Prostanoid receptors: structures, properties, and functions

Physiol Rev. 1999 Oct;79(4):1193-226. doi: 10.1152/physrev.1999.79.4.1193.


Prostanoids are the cyclooxygenase metabolites of arachidonic acid and include prostaglandin (PG) D(2), PGE(2), PGF(2alpha), PGI(2), and thromboxne A(2). They are synthesized and released upon cell stimulation and act on cells in the vicinity of their synthesis to exert their actions. Receptors mediating the actions of prostanoids were recently identified and cloned. They are G protein-coupled receptors with seven transmembrane domains. There are eight types and subtypes of prostanoid receptors that are encoded by different genes but as a whole constitute a subfamily in the superfamily of the rhodopsin-type receptors. Each of the receptors was expressed in cultured cells, and its ligand-binding properties and signal transduction pathways were characterized. Moreover, domains and amino acid residues conferring the specificities of ligand binding and signal transduction are being clarified. Information also is accumulating as to the distribution of these receptors in the body. It is also becoming clear for some types of receptors how expression of their genes is regulated. Furthermore, the gene for each of the eight types of prostanoid receptor has been disrupted, and mice deficient in each type of receptor are being examined to identify and assess the roles played by each receptor under various physiological and pathophysiological conditions. In this article, we summarize these findings and attempt to give an overview of the current status of research on the prostanoid receptors.

Publication types

  • Review

MeSH terms

  • Animals
  • GTP-Binding Proteins / physiology
  • Gene Expression Regulation
  • Humans
  • Mice
  • Mice, Knockout
  • Prostaglandins / metabolism
  • Receptors, Prostaglandin / chemistry*
  • Receptors, Prostaglandin / genetics
  • Receptors, Prostaglandin / physiology*
  • Signal Transduction


  • Prostaglandins
  • Receptors, Prostaglandin
  • GTP-Binding Proteins