Receptor activity modifying proteins regulate the activity of a calcitonin gene-related peptide receptor in rabbit aortic endothelial cells

Autor: Kerstin Leuthäuser, Walter Born, Nicole Bühlmann, Roman Muff, Steven M. Foord, Jan A. Fischer
Rok vydání: 1998
Předmět:
medicine.medical_specialty
Receptor expression
Biophysics
Signal transduction
Calcitonin gene-related peptide
Biology
Receptor Activity-Modifying Protein 2
Receptor Activity-Modifying Protein 3
Biochemistry
Receptor Activity-Modifying Proteins
Cell Line
Receptor Activity-Modifying Protein 1
Adrenomedullin
03 medical and health sciences
0302 clinical medicine
Calcitonin Gene-Related Peptide Receptor Antagonists
Structural Biology
Internal medicine
Cyclic AMP
Genetics
medicine
Enzyme-linked receptor
Animals
Humans
Calcitonin receptor
Molecular Biology
Aorta
Cells
Cultured
030304 developmental biology
0303 health sciences
Receptor activity-modifying protein
Vascular cell
Intracellular Signaling Peptides and Proteins
Membrane Proteins
Cell Biology
Neuropeptide
Endocrinology
RAMP2
RAMP1
COS Cells
Endothelium
Vascular
Rabbits
Peptides
030217 neurology & neurosurgery
Receptors
Calcitonin Gene-Related Peptide
Zdroj: FEBS Letters. 441:366-368
ISSN: 0014-5793
Popis: In Xenopus oocytes with an endogenous calcitonin gene-related peptide (CGRP) receptor, a receptor activity modifying protein (RAMP1) enhancing CGRP stimulated chloride currents of the cystic fibrosis transmembrane regulator was recently cloned [McLatchie, L.M. et al. (1998) Nature 393, 333-339]. Here, transient expression of RAMP1 in rabbit aortic endothelial cells (RAEC) brought about stimulation of cAMP accumulation by human (h) alphaCGRP with an EC50 of 0.41 nM. This was antagonized by a CGRP receptor antagonist alphaCGRP(8-37). Co-expression of RAMP3 together with RAMP1 reduced the maximal cAMP response to h alphaCGRP by 47% (P0.05). The cells also express RAMP2 encoding mRNA and an adrenomedullin (ADM) receptor coupled to stimulation of cAMP formation by hADM (EC50 0.18 nM). The latter was antagonized by an ADM receptor antagonist hADM(22-52). In conclusion, expression of a CGRP receptor in RAEC requires RAMP1. The same receptor presumably recognizes ADM making use of endogenous RAMP2. The results reveal competition between the different RAMPs in the regulation of CGRP/ADM receptor activity.
Databáze: OpenAIRE
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