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High-affinity binding sites for gastrin on isolated rabbit gastric mucosal cells
European Journal of Pharmacology
|August 13, 1982
Summary
Researchers identified specific binding sites for a gastrin analogue, [125I](Nle11)-HG-13, on rabbit gastric mucosal cells. This finding advances understanding of gastrin receptor interactions in the stomach.
Area of Science:
- Gastroenterology
- Endocrinology
- Molecular Biology
Background:
- Gastrin is a key hormone regulating gastric acid secretion.
- Understanding gastrin's cellular interactions is crucial for gastrointestinal research.
Purpose of the Study:
- To investigate the specific binding of a gastrin analogue to isolated rabbit gastric mucosal cells.
- To characterize the binding sites and their affinity for the gastrin analogue.
Main Methods:
- Utilized a radiolabeled gastrin analogue, [125I](Nle11)-HG-13, for binding assays.
- Performed experiments on isolated rabbit gastric mucosal cells at varying temperatures and with different competing ligands.
- Determined dissociation constants (Kd) and assessed the reversibility and specificity of binding.
Main Results:
- Identified specific, saturable binding sites for [125I](Nle11)-HG-13 on rabbit gastric mucosal cells with a Kd of 70 pM.
- Observed increased binding with higher incubation temperatures (4°C to 37°C).
- Demonstrated that gastrin analogues, CCK-7, and gastrin antagonists inhibited binding, while other hormones and neurotransmitters did not.
Conclusions:
- Isolated rabbit gastric fundic mucosal cells possess high-affinity binding sites for the gastrin analogue (Nle11)-HG-13.
- These binding sites exhibit specificity for gastrin and related peptides.
- The findings support the existence of distinct gastrin receptors on gastric mucosal cells.