Autotaxin-lysophosphatidic acid-LPA3 signaling at the embryo-epithelial boundary controls decidualization pathways

EMBO J. 2017 Jul 14;36(14):2146-2160. doi: 10.15252/embj.201696290. Epub 2017 Jun 6.

Abstract

During pregnancy, up-regulation of heparin-binding (HB-) EGF and cyclooxygenase-2 (COX-2) in the uterine epithelium contributes to decidualization, a series of uterine morphological changes required for placental formation and fetal development. Here, we report a key role for the lipid mediator lysophosphatidic acid (LPA) in decidualization, acting through its G-protein-coupled receptor LPA3 in the uterine epithelium. Knockout of Lpar3 or inhibition of the LPA-producing enzyme autotaxin (ATX) in pregnant mice leads to HB-EGF and COX-2 down-regulation near embryos and attenuates decidual reactions. Conversely, selective pharmacological activation of LPA3 induces decidualization via up-regulation of HB-EGF and COX-2. ATX and its substrate lysophosphatidylcholine can be detected in the uterine epithelium and in pre-implantation-stage embryos, respectively. Our results indicate that ATX-LPA-LPA3 signaling at the embryo-epithelial boundary induces decidualization via the canonical HB-EGF and COX-2 pathways.

Keywords: LPA 3; autotaxin; decidualization; embryo implantation; lysophosphatidic acid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cyclooxygenase 2 / metabolism
  • Decidua / growth & development*
  • Embryo, Mammalian / physiology*
  • Embryonic Development
  • Female
  • Gene Knockout Techniques
  • Heparin-binding EGF-like Growth Factor / metabolism
  • Lysophospholipids / metabolism*
  • Mice
  • Mice, Knockout
  • Phosphoric Diester Hydrolases / metabolism*
  • Receptors, Lysophosphatidic Acid / deficiency
  • Receptors, Lysophosphatidic Acid / metabolism*
  • Signal Transduction*
  • Uterus / physiology*

Substances

  • Hbegf protein, mouse
  • Heparin-binding EGF-like Growth Factor
  • Lpar3 protein, mouse
  • Lysophospholipids
  • Receptors, Lysophosphatidic Acid
  • Ptgs2 protein, mouse
  • Cyclooxygenase 2
  • Phosphoric Diester Hydrolases
  • alkylglycerophosphoethanolamine phosphodiesterase
  • lysophosphatidic acid