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Gewählte Publikation:

Montaser, M; Lalmanach, G; Mach, L.
(2002): CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells.
Biol Chem. 2002; 383(7-8):1305-1308 FullText FullText_BOKU

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.
Autor*innen der BOKU Wien:
Mach Lukas
Find related publications in this database (using NML MeSH Indexing)
Animals -
Cathepsin B - antagonists & inhibitors
Cathepsins - antagonists & inhibitors
Cysteine Endopeptidases - antagonists & inhibitors
Dipeptides - pharmacology
Fibroblasts - enzymology
Mice - enzymology
Protease Inhibitors - pharmacology

Find related publications in this database (Keywords)
cathepsin L
cysteine proteinase
proteinase inhibitor

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