Literature summary for 3.4.17.12 extracted from

Zhang, X.; Tan, F.; Skidgel, R.A.
Carboxypeptidase M is a positive allosteric modulator of the kinin B1 receptor (2013), J. Biol. Chem., 288, 33226-33240.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14384	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HEK-293 cell	-	Homo sapiens	-

General Information

General Information	Comment	Organism
physiological function	in HEK-293 cells stably transfected with kinin B1 receptor, co-expression of carboxypeptidase M enhances des-Arg10-kallidin-stimulated increases in intracellular Ca2+ or phosphoinositide turnover. Carboxypeptidase M increases kinin B1 receptor affinity for des-Arg10-kallidin by 5-fold but has no effect on basal kinin B1 receptor-dependent phosphoinositide turnover. Soluble, recombinant carboxypeptidase M binds to HEK cells expressing kinin B1 receptor without stimulating receptor signaling. Carboxypeptidase M positive allosteric action is independent of enzyme activity but depended on interaction of its C-terminal domain with the kinin B1 receptor extracellular loop 2. Disruption of the carboxypeptidase M/kinin B1 receptor interaction or knockdown of carboxypeptidase M in cytokine-treated primary human endothelial cells inhibits the allosteric enhancement of carboxypeptidase M on kinin B1 receptor des-Arg10-kallidin binding or ERK1/2 activation. Carboxypeptidase M also enhances the des-Arg10-kallidin-induced kinin B1 receptor conformational changes	Homo sapiens

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Release 2023.1 (January 2023)