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Related Experiment Videos

Mapping of HCG-receptor complexes

J J Remy1, L Couture, J Pantel

  • 1Unité Récepteurs et Communication Cellulaire, Biologie Cellulaire et Moléculaire, INRA-Biotechnologies, Jouy-en-Josas, France.

Molecular and Cellular Endocrinology
|December 20, 1996
PubMed
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Researchers explored the porcine LH/CG receptor (pLHR) and its interaction with hCG. They found that specific receptor regions and peptides influence hormone binding and signaling, contributing to a topological model of the hCG-receptor complex.

Area of Science:

  • Endocrinology and Reproductive Biology
  • Molecular and Cellular Biology
  • Structural Biology

Background:

  • The luteinizing hormone/chorionic gonadotropin receptor (LHCGR) mediates the effects of key reproductive hormones.
  • Understanding the molecular interactions between hCG and its receptor is crucial for reproductive health research.
  • Previous studies suggested specific peptide regions within the LHCGR ectodomain are involved in hormone binding and signaling.

Purpose of the Study:

  • To characterize molecular forms of the porcine LH/CG receptor (pLHR) and hCG-receptor complexes.
  • To investigate the roles of specific pLHR ectodomain and endodomain regions in hCG binding and signal transduction.
  • To develop a topological model of the hCG-pLHR complex based on immunochemical and peptide mapping data.

Main Methods:

Related Experiment Videos

  • Production of recombinant pLHR (full-length and ectodomain) and hCG-receptor complexes in COS and insect cell systems.
  • Inhibition studies using synthetic peptides mimicking pLHR ectodomain regions and antisera against these peptides.
  • Immunochemical mapping with monoclonal antibodies (mAbs) against hCG epitopes and anti-peptide antibodies against pLHR regions.

Main Results:

  • Co-expression of pLHR ecto- and endodomains reconstituted a functional receptor, dependent on disulfide bridges.
  • Specific pLHR ectodomain peptides and corresponding antibodies interfered with hCG binding and cAMP production.
  • Monoclonal antibodies revealed hCG 'alpha-tip' and 'beta-tip' epitopes are involved in receptor complex formation, while a conformational epitope is masked.
  • A peptide mimicking the receptor's second extracellular loop (EL2) inhibited hCG-induced cAMP production without affecting binding, supporting a 'negative specificity' model.
  • Antibody binding to hCG site IIIa was hindered by an anti-peptide antibody against pLHR exon 8 (pEx8), suggesting proximity in the complex.

Conclusions:

  • The pLHR ectodomain acts as a screening device, modulating hormone access to the signaling endodomain.
  • Specific interactions between the hCG 'alpha-tip' and the pLHR EL2 region are suggested.
  • The pEx8 region of pLHR is located near the hCG 'alpha-tip' and EL2 in the full-length receptor complex, aiding topological modeling.