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Volume 272, Number 5, Issue of January 31, 1997 pp. 2880-2888
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Receptor-induced Internalization of Selective Peptidic µ and  Opioid Ligands

(Received for publication, August 1, 1996, and in revised form, November 4, 1996)

Georges Gaudriault , Dominique Nouel , Claude Dal Farra , Alain Beaudet and Jean-Pierre Vincent

From the Institut de Pharmacologie Moleculaire et Cellulaire, Centre National de la Recherche Scientifique-UPR 411, 660, Route des lucioles, 06560 Valbonne, France and the  Montreal Neurological Institute, Department of Neurology and Neurosurgery, McGill University, Montreal, Quebec, Canada H3A 2B4

The binding and internalization of radioiodinated and fluorescent µ and  opioid peptides in mammalian cells were quantitatively studied by biochemical techniques and directly visualized by confocal microscopy. The labeled peptides were prepared by inserting either a ¹²⁵I-Bolton-Hunter group or a fluorescent probe into the C-terminal part of 5-aminopentylamide derivatives of deltorphin-I and [Lys⁷]dermorphin. The purified derivatives kept most of their specificity and selectivity toward  and µ opioid receptors, respectively. Biochemical and confocal microscopy data showed that both µ and  opioid peptides were internalized in mammalian cells transfected with the corresponding opioid receptor according to a receptor-mediated mechanism. The internalization process was time- and temperature-dependent and was completely blocked by the endocytosis inhibitor phenylarsine oxyde. Internalization of both  and µ ligands occurred from a single large cap at one pole of the cell, indicating that polymerization of ligand-receptor complexes preceeded internalization. Finally, green and red fluorescent analogues of deltorphin-I and [Lys⁷]dermorphin, respectively, were found to internalize through partly distinct endocytic pathways in cells co-transfected with µ and  receptors, suggesting that each of these receptors interacts with distinct proteins mediating intracellular sorting and trafficking.

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