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Green Tea Polyphenols Mitigate Gliadin-Mediated Inflammation and Permeability in Vitro. - PubMed - NCBI
Abstract
SCOPE:
Green tea, a polyphenol-rich beverage, has been reported to mitigate a number of inflammatory and hypersensitivity disorders in laboratory models, and has been shown to moderate pathways related to food allergies in vitro. We sought to determine the impact of decaffeinated green tea extract (GTE) on the digestion of gliadin protein in vitro and the effect of physical interactions with GTE on the ability of gliadin to stimulate celiac disease-related symptoms in vitro.
METHODS AND RESULTS:
Complexation of GTE and gliadin in vitro was confirmed by monitoring increases in turbidity upon titration of GTE into a gliadin solution. We observed this phenomenon again during in vitro digestion when gliadin was exposed to the digestive proteases pepsin and trypsin. SDS-PAGE and enzymatic assays revealed that GTE inhibited digestive protease activity and gliadin digestion. Using differentiated Caco-2 cell monolayers as a model of the small intestinal epithelium, we found that complexation of gliadin with GTE reduces gliadin-stimulated monolayer permeability and the release of interleukin (IL)-6 and -8.
CONCLUSION:
Our findings provide support for the potential beneficial effects of GTE as an adjuvant therapy for celiac disease through direct interaction between gliadin proteins and green tea polyphenols.
Abstract
SCOPE:
Green tea, a polyphenol-rich beverage, has been reported to mitigate a number of inflammatory and hypersensitivity disorders in laboratory models, and has been shown to moderate pathways related to food allergies in vitro. We sought to determine the impact of decaffeinated green tea extract (GTE) on the digestion of gliadin protein in vitro and the effect of physical interactions with GTE on the ability of gliadin to stimulate celiac disease-related symptoms in vitro.
METHODS AND RESULTS:
Complexation of GTE and gliadin in vitro was confirmed by monitoring increases in turbidity upon titration of GTE into a gliadin solution. We observed this phenomenon again during in vitro digestion when gliadin was exposed to the digestive proteases pepsin and trypsin. SDS-PAGE and enzymatic assays revealed that GTE inhibited digestive protease activity and gliadin digestion. Using differentiated Caco-2 cell monolayers as a model of the small intestinal epithelium, we found that complexation of gliadin with GTE reduces gliadin-stimulated monolayer permeability and the release of interleukin (IL)-6 and -8.
CONCLUSION:
Our findings provide support for the potential beneficial effects of GTE as an adjuvant therapy for celiac disease through direct interaction between gliadin proteins and green tea polyphenols.