CATHEPSIN-B ACTIVITY IN STIMULATED MOUSE PERITONEAL-MACROPHAGES

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  • 1 January 1979
    • journal article
    • research article
    • Vol. 41  (5) , 379-384
Abstract
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 3 other lysosmal 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 h culture of macrophages. 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. Increased enzyme activity was dependent on new protein synthesis.

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