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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: Journal of Agricultural and Food Chemistry, Vol. 69, No. 31, 2021, p. 8787-8796.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Shi, J, Zhao, X-H, Fu, Y & Lametsch, R 2021, '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', Journal of Agricultural and Food Chemistry, vol. 69, no. 31, pp. 8787-8796. https://doi.org/10.1021/acs.jafc.1c02858

APA

Shi, J., Zhao, X-H., Fu, Y., & Lametsch, R. (2021). 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. Journal of Agricultural and Food Chemistry, 69(31), 8787-8796. https://doi.org/10.1021/acs.jafc.1c02858

Vancouver

Shi J, Zhao X-H, Fu Y, Lametsch R. 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. Journal of Agricultural and Food Chemistry. 2021;69(31):8787-8796. https://doi.org/10.1021/acs.jafc.1c02858

Author

Shi, Jia ; Zhao, Xin-Huai ; Fu, Yu ; Lametsch, Rene. / 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. In: Journal of Agricultural and Food Chemistry. 2021 ; Vol. 69, No. 31. pp. 8787-8796.

Bibtex

@article{ccea0711f0904e24886b30ad93c38711,
title = "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",
abstract = "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. ",
keywords = "caseinate, cell barrier, IEC-6 cells, lipopolysaccharide, tight junction, transglutaminase",
author = "Jia Shi and Xin-Huai Zhao and Yu Fu and Rene Lametsch",
note = "Publisher Copyright: {\textcopyright} 2021 American Chemical Society.",
year = "2021",
doi = "10.1021/acs.jafc.1c02858",
language = "English",
volume = "69",
pages = "8787--8796",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "31",

}

RIS

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