scholarly journals Intestinal epithelial cells related lncRNA and mRNA expression profiles in dextran sulphate sodium‐induced colitis

2020 ◽  
Author(s):  
Huan Liu ◽  
Teming Li ◽  
Shizhen Zhong ◽  
Min Yu ◽  
Wenhua Huang
Keyword(s):  
Epithelial Cells ◽  
Mrna Expression ◽  
Intestinal Epithelial Cells ◽  
Expression Profiles ◽  
Intestinal Epithelial ◽  
Dextran Sulphate ◽  
Dextran Sulphate Sodium

scholarly journals Sodium butyrate stimulates NHE8 expression via its role on activating NHE8 basal promoter activity

2015 ◽  
Vol 309 (6) ◽  
pp. G500-G505 ◽  
Author(s):  
Hua Xu ◽  
Anthony McCoy ◽  
Jing Li ◽  
Yang Zhao ◽  
Fayez K. Ghishan
Keyword(s):  
Epithelial Cells ◽  
Mrna Expression ◽  
Promoter Region ◽  
Intestinal Epithelial Cells ◽  
Gene Promoter ◽  
Sodium Absorption ◽  
Intestinal Epithelial ◽  
Mobility Shift ◽  
Bacterial Fermentation ◽  
Butyrate Treatment

Butyrate is a major metabolite in colonic lumen. It is produced from bacterial fermentation of dietary fiber. Butyrate has been shown to stimulate electroneutral sodium absorption through its regulation on sodium/hydrogen exchanger 3 (NHE3). Although NHE8, the newest addition of intestinal NHE family, is involved in sodium absorption in the intestinal tract, whether butyrate modulates NHE8 expression in the intestinal epithelial cells is not known. In the current study, we showed that butyrate treatment strongly induced NHE8 protein and NHE8 mRNA expression in human intestinal epithelial cells. Transfection with the human NHE8 promoter reporter constructs showed that butyrate treatment stimulated reporter gene expression at an amount comparable with its stimulation of NHE8 mRNA expression. Interestingly, a similar result was also observed in human NHE8 promoter transfected cells after trichostatin (TSA) treatment. Gel mobility shift assay identified an enhanced Sp3 protein binding on the human NHE8 basal promoter region upon butyrate stimulation. Furthermore, Sp3 acetylation modification is involved in butyrate-mediated NHE8 activation in Caco-2 cells. Our findings suggest that the mechanism of butyrate action on NHE8 expression involves enhanced Sp3 interaction at the basal promoter region of the human NHE8 gene promoter to activate NHE8 gene transcription. Thus butyrate is involved in intestinal regulation of NHE8 resulting enhanced sodium absorption.

scholarly journals Rspo3 regulates abnormal differentiation of small intestinal epithelial cells in diabetic state

2021 ◽  
Author(s):  
Ti-Dong Shan ◽  
Yue Han ◽  
Xue-Guo Sun ◽  
Yue-Ping Jiang ◽  
Li Chen
Keyword(s):  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Expression Profiles ◽  
Underlying Mechanism ◽  
Bioinformatic Analysis ◽  
Luciferase Reporter ◽  
Intestinal Epithelial ◽  
Definitive Evidence ◽  
Small Intestinal

Abstract Objective: The problems caused by diabetes mellitus (DM) related complications are the focus in clinical treatment. However, little is known about diabetic enteropathy (DE) and its the potential underlying mechanism. Methods: Intestinal cells (IEC) and Intestinal stem cells (IESC) obtained from BKS.Cg-Dock7m+/+Leprdb/JNju (DM) mice were used to detect Rspo3 by RT-qPCR, western blotting, Immunohistochemistry, and immunofluorescence. The role of Rspo3 in the abnormal differentiation of IECs of DM was clarified by knockout experiments. Through miRNA expression profiles, bioinformatic analysis, and RT-qPCR, we further analyzed differentiation related miRNA from IECs in DM mice. Results: The abnormal differentiation of small intestinal epithelial cells (IECs) was found in DM state. The expression of R-spondin 3 (Rspo3) was upregulated in IECs of DM state. And this phenomenon was associated with R-spondin 3 (Rspo3) overexpression. Additionally, Rspo3 is a major determinant of Lgr5+ stem cell identity upon DM state. Microarray analysis, Bioinformatics analysis and luciferase reporter assays revealed that microRNA (miR)-380-5p was directly targeted Rspo3. Moreover, miR-380-5p upregulation was observed to attenuate the abnormal differentiation of IECs through Rspo3 expression. Conclusion: Together, our results provide definitive evidence for the essential role of Rspo3 in differentiation of small intestinal epithelial cells (IECs) in DM state.

