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Identification of potential activators of proteinase‐activated receptor‐2 1
Author(s) -
Fox Mark T.,
Harriott Patrick,
Walker Brian,
Stone Stuart R.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01298-2
Subject(s) - trypsin , chemistry , acrosin , biochemistry , tryptase , serine , proteinase k , enzyme , receptor , microbiology and biotechnology , peptide , biology , mast cell , sperm , botany , immunology , acrosome
In order to identify physiological activators of proteinase‐activated receptor‐2 (PAR‐2), a peptide chloromethane inhibitor (biotinyl‐Ser‐Lys‐Gly‐Arg‐CH 2 Cl) 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 ( k i / K i ) for the formation of the covalent proteinase‐inhibitor complex varied by 2×10 5 ‐fold between the proteinases. Biotinyl‐Ser‐Lys‐Gly‐Arg‐CH 2 Cl reacted very rapidly with trypsin, acrosin from sperm and tryptase from mast cells: the k i / K i values with these proteinases were greater than 10 5 M −1 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.