Brain cathepsin B cleaves a caspase substrate

We show that an enzyme exists in rat brain capable of cleaving the caspase-3 specific peptide substrate Ac-DEVD-AMC at low pH. The enzyme shows properties of a cysteine protease and is localized, predominantly, in lysosomes. We have purified this enzyme from rat brain and identified it by MALDI-TOF...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2008-03, Vol.73 (3), p.332-336
Main Authors: Yakovlev, A. A., Gorokhovatsky, A. Yu, Onufriev, M. V., Beletsky, I. P., Gulyaeva, N. V.
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Brain - enzymology
Caspase 3 - metabolism
Cathepsin B - isolation & purification
Cathepsin B - metabolism
Coumarins - metabolism
Cysteine Proteinase Inhibitors - metabolism
Cysteine Proteinase Inhibitors - pharmacology
Hydrogen-Ion Concentration
Life Sciences
Microbiology
Oligopeptides - metabolism
Rats
Sulfhydryl Reagents - pharmacology
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Summary:We show that an enzyme exists in rat brain capable of cleaving the caspase-3 specific peptide substrate Ac-DEVD-AMC at low pH. The enzyme shows properties of a cysteine protease and is localized, predominantly, in lysosomes. We have purified this enzyme from rat brain and identified it by MALDI-TOF MS. The enzyme possessing “acidic” DEVDase activity in rat brain appears to be cathepsin B. It remains obscure, whether cathepsin B participates in cleavage of caspase-3 substrates in vivo . We suggest that under certain conditions (e.g. in hypoxia) cathepsin B participates in cleavage of caspase-3 substrates in brain cells.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297908030140