scholarly journals Surface Expression of Toll-Like Receptor 9 Is Upregulated on Intestinal Epithelial Cells in Response to Pathogenic Bacterial DNA

2007 ◽  
Vol 75 (5) ◽  
pp. 2572-2579 ◽  
Author(s):  
Julia B. Ewaschuk ◽  
Jody L. Backer ◽  
Thomas A. Churchill ◽  
Florian Obermeier ◽  
Denis O. Krause ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mrna Expression ◽  
Intestinal Epithelial Cells ◽  
Surface Expression ◽  
Intestinal Epithelial ◽  
Toll Like Receptor ◽  
Colonic Epithelial Cells ◽  
Bacterial Dna ◽  
Tlr9 Expression ◽  
Ht 29

ABSTRACT Colonic epithelial cells are constantly exposed to high levels of bacterial DNA in the intestinal lumen and must recognize and respond appropriately to pathogens, while they maintain a tolerance to nonpathogenic commensal bacterial strains. Bacterial DNA is recognized by Toll-like receptor 9 (TLR9). The aim of this study was to investigate TLR9 expression and localization in colonic epithelial cells under basal conditions and in response to bacterial DNA. HT-29 cells were exposed to DNA from various strains of commensal and pathogenic microbes. TLR9 mRNA expression was determined by real-time reverse transcription-PCR, and interleukin-8 (IL-8) secretion was measured by an enzyme-linked immunosorbent assay. Localization of TLR9 was determined by flow cytometry in HT-29 cells and by immunofluorescence in HT-29 cells and mouse colonic tissue. Immunofluorescence and flow cytometric analyses demonstrated that there was intracellular and surface expression of TLR9 in HT-29 cells under basal conditions. Exposure of cells to DNA from pathogenic strains of Salmonella and Escherichia coli resulted in a significant increase in TLR9 mRNA expression. Salmonella enterica serovar Dublin DNA increased surface TLR9 protein and IL-8 secretion. There was no change in mRNA levels or localization of TLR9 in response to Bifidobacterium breve. Chloroquine did not block IL-8 secretion in response to S. enterica serovar Dublin DNA. TLR9 was expressed on the colonic apical surface in wild-type mice but not in germfree mice. These results demonstrate that intestinal epithelial cells recognize pathogenic bacterial DNA and respond by increasing surface localization and expression of TLR9, suggesting that the epithelial inflammatory response to pathogenic DNA is mediated at least in part by increased TLR9 expression.

scholarly journals Uptake of Manganese from the Manganese-Lysine Complex in Primary Chicken Intestinal Epithelial Cells

Animals ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 559
Author(s):  
Shiping Bai ◽  
Keying Zhang ◽  
Xuemei Ding ◽  
Jianping Wang ◽  
Qiufeng Zeng ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mrna Expression ◽  
Transport System ◽  
Intestinal Epithelial Cells ◽  
Mrna Level ◽  
Intestinal Epithelial ◽  
Divalent Metal Transporter 1 ◽  
Divalent Metal Transporter ◽  
Cationic Amino Acid ◽  
Metal Transporter

Organic manganese (Mn) sources can replace inorganic Mn as dietary Mn supplements in poultry. To compare the uptake of Mn from the Mn-lysine complex (MnLys) and MnSO4, we first established the primary chicken intestinal epithelial cells (IECs) model and used it to determine Mn uptake. The MnLys increased the uptake of Mn compared to MnSO4. The uptake of Mn decreased in the IECs with Fe addition in the medium regardless of the Mn sources. The MnLys decreased the Mn2+ efflux transporter ferroportin 1 (FPN1) mRNA level but did not influence the Mn2+ influx transporter divalent metal transporter 1 (DMT1) mRNA expression when compared to MnSO4. The results above indicated that the increase of Mn accumulation for MnLys at least partly was due to the decrease of Mn efflux by reduced FPN1 expression. The addition of N-ethylmaleimide, an L-lysine transport system y+ inhibitor, decreased the uptake of Mn from MnLys but did not affect the uptake of Mn from MnSO4. The cycloheximide, as an L-lysine transport system b0,+ activator, increased the uptake of Mn from MnLys, whereas they did not influence the uptake of Mn from MnSO4. The MnLys increased the system y+ members cationic amino acid transporter (CAT) 1 and CAT2, and system b0,+ components rBAT and b0,+AT mRNA expression when compared to MnSO4. These results suggested that the uptake of MnLys complex might be transported by CAT1/2 and system b0,+, which was different from the ionized Mn2+ uptake pathway. In conclusion, the uptake of Mn from MnLys complex not only might be uptake through the ionized Mn2+ pathway, but also appeared to be transported through the CAT1/2 and system b0,+ in primary chicken IECs.

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