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Characterization of pharmacologically active antipeptide antibodies directed against the first and 2nd extracellular loops of the serotonin 5-ht1a receptor

Academic Article
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Overview

authors

  • Verdot, L.
  • Bertin, B.
  • Guilloteau, D.
  • Strosberg, Donny
  • Hoebeke, J.

publication date

  • July 1995

journal

  • Journal of Neurochemistry  Journal

abstract

  • The immunological properties and the functional role of the first (loop I) and second (loop II) extracellular loops of the human serotonin 5-HT1A receptor were studied with three populations of anti-peptide antibodies: Ab-1 (loop I; sequence Y-Q-V-L-N-K-W-T-L-G-Q-V-T-C-D-L; residues 96-111), Ab-2 (loop II; sequence G-W-R-T-P-E-D-R-S-D-P-D-A-C-T-I-S-K-D-H-G; residues 173-193), and Ab-12 (produced against loop I but cross-reacting with loop II). Chemical modification of peptide amino acid residues revealed the importance of the polyanionic stretch near the N-terminal domain of loop II for Ab-2 antibody binding and the role of the cysteine residues in both loops for the binding of Ab-1 and Ab-12 antibodies. Antibodies Ab-2 and Ab-12 recognized only the nonglycosylated form of the receptor (42 kDa) on immunoblots with transfected HeLa cells expressing the human 5-HT1A receptor but recognized the glycosylated forms (55 and 65 kDa) of rat 5-HT1A receptor from hippocampus membranes. The Ab-1 antibodies recognized no protein band from any cell type studied. Preincubation of transfected HeLa cell membranes with Ab-2 antibodies revealed two affinity binding sites of the 5-HT1A receptor (KDH = 0.54 +/- 0.09 nM and KDL = 13.74 +/- 4.9 nM) for the agonist 8-hydroxy-2-(di-n-[3H]propylamino) tetralin ([3H]8-OH-DPAT) binding, but Ab-1 and Ab-12 revealed only one site (KD of approximately 2.5 nM). In contrast to the Ab-2 antibodies, Ab-1 and Ab-12 antibodies decreased the Bmax of the [3H]8-OH-DPAT binding to 42 and 31%, respectively. These findings suggest that there are at least two epitopes on the extracellular loops: one inducing a high-affinity state for agonist binding and the other interfering with the accessibility of the ligand binding pocket.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antibodies
  • Epitopes
  • HeLa Cells
  • Humans
  • Immunoblotting
  • Ligands
  • Male
  • Molecular Sequence Data
  • Peptide Fragments
  • Rats
  • Rats, Wistar
  • Receptors, Serotonin
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Research

keywords

  • ANTIBODY
  • AUTOIMMUNITY
  • SEROTONIN 5-HT1A RECEPTOR
  • SYNTHETIC PEPTIDE
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Identity

International Standard Serial Number (ISSN)

  • 0022-3042

PubMed ID

  • 7540664
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Additional Document Info

start page

  • 319

end page

  • 328

volume

  • 65

issue

  • 1

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