title: Inhibition of cathepsin L-like proteases by cathepsin V propeptide.
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.
authors.affiliation: School of Pharmacy, Queen's University Belfast, Belfast, UK.
authors.forename: Roberta E
authors.initials: RE
authors.lastname: Burden
authors.forename: Philip
authors.initials: P
authors.lastname: Snoddy
authors.forename: Caroline A
authors.initials: CA
authors.lastname: Jefferies
authors.forename: Brian
authors.initials: B
authors.lastname: Walker
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Scott
mesh_terms: D002401:Cathepsin B / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D002403:Cathepsins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology*; D045744:Cell Line, Tumor; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology*; D015870:Gene Expression; D006801:Humans; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology*
chemical_list: D010446:Peptide Fragments; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; C117627:CTSV protein, human