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- W1981488062 abstract "The catabolism of two gastric neuropeptides, the C-terminal decapeptide of gastrin releasing peptide-27 (GRP10) and substance P (SP), by membrane-bound peptidases of the porcine gastric corpus and by porcine endopeptidase-24.11 (“enkephalinase”) has been investigated. GRP10 was catabolized by gastric muscle peptidases (specific activity 1.8 nmol min−1 mg−1 protein) by hydrolysis of the His8-Leu9 bond and catabolism was inhibited by phosphoramidon (I50 approx. 10−8 M), a specific inhibitor of endopeptidase-24.11. The same bond in GRP10 was cleaved by purified endopeptidase-24.11, and hydrolysis was equally sensitive to inhibition by phosphoramidon. SP was catabolized by gastric muscle peptidases (specific activity 1.7 nmol min−1 mg−1 protein) by hydrolysis of the Gln6-Phe7, Phe7-Phe8 and Gly9-Leu10 bonds, which is identical to the cleavage of SP by purified endopeptidase-24.11. The C-terminal cleavage of GRP10 and SP would inactivate the peptides. It is concluded that a membrane-bound peptidase in the stomach wall catabolizes and inactivates GRP10 and SP and that, in its specificity and sensitivity to phosphoramidon, this peptidase resembles endopeptidase-24.11." @default.
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- W1981488062 date "1985-03-01" @default.
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- W1981488062 title "Catabolism of gastrin releasing peptide and substance P by gastric membrane-bound peptidases" @default.
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- W1981488062 doi "https://doi.org/10.1016/0196-9781(85)90052-x" @default.
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