Identification of potential activators of proteinase-activated receptor-2.

Abstract:

:In order to identify physiological activators of proteinase-activated receptor-2 (PAR-2), a peptide chloromethane inhibitor (biotinyl-Ser-Lys-Gly-Arg-CH2Cl) based on the cleavage site for activation of PAR-2 was synthesised and tested with 12 trypsin-like serine proteinases. The second-order rate constant (ki/Ki) for the formation of the covalent proteinase-inhibitor complex varied by 2 x 10(5)-fold between the proteinases. Biotinyl-Ser-Lys-Gly-Arg-CH2Cl reacted very rapidly with trypsin, acrosin from sperm and tryptase from mast cells: the ki/Ki values with these proteinases were greater than 10(5) M(-1) x s(-1). Thus, the specificity of these proteinases matched the sequence of the activation site of PAR-2 and it can be concluded that these proteinases are potential physiological activators of PAR-2.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fox MT,Harriott P,Walker B,Stone SR

doi

10.1016/s0014-5793(97)01298-2

subject

Has Abstract

pub_date

1997-11-17 00:00:00

pages

267-9

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)01298-2

journal_volume

417

pub_type

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