Full characterization of PDX, a neuroprotectin/protectin D1 isomer, which inhibits blood platelet aggregation

FEBS Lett. 2009 Nov 3;583(21):3478-84. doi: 10.1016/j.febslet.2009.10.004. Epub 2009 Oct 8.

Abstract

Our study aimed to establish the complete structure of the main dihydroxy conjugated triene issued from the lipoxygenation (soybean enzyme) of docosahexaenoic acid, named PDX, an isomer of protectin/neuroprotectin D1 (PD1/NPD1) described by Bazan and Serhan. NMR approaches and other chemical characterization (e.g. GC-MS, HPLC and LC-MS/MS) indicated that PDX is 10(S),17(S)-dihydroxy-docosahexa-4Z,7Z,11E,13Z,15E,19Z-enoic acid. The use of (18)O(2) and mass spectrometry showed that PDX is a double lipoxygenation product. Its structure differs from PD1, with E,Z,E geometry (PDX) instead of E,E,Z (PD1) and S configuration at carbon 10 instead of R. PDX inhibits human blood platelet aggregation at sub-micromolar concentrations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arachidonate 15-Lipoxygenase / metabolism
  • Carbon / chemistry
  • Docosahexaenoic Acids / chemistry*
  • Docosahexaenoic Acids / metabolism
  • Docosahexaenoic Acids / pharmacology*
  • Dose-Response Relationship, Drug
  • Gas Chromatography-Mass Spectrometry
  • Humans
  • Hydroxides / chemistry
  • Magnetic Resonance Spectroscopy
  • Platelet Aggregation / drug effects*
  • Soybeans / enzymology
  • Stereoisomerism

Substances

  • Hydroxides
  • protectin D1
  • Docosahexaenoic Acids
  • Carbon
  • hydroxide ion
  • Arachidonate 15-Lipoxygenase