Full characterization of PDX, a neuroprotectin/protectin D1 isomer, which inhibits blood platelet aggregation. - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Accéder directement au contenu
Article Dans Une Revue FEBS Letters Année : 2009

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

Résumé

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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Dates et versions

inserm-00429322 , version 1 (02-11-2009)

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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, 2009, 583 (21), pp.3478-84. ⟨10.1016/j.febslet.2009.10.004⟩. ⟨inserm-00429322⟩
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