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

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.
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https://www.hal.inserm.fr/inserm-00429322
Contributor : Evelyne Vericel <>
Submitted on : Monday, November 2, 2009 - 3:15:43 PM
Last modification on : Wednesday, July 8, 2020 - 12:44:08 PM
Long-term archiving on: : Saturday, November 26, 2016 - 2:12:42 PM

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Ping Chen, Bernard Fenet, Sabine Michaud, Nick Tomczyk, Evelyne Véricel, et al.. Full characterization of PDX, a neuroprotectin/protectin D1 isomer, which inhibits blood platelet aggregation.. FEBS Letters, Wiley, 2009, 583 (21), pp.3478-84. ⟨10.1016/j.febslet.2009.10.004⟩. ⟨inserm-00429322⟩

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