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Related Experiment Videos

Prostanoid receptors: subtypes and signaling.

R M Breyer1, C K Bagdassarian, S A Myers

  • 1Division of Nephrology, Department of Medicine, Vanderbilt University, Nashville, Tennessee 37232, USA. rich.breyer@mcmail.vanderbilt.edu

Annual Review of Pharmacology and Toxicology
|March 27, 2001
PubMed
Summary

Prostanoid receptors, a family of G-protein-coupled receptors, mediate the effects of lipid mediators like prostaglandin E2 (PGE2). Alternative splicing in receptor tails affects signaling, phosphorylation, and constitutive activity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Cyclooxygenases produce five prostanoids: PGE(2), PGF(2 alpha), PGI(2), TxA(2), and PGD(2).
  • These prostanoids act as autocrine lipid mediators.
  • They interact with specific G-protein-coupled receptors: EP, FP, IP, TP, and DP.

Purpose of the Study:

  • To characterize the cloned and expressed prostanoid receptors.
  • To understand the structural basis of ligand-binding selectivity.
  • To investigate the role of receptor regions in G-protein interaction and signaling.

Main Methods:

  • Cloning and expression of eight prostanoid receptor cDNAs.
  • Characterization of seven-transmembrane proteins typical of G-protein-coupled receptors.

Related Experiment Videos

  • Analysis of ligand-binding profiles and signal transduction pathways.

    • Main Results:

    • Receptor selectivity is determined by transmembrane sequences and extracellular-loop residues.
    • C-terminal tail regions mediate G-protein interaction selectivity.
    • Alternative splice variants in EP(1), EP(3), FP, and TP receptors alter C-terminal coding sequences.

    Conclusions:

    • C-terminal variants modulate receptor signal transduction, phosphorylation, and desensitization.
    • These variants can also alter agonist-independent constitutive activity.
    • Prostanoid receptor structure dictates ligand binding and G-protein coupling.