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Mucosal gastrin receptor. IV. Binding specificity.

K Takeuchi, G R Speir, L R Johnson

The American Journal of Physiology

|November 1, 1980

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This study investigated gastrin analogues and their binding to the gastrin receptor. Shorter gastrin peptides and modifications to the C-terminal phenylalanine significantly impacted binding affinity, confirming receptor specificity.

Area of Science:

Gastroenterology
Endocrinology
Molecular Pharmacology

Background:

The gastrin receptor plays a crucial role in regulating gastric acid secretion.
Understanding the binding characteristics of gastrin analogues is essential for elucidating receptor function.

Purpose of the Study:

To investigate the binding specificity of various gastrin analogues to the gastrin receptor.
To correlate binding affinities with known biological potencies of gastrin peptides.

Main Methods:

Utilized membrane preparations from rat oxyntic gland mucosa.
Employed [125I]15-Leu G-17 as a radioligand to measure gastrin receptor binding.
Assessed the inhibitory effects of various unlabeled gastrin analogues on radioligand binding.

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Main Results:

Unlabeled G-17 inhibited gastrin receptor binding by 50% at 4 x 10(-9) M.
Gastrin tetra-, penta-, and hexapeptides showed 50% inhibition at 1 x 10(-7) M, 3 x 10(-8) M, and 7 x 10(-9) M, respectively.
Analogues lacking the active tetrapeptide or C-terminal amide showed significantly reduced binding inhibition, while atropine, metiamide, and mepyramine did not affect binding.

Conclusions:

The binding specificity of gastrin analogues closely mirrors their biological potencies.
These findings support the role of the identified gastrin receptor in mediating the physiological effects of gastrin.
The active site for gastrin receptor binding involves the C-terminal tetrapeptide and the C-terminal amide group.