期刊
BIOLOGICAL CHEMISTRY
卷 383, 期 7-8, 页码 1305-1308出版社
WALTER DE GRUYTER & CO
DOI: 10.1515/BC.2002.147
关键词
cathepsin L; cysteine proteinase; lysosome; proteinase inhibitor
Studies using inhibitors that reportedly discriminate between cathepsin B and related lysosomal cysteine proteinases have implicated the enzyme in a wide range of physiological and pathological processes. The most popular substance to selectively inhibit cathepsin B in vivo is CA-074Me, the methyl ester of the E-64 derivative CA-074. However, we now have found that CA-074Me inactivates both cathepsin B and cathepsin L within murine fibroblasts. In contrast, exposure of these cells to the parental compound CA 074 leads to the selective inhibition of endogenous cathepsin B, while intracellular cathepsin L remains unaffected. These results indicate that CA-074 rather than CA-074Me should be used to specifically inactivate cathepsin B within living cells.
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