Article: article from journal or magazin.
n-3 PUFAs modulate T-cell activation via protein kinase C-alpha and -epsilon and the NF-kappaB signaling pathway.
Journal of lipid research
Publication types: Journal Article ; Research Support, Non-U.S. Gov't - Publication Status: ppublish
We elucidated the mechanisms of action of two n-3 PUFAs, eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), in Jurkat T-cells. Both DHA and EPA were principally incorporated into phospholipids in the following order: phosphatidylcholine < phosphatidylethanolamine < phosphatidylinositol/phosphatidylserine. Furthermore, two isoforms of phospholipase A(2) (i.e., calcium-dependent and calcium-independent) were implicated in the release of DHA and EPA, respectively, during activation of these cells. The two fatty acids inhibited the phorbol 12-myristate 13-acetate (PMA)-induced plasma membrane translocation of protein kinase C (PKC)-alpha and -epsilon. The two n-3 PUFAs also inhibited the nuclear translocation of nuclear factor kappaB (NF-kappaB) and the transcription of the interleukin-2 (IL-2) gene in PMA-activated Jurkat T-cells. Together, these results demonstrate that DHA and EPA, being released by two isoforms of phospholipase A(2), modulate IL-2 gene expression by exerting their action on two PKC isoforms and NF-kappaB in Jurkat T-cells.
Cell Membrane, Docosahexaenoic Acids, Eicosapentaenoic Acid, Fatty Acids, Omega-3, Humans, Interleukin-2, Isoenzymes, Jurkat Cells, Lymphocyte Activation, NF-kappa B, Phorbol Esters, Phospholipases A, Phospholipids, Protein Kinase C, Protein Kinase C-alpha, Protein Kinase C-epsilon, Protein Transport, RNA, Messenger, Signal Transduction, T-Lymphocytes
Web of science
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