Kinetic analysis of the cleavage of human protease-activated receptor-1 / 2 / 3 and 4 using quenched-fluorescent peptide substrates

Protease-activated receptors [PARs] are a family of G-protein-coupled seven-transmembrane domain receptors that are activated by proteolytic cleavage of their amino-terminal exodomain. To characterize the cleavage rate of human PAR-1 / 2 / 3 and 4 by trypsin and thrombin, four synthetic quenched-flu...

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Bibliographic Details
Published inProtein and peptide letters Vol. 9; no. 5; p. 387
Main Authors Fox, Mark T, Greer, Brett, Lawson, Jill, Healy, Adrienne, Harriott, Patrick
Format Journal Article
LanguageEnglish
Published Netherlands 01.10.2002
Subjects
Kinetics
Protein Processing, Post-Translational
Receptor, PAR-1
Receptor, PAR-2
Receptors, Thrombin - metabolism
Spectrometry, Fluorescence
Thrombin - metabolism
Trypsin - metabolism
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Summary:Protease-activated receptors [PARs] are a family of G-protein-coupled seven-transmembrane domain receptors that are activated by proteolytic cleavage of their amino-terminal exodomain. To characterize the cleavage rate of human PAR-1 / 2 / 3 and 4 by trypsin and thrombin, four synthetic quenched-fluorescent peptide substrates have been synthesized. Each substrate consisted of a ten-residue peptide spanning the receptor activation cleavage site and using progress-curve kinetics, k(cat) / K(m) values were determined.
ISSN:0929-8665
DOI:10.2174/0929866023408490