞分泌的一种与特异性胶原酶同时产生的中性蛋白酶，通过离子交换色谱法进行了部分纯化。在pH 7.6时，这种蛋白酶能降解35S标记的牛鼻蛋白聚糖和偶氮酪蛋白。酶活性受到EDTA、1,10 - 菲咯啉和血清的抑制，而二异丙基氟磷酸酯和大豆胰蛋白酶抑制剂的影响较小。通过凝胶过滤法测得该酶的表观分子量为25000。将成纤维细胞中性蛋白酶与兔多形核白细胞颗粒中降解蛋白聚糖的中性蛋白酶进行了比较。在颗粒中发现了两种不同的活性：一种被大豆胰蛋白酶抑制剂抑制，另一种被EDTA抑制。还研究了兔成纤维细胞和多形核白细胞在酸性pH下的蛋白聚糖降解蛋白酶。组织蛋白酶D和一种硫醇依赖性蛋白酶在pH 4.5时都参与了蛋白聚糖的降解。
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