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    Milk-derived bioactive peptides inhibit human endothelial-monocyte interactions via PPAR-¿ dependent regulation of NF-¿B

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    Authors
    Marcone, Simone
    Haughton, Karen
    Simpson, Paul J
    Belton, Orina
    Fitzgerald, Desmond J
    Issue Date
    2015-01-20
    Keywords
    ATHEROSCLEROSIS
    INFLAMMATION
    
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    Citation
    Journal of Inflammation. 2015 Jan 20;12(1):1
    URI
    http://dx.doi.org/10.1186/s12950-014-0044-1
    http://hdl.handle.net/10147/560476
    Abstract
    Abstract Background Milk-derived bioactive peptides retain many biological properties and have therapeutic effects in cardiovascular disorders such as atherosclerosis. Under inflammatory conditions the expression of endothelial cells adhesion molecules is induced, increasing monocyte adhesion to human vessel wall, a critical step in the pathogenesis of atherosclerosis. In the present work we explored the effects of milk-derived bioactive peptides on the expression of the inflammatory phenotype of human endothelial cells and their effects on monocyte adherence to endothelial cells. Results Treatment of endothelial cells with milk-derived hydrolysate inhibited their production of inflammatory proteins MCP-1 and IL-8 and expression of VCAM-1, ICAM-1 and E-selectin. Milk derived hydrolysate also attenuated the adhesion of human monocytes to activated endothelial cells. The effect was similar to that obtained in endothelial cells treated with troglitazone, a ligand of peroxisome proliferators-activator receptor-gamma (PPAR-γ). PPAR-γ is a transcription factor which when activated antagonises the pro-inflammatory capability of nuclear factor κB (NF-κB). We further examined whether the effects of milk-derived hydrolysates on endothelial cells may be mediated through NF-κB activation via a PPAR-γ dependent mechanism. The specific PPAR-γ inhibitor, GW9662 blocked the effects of the hydrolysate on the NF-κB-mediated chemokines and adhesion molecules expression in endothelial cells. Conclusions These results suggest that milk-derived bioactive peptides work as anti-atherogenic agents through the inhibition of endothelial-dependent adhesive interactions with monocytes by inhibiting the NF-κB pathway through a PPAR-γ dependent mechanism.
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