Phospholipid Potentially Prevents Pathology
ironjustice
Phospholipids block nuclear factor-kappa B and tau
phosphorylation and inhibit amyloid-beta secretion
in human neuroblastoma cells
Neuroscience, Volume 164, Issue 4, 29
December 2009, Pages 1744-1753
N.R. Pandey, K. Sultan, E. Twomey, D.L. Sparks
Abstract
Inflammation and oxidative stress have been shown to
play a critical role in the pathophysiology that leads
to neurodegeneration.
Omega-6 phospholipids, e.g. dilinoleoylphosphatidylcholine
(DLPC), have been shown to have anti-inflammatory properties
and therefore experiments were undertaken to determine
whether DLPC can prevent inflammatory neurodegenerative
events in the model neuronal cell line, SH-SY5Y.
Tumor necrosis factor (TNF-α) and H2O2 activate
mitogen-activated protein kinase (MAPK) in SH-SY5Y cells
within 5 min and this activation is completely blocked by
DLPC (12 μM). DLPC blocks IκBα phosphorylation in the
SH-SY5Y cells and prevents the phosphorylation and
activation of nuclear factor-kappa B (NF-κB).
The phospholipid inhibits induction of MAPK and NF-κB in
similar fashion to the MEK1/2-inhibitor, U0126 (10 μM).
DLPC completely abolishes TNF-α, H2O2 and
lipopolysaccaride (LPS)-induced neuronal tau
phosphorylation.
Cellular amyloid precursor protein levels are reduced
by DLPC and LPS-induced amyloid-β expression and
secretion in SH-SY5Y cells are completely blocked by
DLPC.
Taken together, these data suggest that DLPC can act
through MAPK to block neuronal inflammatory cascades
and prevent potential pathological consequences in the
neuronal metabolism of amyloid and tau proteins.
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