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

Mark Fox, Brett Greer, Jill Lawson, Adrienne Healy, Patrick Harriott

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)387-393
Number of pages7
JournalProtein and Peptide Letters
Volume9
Issue number5
Publication statusPublished - 2002

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Proteinase-Activated Receptors
PAR-2 Receptor
PAR-1 Receptor
Peptide Receptors
Thrombin
Trypsin
Peptides
Kinetics
Substrates
GTP-Binding Proteins
Chemical activation
seven-transmembrane G-protein-coupled receptor

Cite this

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abstract = "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.",
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Kinetic analysis of the cleavage of human protease-activated receptor-1/2/3 and 4 using quenched-fluorescent peptide substrates. / Fox, Mark; Greer, Brett; Lawson, Jill; Healy, Adrienne; Harriott, Patrick.

In: Protein and Peptide Letters, Vol. 9, No. 5, 2002, p. 387-393.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Kinetic analysis of the cleavage of human protease-activated receptor-1/2/3 and 4 using quenched-fluorescent peptide substrates

AU - Fox, Mark

AU - Greer, Brett

AU - Lawson, Jill

AU - Healy, Adrienne

AU - Harriott, Patrick

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

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M3 - Article

VL - 9

SP - 387

EP - 393

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

SN - 0929-8665

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ER -