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Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages
Author(s) -
Hara Kenji,
Kominami Eiki,
Katunuma Nobuhiko
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80737-3
Subject(s) - leupeptin , cathepsin b , cathepsin , cathepsin h , biochemistry , pepstatin , cathepsin o , chemistry , cathepsin a , cathepsin c , cystatin , cathepsin l , cysteine proteinase inhibitors , endopeptidase , serine , cysteine , intracellular , microbiology and biotechnology , enzyme , biology , protease , cystatin c , apoptosis , programmed cell death , renal function , caspase
The effects of various proteinase inhibitors on the processing of lysosomal cathepsins B, H and L were investigated in cultured rat peritoneal macrophages. The processing of newly synthesized pro‐cathepsins B, H and L to the mature single‐chain enzymes was sensitive to a metal chelator,1,10‐phenanthroline, and a synthetic metalloendopeptidase substrate, Z‐Gly‐Leu‐NH 2 , and insensitive to inhibitors of serine proteinases, aspartic proteinases and cysteine proteinases. Inhibitors of cysteine proteinases, E‐64‐d and leupeptin, inhibited the processing of the single‐chain forms of cathepsins B, H and L to the two‐chain forms. These results suggest that (a) metal endopeptidase(s) is (are) involved in the propeptide processing of cathepsin B, H and L, and that proteolytic cleavages of the mature single‐chain cathepsins are accomplished by cysteine proteinases in lysosomes.