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Palmitoylethanolamide counteracts reactive astrogliosis induced by β-amyloid peptide.

Scuderi C, Esposito G, Blasio A, Valenza M, Arietti P, Steardo L, Carnuccio R, De Filippis D, Petrosino S, Iuvone T, Di Marzo V, Steardo L - J. Cell. Mol. Med. (2011)

Bottom Line: Experiments were carried out to investigate PEA's (10(-7) M) effects upon the expression and release of pro-inflammatory molecules in rat primary astrocytes activated by soluble Aβ(1-42) (1 μg/ml) as well as to identify mechanisms responsible for such actions.This effect was reduced by PPAR-α antagonist.Moreover, this ALIAmide, like Aβ, increased 2-AG levels.

View Article: PubMed Central - PubMed

Affiliation: Department of Physiology and Pharmacology, Sapienza University of Rome, Rome, Italy.

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Related in: MedlinePlus

Anti-inflammatory actions of PEA depend upon MAPK inhibition. Aβ-challenged (1 μg/ml) cells were treated with PEA (10–7 M) in the presence of the selective PPAR-γ antagonist (GW9662, 9 nM) or the selective PPAR-α antagonist (MK886, 3 μM). p38 and JNK phosphorylated protein expression was analysed after 30 min. of treatments by Western blot. β-actin was used as loading control. Each bar shows the mean ± S.E.M. of n = 3 independent experiments. ***P < 0.001 versus control; ###P < 0.001 versus Aβ-challenged cells; °P < 0.05 versus Aβ+ PEA-challenged cells.
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fig04: Anti-inflammatory actions of PEA depend upon MAPK inhibition. Aβ-challenged (1 μg/ml) cells were treated with PEA (10–7 M) in the presence of the selective PPAR-γ antagonist (GW9662, 9 nM) or the selective PPAR-α antagonist (MK886, 3 μM). p38 and JNK phosphorylated protein expression was analysed after 30 min. of treatments by Western blot. β-actin was used as loading control. Each bar shows the mean ± S.E.M. of n = 3 independent experiments. ***P < 0.001 versus control; ###P < 0.001 versus Aβ-challenged cells; °P < 0.05 versus Aβ+ PEA-challenged cells.

Mentions: Further experiments were aimed at investigating whether the increase in the production of inflammatory factors induced by Aβ was dependent on the activation of the MAPK pathway. Activation of the MAPKs, p38 MAPK and JNK, was measured by quantifying the level of phosphorylation of each kinase by Western blot 30 min. after the exposure to Aβ (Fig. 4). Treatment of astrocytes with Aβ resulted in an increase in the level of phosphorylation of the kinases, and it was accompanied with the activation of the nuclear factor NF-κB and AP-1, as shown by EMSA analysis (Fig. 5). PEA significantly inhibited MAPK phosphorylation and nuclear transcription factors, NF-κB and AP-1. This inhibition was attenuated by the PPAR-α antagonist, MK886, in a partly, although significant, manner.


Palmitoylethanolamide counteracts reactive astrogliosis induced by β-amyloid peptide.

Scuderi C, Esposito G, Blasio A, Valenza M, Arietti P, Steardo L, Carnuccio R, De Filippis D, Petrosino S, Iuvone T, Di Marzo V, Steardo L - J. Cell. Mol. Med. (2011)

Anti-inflammatory actions of PEA depend upon MAPK inhibition. Aβ-challenged (1 μg/ml) cells were treated with PEA (10–7 M) in the presence of the selective PPAR-γ antagonist (GW9662, 9 nM) or the selective PPAR-α antagonist (MK886, 3 μM). p38 and JNK phosphorylated protein expression was analysed after 30 min. of treatments by Western blot. β-actin was used as loading control. Each bar shows the mean ± S.E.M. of n = 3 independent experiments. ***P < 0.001 versus control; ###P < 0.001 versus Aβ-challenged cells; °P < 0.05 versus Aβ+ PEA-challenged cells.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4373435&req=5

fig04: Anti-inflammatory actions of PEA depend upon MAPK inhibition. Aβ-challenged (1 μg/ml) cells were treated with PEA (10–7 M) in the presence of the selective PPAR-γ antagonist (GW9662, 9 nM) or the selective PPAR-α antagonist (MK886, 3 μM). p38 and JNK phosphorylated protein expression was analysed after 30 min. of treatments by Western blot. β-actin was used as loading control. Each bar shows the mean ± S.E.M. of n = 3 independent experiments. ***P < 0.001 versus control; ###P < 0.001 versus Aβ-challenged cells; °P < 0.05 versus Aβ+ PEA-challenged cells.
Mentions: Further experiments were aimed at investigating whether the increase in the production of inflammatory factors induced by Aβ was dependent on the activation of the MAPK pathway. Activation of the MAPKs, p38 MAPK and JNK, was measured by quantifying the level of phosphorylation of each kinase by Western blot 30 min. after the exposure to Aβ (Fig. 4). Treatment of astrocytes with Aβ resulted in an increase in the level of phosphorylation of the kinases, and it was accompanied with the activation of the nuclear factor NF-κB and AP-1, as shown by EMSA analysis (Fig. 5). PEA significantly inhibited MAPK phosphorylation and nuclear transcription factors, NF-κB and AP-1. This inhibition was attenuated by the PPAR-α antagonist, MK886, in a partly, although significant, manner.

Bottom Line: Experiments were carried out to investigate PEA's (10(-7) M) effects upon the expression and release of pro-inflammatory molecules in rat primary astrocytes activated by soluble Aβ(1-42) (1 μg/ml) as well as to identify mechanisms responsible for such actions.This effect was reduced by PPAR-α antagonist.Moreover, this ALIAmide, like Aβ, increased 2-AG levels.

View Article: PubMed Central - PubMed

Affiliation: Department of Physiology and Pharmacology, Sapienza University of Rome, Rome, Italy.

Show MeSH
Related in: MedlinePlus