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- Title
Full characterization of PDX, a neuroprotectin/protectin D1 isomer, which inhibits blood platelet aggregation
- Authors
Chen, P.; Fenet, B.; Michaud, S.; Tomczyk, N.; Véricel, E.; Lagarde, M.; Guichardant, M.
- Abstract
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 18O2 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.
- Subjects
BLOOD platelet aggregation; DOCOSAHEXAENOIC acid; MASS spectrometry; IONIC mobility; PLANT enzymes; PREVENTION
- Publication
FEBS Letters, 2009, Vol 583, Issue 21, p3478
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.10.004