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Molecular Pharmacology

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Research ArticleArticle

The Amino Terminus of Receptor Activity Modifying Proteins Is a Critical Determinant of Glycosylation State and Ligand Binding of Calcitonin Receptor-Like Receptor

Neil J. Fraser, Alan Wise, Jason Brown, Linda M. McLatchie, Martin J. Main and Steven M. Foord
Molecular Pharmacology June 1999, 55 (6) 1054-1059; DOI: https://doi.org/10.1124/mol.55.6.1054
Neil J. Fraser
Receptor Systems, Molecular Pharmacology Unit, GlaxoWellcome Research and Development, Medicines Research Centre, Hertfordshire, United Kingdom
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Alan Wise
Receptor Systems, Molecular Pharmacology Unit, GlaxoWellcome Research and Development, Medicines Research Centre, Hertfordshire, United Kingdom
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Jason Brown
Receptor Systems, Molecular Pharmacology Unit, GlaxoWellcome Research and Development, Medicines Research Centre, Hertfordshire, United Kingdom
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Linda M. McLatchie
Receptor Systems, Molecular Pharmacology Unit, GlaxoWellcome Research and Development, Medicines Research Centre, Hertfordshire, United Kingdom
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Martin J. Main
Receptor Systems, Molecular Pharmacology Unit, GlaxoWellcome Research and Development, Medicines Research Centre, Hertfordshire, United Kingdom
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Steven M. Foord
Receptor Systems, Molecular Pharmacology Unit, GlaxoWellcome Research and Development, Medicines Research Centre, Hertfordshire, United Kingdom
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Abstract

The calcitonin receptor-like receptor (CRLR) can function as either a receptor for calcitonin gene-related peptide (CGRP) or for adrenomedullin (ADM), depending upon the coexpression of a novel family of single transmembrane proteins, which we have called receptor activity modifying proteins or RAMPs. RAMPs 1, 2, and 3 transport CRLR to the plasma membrane with similar efficiencies, however RAMP1 presents CRLR as a terminally glycosylated, mature glycoprotein and a CGRP receptor, whereas RAMPs 2 and 3 present CRLR as an immature, core glycosylated ADM receptor. Characterization of the RAMP2/CRLR and RAMP3/CRLR receptors in HEK293T cells by radioligand binding (125I-ADM as radioligand), functional assay (cAMP measurement), or biochemical analysis (SDS-polyacrylamide gel electrophoresis) revealed them to be indistinguishable, even though RAMPs 2 and 3 share only 30% identity. Chimeric proteins were created with the transmembrane and cytosolic portions of RAMP1 associated with the amino terminus of RAMP2 (RAMP2/1) and vice versa (RAMP1/2). Coexpression of RAMP2/1 with CRLR formed a core glycosylated ADM receptor, whereas the RAMP1/2 chimera generated both core glycosylated and mature forms of CRLR and enabled both ADM and CGRP receptor binding. Hence, the glycosylation state of CRLR appears to correlate with its pharmacology.

Footnotes

    • Received August 17, 1998.
    • Accepted December 28, 1998.
  • Send reprint requests to: Dr. Steven M. Foord, Receptor Systems, GlaxoWellcome Medicines Research Centre, Gunnels Wood Rd., Stevenage, Hertfordshire, SG1 2NY, United Kingdom. E-mail:smf3746{at}ggr.co.uk

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Molecular Pharmacology: 55 (6)
Molecular Pharmacology
Vol. 55, Issue 6
1 Jun 1999
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Research ArticleArticle

The Amino Terminus of Receptor Activity Modifying Proteins Is a Critical Determinant of Glycosylation State and Ligand Binding of Calcitonin Receptor-Like Receptor

Neil J. Fraser, Alan Wise, Jason Brown, Linda M. McLatchie, Martin J. Main and Steven M. Foord
Molecular Pharmacology June 1, 1999, 55 (6) 1054-1059; DOI: https://doi.org/10.1124/mol.55.6.1054

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Research ArticleArticle

The Amino Terminus of Receptor Activity Modifying Proteins Is a Critical Determinant of Glycosylation State and Ligand Binding of Calcitonin Receptor-Like Receptor

Neil J. Fraser, Alan Wise, Jason Brown, Linda M. McLatchie, Martin J. Main and Steven M. Foord
Molecular Pharmacology June 1, 1999, 55 (6) 1054-1059; DOI: https://doi.org/10.1124/mol.55.6.1054
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