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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 May;84(9):2698–2702. doi: 10.1073/pnas.84.9.2698

Monoclonal antibody to the gastrin receptor on parietal cells recognizes a 78-kDa protein.

F T Mu, G Baldwin, J Weinstock, D Stockman, B H Toh
PMCID: PMC304725  PMID: 3554245

Abstract

Four monoclonal antibodies reactive by immunofluorescence and by flow microfluorimetry with canine and porcine gastric parietal cell membranes were produced by fusion of mouse NS-1 myeloma cells with splenocytes from mice immunized with a population of canine gastric mucosal cells containing 60-70% parietal cells. One of these, an IgM antibody designated 2C1, reacted with the surface membranes of parietal cells by immunofluorescence, flow microfluorimetry, and immunogold electron microscopy; competed with 125I-labeled gastrin for binding to gastric cells; and inhibited by 56% maximal gastrin stimulation of [14C]aminopyrine uptake in parietal cells. The antibody immunoprecipitated 125I-labeled samples of a 78-kDa gastrin-binding protein purified from membrane extracts of porcine gastrin mucosa but did not recognize the same protein labeled covalently with 125I-labeled gastrin-(2-17)-hexadecapeptide. These observations suggest that the previously identified 78-kDa gastrin-binding protein is the gastrin receptor and that the antibody 2C1 is directed against the gastrin binding site of the gastrin receptor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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