Cloning and Functional Characterization of a Complementary DNA Encoding the Murine Fibroblast Bombesin/Gastrin-Releasing Peptide Receptor (original) (raw)
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1Division of Neuroscience, Oregon Regional Primate Research Center Beaverton, Oregon 97006
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1Division of Neuroscience, Oregon Regional Primate Research Center Beaverton, Oregon 97006
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2Department of Neurobiology and Behavior, State University of New York-Stony Brook Stony Brook, New York 11794
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3Vollum Institute for Advanced Biomedical Research Portland, Oregon 97201
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3Vollum Institute for Advanced Biomedical Research Portland, Oregon 97201
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This work was supported by NIH Grants RR-00163 and CA-39237 and grants from the Medical Research Foundation of Oregon, the Council on Tobacco Research, and the American Lung Association of Oregon.
Revision received:
21 September 1990
Accepted:
21 September 1990
Published:
01 December 1990
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E. R. Spindel, E. Giladi, P. Brehm, R. H. Goodman, T. P. Segerson, Cloning and Functional Characterization of a Complementary DNA Encoding the Murine Fibroblast Bombesin/Gastrin-Releasing Peptide Receptor, Molecular Endocrinology, Volume 4, Issue 12, 1 December 1990, Pages 1956–1963, https://doi.org/10.1210/mend-4-12-1956
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Abstract
The amphibian tetradecapeptide bombesin and its mammalian homolog gastrin-releasing peptide are neurotransmitters and paracrine hormones, and are mitogenic for fibroblast and small cell lung carcinoma cell lines. cDNAs encoding the bombesin/gastrin-releasing peptide receptor (BR) expressed by murine Swiss 3T3 fibroblasts were isolated using electrophysiological and luminometric Xenopus oocyte expression assays. Oocytes microinjected with BR transcripts responded to concentrations of bombesin from 1 × 10−10 to 1 × 10−6m. These responses showed homologous desensitization and could be specifically blocked by bombesin antagonists. Sequence analysis showed that the BR has seven membrane-spanning domains and five potential Nlinked glycosylation sites. Data base analysis showed that the BR is most homologous to the tachykinin receptors. Although tyrosine kinase activity has been associated with BR function, no tyrosine kinase homologies occur within the BR sequence.
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Author notes
This work was supported by NIH Grants RR-00163 and CA-39237 and grants from the Medical Research Foundation of Oregon, the Council on Tobacco Research, and the American Lung Association of Oregon.
Copyright © 1990 by The Endocrine Society
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