Open AccessSodium Salicylate Activates Cathepsin B But Not Cathepsin H from Rat Spleen
Author(s) -
Kazuo Yamamoto,
Mitsue Takeda,
Yuzo Kato
Publication year - 1985
Publication title -
japanese journal of pharmacology/japanese journal of pharmacology
Language(s) - English
Resource type - Journals
eISSN - 1347-3506
pISSN - 0021-5198
DOI - 10.1254/jjp.38.215
Subject(s) - leupeptin , cathepsin b , chemistry , cathepsin o , cathepsin h , cathepsin , cysteine , cathepsin c , cathepsin s , sodium salicylate , microbiology and biotechnology , biochemistry , cathepsin l , cathepsin l1 , enzyme , biology , organic chemistry , protease
Effect of sodium salicylate (SA) and its analogues on lysosomal cysteine proteinases, cathepsins B and H, was investigated. Using a sensitive fluorometric assay, SA was shown to activate cathepsin B but not cathepsin H in the presence of cysteine. Kinetics data showed that the SA-stimulated reaction was due to a 4.5-fold decrease in Km. SA caused a decrease in the inactivation rate of cathepsin B by leupeptin and E-64. It was suggested that SA stimulates the activation process of the essential cysteine residue.