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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Cholecystokinin-B receptor ligands of the dipeptoid series act as agonists on rat stomach histidine decarboxylase.

BACKGROUND & AIMS: The effect of gastrin on the enterochromaffin-like cells in the rat stomach is mediated by cholecystokinin (CCK)-B receptors and manifested as activation of histidine decarboxylase ( HDC). The dipeptoids PD 136450, PD 135158, and PD 134308 are thought to be selective CCK-B receptor antagonists. The effects of the dipeptoids and of gastrin-17 and sulfated CCK-8 on rat stomach HDC activity were examined. METHODS: Drugs were infused intravenously or subcutaneously to fasted rats, and the HDC activity was determined. RESULTS: The dipeptoids activated HDC with maximal responses (50%-60% of the maximal response to gastrin) at 1 mumol.kg-1.h-1. Rat gastrin-17 activated HDC maximally at 3 nmol.kg-1.h-1, and sulfated CCK-8 produced maximal response at 20 nmol.kg-1.h-1. The CCK-B receptor antagonist L-365,260 inhibited the HDC activation induced by gastrin, sulfated CCK-8, or the dipeptoids. The dipeptoids did not inhibit the gastrin- induced HDC activation. CONCLUSIONS: Gastrin, sulfated CCK-8, and the dipeptoids activated rat stomach HDC. L-365,260 but not devazepide inhibited the HDC activation. Thus, the dipeptoids, which failed to inhibit the gastrin- induced HDC activation, act as CCK-B receptor agonists and not as antagonists. It is important to recognize this to ensure appropriate interpretation of data obtained with these drugs.[1]

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