Transglutaminase-Mediated Caseinate Oligochitosan Glycation Enhances the Effect of Caseinate Hydrolysate to Ameliorate the LPS-Induced Damage on the Intestinal Barrier Function in IEC-6 Cells
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Transglutaminase-Mediated Caseinate Oligochitosan Glycation Enhances the Effect of Caseinate Hydrolysate to Ameliorate the LPS-Induced Damage on the Intestinal Barrier Function in IEC-6 Cells. / Shi, Jia; Zhao, Xin-Huai; Fu, Yu; Lametsch, Rene.
I: Journal of Agricultural and Food Chemistry, Bind 69, Nr. 31, 2021, s. 8787-8796.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Transglutaminase-Mediated Caseinate Oligochitosan Glycation Enhances the Effect of Caseinate Hydrolysate to Ameliorate the LPS-Induced Damage on the Intestinal Barrier Function in IEC-6 Cells
AU - Shi, Jia
AU - Zhao, Xin-Huai
AU - Fu, Yu
AU - Lametsch, Rene
N1 - Publisher Copyright: © 2021 American Chemical Society.
PY - 2021
Y1 - 2021
N2 - Some food components can regulate the intestinal barrier function. Herein, the effect of transglutaminase-type oligochitosan glycation on caseinate hydrolysate for its ability to maintain intestinal epithelial integrity and the tight junction (TJ) structure was investigated by assessing and comparing the bioactivities of glycated caseinate hydrolysate and caseinate hydrolysate against the lipopolysaccharide-induced barrier damage in the model cells (rat intestinal epithelial IEC-6 cells). The results from liquid chromatography with tandem mass spectrometry (LC-MS/MS) analysis demonstrated that oligochitosan glycation occurred at the Gln residues of α-S1-casein and α-S2-casein. The two hydrolysates retarded the lipopolysaccharide cytotoxicity toward IEC-6 cells and enhanced the barrier integrity by increasing the transepithelial electrical resistance or decreasing the paracellular permeability. In addition, these two hydrolysates could upregulate both mRNA and protein expression of three TJ proteins in IEC-6 cells. More importantly, the glycated caseinate hydrolysate had higher potential than caseinate hydrolysate to protect IEC-6 cells against the lipopolysaccharide-induced barrier damage, suggesting that the transglutaminase-mediated oligochitosan glycation of proteins is a useful approach to enforce protein biofunctions in the intestine.
AB - Some food components can regulate the intestinal barrier function. Herein, the effect of transglutaminase-type oligochitosan glycation on caseinate hydrolysate for its ability to maintain intestinal epithelial integrity and the tight junction (TJ) structure was investigated by assessing and comparing the bioactivities of glycated caseinate hydrolysate and caseinate hydrolysate against the lipopolysaccharide-induced barrier damage in the model cells (rat intestinal epithelial IEC-6 cells). The results from liquid chromatography with tandem mass spectrometry (LC-MS/MS) analysis demonstrated that oligochitosan glycation occurred at the Gln residues of α-S1-casein and α-S2-casein. The two hydrolysates retarded the lipopolysaccharide cytotoxicity toward IEC-6 cells and enhanced the barrier integrity by increasing the transepithelial electrical resistance or decreasing the paracellular permeability. In addition, these two hydrolysates could upregulate both mRNA and protein expression of three TJ proteins in IEC-6 cells. More importantly, the glycated caseinate hydrolysate had higher potential than caseinate hydrolysate to protect IEC-6 cells against the lipopolysaccharide-induced barrier damage, suggesting that the transglutaminase-mediated oligochitosan glycation of proteins is a useful approach to enforce protein biofunctions in the intestine.
KW - caseinate
KW - cell barrier
KW - IEC-6 cells
KW - lipopolysaccharide
KW - tight junction
KW - transglutaminase
U2 - 10.1021/acs.jafc.1c02858
DO - 10.1021/acs.jafc.1c02858
M3 - Journal article
C2 - 34323484
AN - SCOPUS:85112712510
VL - 69
SP - 8787
EP - 8796
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 31
ER -
ID: 277225708