Full characterization of PDX, a neuroprotectin/protectin D1 isomer, which inhibits blood platelet aggregation. - Archive ouverte HAL Access content directly
Journal Articles FEBS Letters Year : 2009

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

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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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Dates and 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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