Inhibition of cathepsin L-like proteases by cathepsin V propeptide.
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.
Burden
Roberta E
RE
School of Pharmacy, Queen's University Belfast, Belfast, UK.
Snoddy
Philip
P
Jefferies
Caroline A
CA
Walker
Brian
B
Scott
Christopher J
CJ
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*
D010446:Peptide Fragments; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; C117627:CTSV protein, human