Abstract
The N-terminal propeptide domains of several cathepsin L-like cysteine proteases have been shown to possess potent inhibitory activity. Here we report the first kinetic characterisation of the inhibition properties of the cathepsin V propeptide (CatV PP). Using a facile recombinant approach we demonstrate expression, purification and evaluation of the CatV PP. This propeptide was found to behave as a tight-binding inhibitor against CatV (K (i) 10.2 nm). It also functions as an inhibitor against other members of the CatL-like subclass (CatL, 9.8 nm; CatS, 10.7 nm; and CatK, 149 nm) and had no discernible effects upon the more distantly related CatB.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Cathepsin B / antagonists & inhibitors*
-
Cathepsin B / metabolism*
-
Cathepsins / genetics
-
Cathepsins / isolation & purification
-
Cathepsins / metabolism*
-
Cathepsins / pharmacology*
-
Cell Line, Tumor
-
Cysteine Endopeptidases / genetics
-
Cysteine Endopeptidases / isolation & purification
-
Cysteine Endopeptidases / metabolism*
-
Cysteine Endopeptidases / pharmacology*
-
Gene Expression
-
Humans
-
Peptide Fragments / genetics
-
Peptide Fragments / isolation & purification
-
Peptide Fragments / metabolism*
-
Peptide Fragments / pharmacology*
Substances
-
Peptide Fragments
-
Cathepsins
-
Cysteine Endopeptidases
-
Cathepsin B
-
CTSV protein, human