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Post-activation-mediated changes in opioid receptors detected by N-terminal antibodies

Academic Article
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Overview

authors

  • Gupta, A.
  • Rozenfeld, R.
  • Gomes, I.
  • Raehal, K. M.
  • Decaillot, F. M.
  • Bohn, Laura
  • Devi, L. A.

publication date

  • April 2008

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The majority of studies examining activity-induced conformational changes in G protein-coupled receptors have focused on transmembrane helices or intracellular regions. Relatively few studies have examined the involvement of the extracellular region in general and the N-terminal region in particular in this process. To begin to address this, we generated a series of antibodies to the N-terminal region of opioid receptors. Characterization of these antibodies revealed that they differentially recognize activated receptors. Recently, we generated monoclonal antibodies that recognize regions proximal to glycosylation sites in the receptor N terminus. Characterization of these antibodies revealed that agonist treatment leads to a decrease in epitope recognition by the antibody presumably because of a movement of the region of the N terminus proximal to glycosylation sites. The time course of the decrease in antibody recognition suggested that it could be due to a post-activation-mediated event. Examination of the involvement of receptor residues in the C-tail and beta-arrestin binding using site-directed mutagenesis and cells or tissues lacking beta-arrestin 2 suggests a role for these desensitization-related mechanisms in governing antibody binding to the receptor. Thus, these N-terminally directed antibodies can differentially recognize post-activation-mediated changes in the C-terminal (intracellular) region of the receptor. Therefore, these conformation-sensitive antibodies represent powerful reagents to probe receptor activation states and provide a potential tool for identifying and characterizing new compounds of therapeutic interest.

subject areas

  • Animals
  • Antibodies
  • Antibodies, Monoclonal
  • Arrestins
  • CHO Cells
  • Cricetinae
  • Cricetulus
  • Dose-Response Relationship, Drug
  • Glycosylation
  • Ligands
  • Phosphorylation
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Receptors, Opioid
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Identity

PubMed Central ID

  • PMC2447646

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M709454200

PubMed ID

  • 18256033
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Additional Document Info

start page

  • 10735

end page

  • 10744

volume

  • 283

issue

  • 16

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