Differential proteomic analysis of HT29 Cl.16E and intestinal epithelial cells by LC ESI/QTOF mass spectrometry

2009 ◽  
Vol 72 (5) ◽  
pp. 865-873 ◽  
Author(s):  
Paolo Nanni ◽  
Laura Mezzanotte ◽  
Giulia Roda ◽  
Alessandra Caponi ◽  
Fredrik Levander ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Epithelial Cells ◽  
Proteomic Analysis ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial

Fructooligosaccharide Inhibits the Absorption of β-conglycinin (A Major Soybean Allergen) in IPEC-J2

2018 ◽  
Vol 15 (1-2) ◽  
Author(s):  
Yuan Zhao ◽  
Shiyao Zhang ◽  
Xiaodong Zhang ◽  
Li Pan ◽  
Nan Bao ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Enzymatic Hydrolysis ◽  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Time Dependent ◽  
Dependent Manner ◽  
Intestinal Epithelial ◽  
Intracellular Accumulation ◽  
Novel Therapeutic ◽  
Soybean Allergen

AbstractDissecting the inhibited variation of allergen absorption could contribute to the development of novel therapeutic or preventive treatments for food/feed allergies. This study investigated the effects of fructooligosaccharide (FOS) on the absorption, intracellular accumulation of intact or hydrolysed β-conglycinin in porcine intestinal epithelial cells (IPEC-J2). As demonstrated by ELISA and immunoblotting, β-conglycinin was absorbed in a dose- and time-dependent manner (p < 0.05). Actually, β-conglycinin was easily transported and absorbed after enzymatic hydrolysis. Three peptides (52 kDa, 30 kDa and 25 kDa) were produced during transcellular absorption of intact or hydrolysed β-conglycinin. FOS inhibited the absorption of β-conglycinin, especially the 52 and 30 kDa peptides. The immunoreactive peptides derived from the 52, 35 or 22 kDa peptides were the substrings of the known epitopes determined by mass spectrometry and bioinformatic analyses. These results indicate that FOS can efficiently inhibit the absorption of 52 and 30 kDa peptides derived from β-conglycinin.

Proteomic analysis of nuclear proteins from proliferative and differentiated human colonic intestinal epithelial cells

PROTEOMICS ◽  
2003 ◽  
Vol 4 (1) ◽  
pp. 93-105 ◽  
Author(s):  
Natacha Turck ◽  
Sophie Richert ◽  
Patrick Gendry ◽  
Jeanne Stutzmann ◽  
Michèle Kedinger ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Proteomic Analysis ◽  
Intestinal Epithelial Cells ◽  
Nuclear Proteins ◽  
Intestinal Epithelial

The Immunoreactive Protein was Produced During Absorption of Glycinin or its Hydrolysate in IPEC-J2

2017 ◽  
Vol 13 (9) ◽  
Author(s):  
Yuan Zhao ◽  
Shiyao Zhang ◽  
Gaowa Naren ◽  
Guixin Qin
Keyword(s):  
Mass Spectrometry ◽  
Epithelial Cells ◽  
Immunosorbent Assay ◽  
Intestinal Epithelial Cells ◽  
Enzyme Linked Immunosorbent Assay ◽  
Intestinal Epithelial ◽  
Intracellular Accumulation ◽  
Immunoreactive Protein ◽  
Gut Epithelium

AbstractThe allergens absorbed in immunoreactive form by the gut epithelium might induce the occurrence of allergy. The purpose of this study was to investigate the absorption and intracellular accumulation of the intact or hydrolyzed glycinin in the porcine intestinal epithelial cells (IPEC-J2). The IPEC-J2 cells were incubated by 0, 0.25, 0.5 and 1.0 mg/mL glycinin or its hydrolysate for 2, 4, 8 or 12 h. The amounts of immunoreactive glycinin were measured by enzyme-linked immunosorbent assay. The intact and hydrolyzed glycinin fragments of epithelial absorption were identified by immunoblotting and mass spectrometry (MS). We found that glycinin or its hydrolysate is expensively absorbed with the increase of dose and time. The 35 kD or 22 kD protein with glycinin-specific epitopes was detected in the intracellular extracts and basolateral solutions. The results indicate that the glycinin or its hydrolysate could be absorbed; meanwhile, the 35kD or 22kD protein was correspondingly produced during absorption.

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