Mørland B, Pedersen A
Lab Invest. 1979 Nov;41(5):379-84.
The activity of cathepsin B was assayed in murine resident peritoneal macrophages, and after stimulation of the cells in vivo and in vitro. The resident cells showed a very low activity of the enzyme, compared to the activities of three other lysosomal enzymes: cathepsin D, acid phosphatase, and beta-glucuronidase which were tested simultaneously. Endocytosis of carrageenan, latex, or carbon particles in vitro induced a prominent rise in intracellular cathepsin B activity. Addition of endotoxin from Escherichia coli in vivo or in vitro, or cell wall products from streptococci in vitro caused no change in cathepsin B activity. There was a release of enzyme activity to the medium after a 72-hour culture of macrophages. However, the release, calculated as a percentage of total activity, was not influenced by any treatments mentioned. All significant rises in enzyme activity could be inhibited by the addition of cycloheximide, and it was concluded that increased enzyme activity was dependent on new protein synthesis.
在小鼠腹腔常驻巨噬细胞中，以及在体内和体外刺激这些细胞后，对组织蛋白酶B的活性进行了测定。与同时检测的其他三种溶酶体酶（组织蛋白酶D、酸性磷酸酶和β-葡萄糖醛酸酶）的活性相比，常驻细胞显示出该酶的活性非常低。体外吞噬角叉菜胶、乳胶或碳颗粒会导致细胞内组织蛋白酶B的活性显著升高。体内或体外添加来自大肠杆菌的内毒素，或体外添加链球菌的细胞壁产物，均不会引起组织蛋白酶B活性的变化。巨噬细胞培养72小时后，酶活性会释放到培养基中。然而，以总活性的百分比计算，这种释放不受上述任何处理的影响。添加环己酰亚胺可抑制酶活性的所有显著升高，由此得出结论，酶活性的增加依赖于新的蛋白质合成。
