The Experts below are selected from a list of 270 Experts worldwide ranked by ideXlab platform
Yashwant R Mahida - One of the best experts on this subject based on the ideXlab platform.
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Selective reduction of intestinal trefoil factor in untreated coeliac disease
Clinical and Experimental Immunology, 2002Co-Authors: Carolina Ciacci, Daniel K Podolsky, Dolores Di Vizio, R. Seth, G. Insabato, Gabriele Mazzacca, Yashwant R MahidaAbstract:The trefoil factor family (TFF) encompasses small peptides of which intestinal trefoil factor (ITF) is expressed specifically in goblet cells of the small and large intestine. Previous studies have shown that ITF plays an important role in Mucosal protection and repair. Coeliac disease represents a model of immune-mediated small intestinal inflammation and damage, with recovery on gluten-free diet. The aim of this study was to investigate the expression of ITF in the distal duodenal Mucosa of subjects with coeliac disease, before and after treatment with a gluten-free diet. Expression of ITF and mucin in the distal duodenal biopsies from treated (n = 11) and untreated (n = 9) coeliac subjects and controls (n = 8) was investigated by immunohistochemistry and semiquantitative PCR. In untreated coeliac disease, there was reduction of ITF immunoreactivity in goblet cells but mucin expression was preserved. Mucosal recovery on gluten-free diet was associated with increased ITF immunoreactivity in goblet cells. There was also reduction in the expression of ITF transcripts, relative to MUC2 mRNA, in untreated coeliac duodenal samples, with recovery on gluten-free diet. Our study suggests that there is a selective reduction in the expression of the ITF gene in untreated coeliac disease. Recovery of ITF expression on a gluten-free diet suggests that the Mucosal immune system regulates goblet cell differentiation and ITF expression in the human intestinal Mucosa.
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identification of human intestinal trefoil factor goblet cell specific expression of a peptide targeted for apical secretion
Journal of Biological Chemistry, 1993Co-Authors: Daniel K Podolsky, Kathryn Lynchdevaney, Jennifer L Stow, Philip Oates, Bernadette Murgue, Michelle Debeaumont, Bruce E Sands, Yashwant R MahidaAbstract:Abstract Trefoil peptides are a recently recognized group of small peptides abundantly produced at Mucosal surfaces that offer the opportunity to define mechanisms of Mucosal cell-specific differentiation and to illuminate new mechanisms for the preservation of Mucosal integrity. We report the cDNA cloning of a 75-amino acid human trefoil factor expressed in small and large intestinal Mucosas that is highly homologous to the intestinal trefoil factor, with 70% identity at the amino acid level of the predicted mature protein. This human intestinal trefoil factor is also homologous, although to a lesser extent, to trefoil peptides expressed at other sites in the gastrointestinal tract in man, exhibiting absolute conservation of the P domain motif (CX9CX9CX4CCX9WCF) that defines this family of peptides. These findings indicate a high degree of evolutionary conservation of organ/region-specific members of this peptide family. In situ hybridization of intestinal trefoil factor demonstrates a high degree of expression in mature small intestine villus and colonic epithelial goblet cells. Immunogold staining demonstrates high concentrations of intestinal trefoil factor in the rough endoplasmic reticulum and theca of goblet cells as well as throughout the Mucosal surface, consistent with vectorial secretion of this factor by goblet cells onto the intestinal luminal surface. In addition, intestinal trefoil factor was also localized within columnar epithelial cells by immunogold labeling despite the absence of mRNA. These observations suggest that peptide secreted by goblet cells might be taken up from the luminal surface and transcytosed by enterocytes. Human intestinal trefoil factor expression was also detected in the HT-29N2 and HT-29H2 subclones in conjunction with the emergence of the goblet cell phenotype, but not in the CaCO2 cell line that exhibits enterocytic phenotype. In summary, these findings confirm the existence of a highly conserved family of peptides that are abundantly expressed in distinctive regions throughout the gastrointestinal tract in a highly cell-specific pattern reflecting a goblet cell differentiation pathway. They form one of the more abundant constituents of the interface between the Mucosa and "outside" environment and may provide a new paradigm of regulation of the integrity of epithelial surfaces as well as a previously unrecognized dimension of goblet cell function.
Mark F Cesta - One of the best experts on this subject based on the ideXlab platform.
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normal structure function and histology of Mucosa associated lymphoid tissue
Toxicologic Pathology, 2006Co-Authors: Mark F CestaAbstract:The Mucosa-associated lymphoid tissue (MALT) initiates immune responses to specific antigens encountered along all Mucosal surfaces. MALT inductive sites are secondary immune tissues where antigen sampling occurs and immune responses are initiated. Effector sites, present as diffuse lymphoid tissue along all Mucosal surfaces are the sites of IgA transport across the Mucosal epithelium. Though there are many differences between inductive sites in various organs, they all contain the same basic compartments—follicles, interfollicular regions, subepithelial dome regions, and follicle-associated epithelium. The morphologic differences between MALT and other secondary lymphoid tissues, between the MALT sites of differing anatomic locations, and species differences among laboratory animals are described. The morphologic changes in MALT associated with aging, route of nutrition, and genetic mutation (i.e., the nude and SCID mutations) are also discussed. MALT tissues comprise the Mucosal immune system which can ...
Bing Yu - One of the best experts on this subject based on the ideXlab platform.
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dietary lactobacillus rhamnosus gg supplementation improves the Mucosal barrier function in the intestine of weaned piglets challenged by porcine rotavirus
PLOS ONE, 2016Co-Authors: Changsong Gu, Haiyan Hu, Jun Tang, Daiwen Chen, Bing YuAbstract:Lactobacillus rhamnosus GG (LGG) has been regarded as a safe probiotic strain. The aim of this study was to investigate whether dietary LGG supplementation could alleviate diarrhea via improving jejunal Mucosal barrier function in the weaned piglets challenged by RV, and further analyze the potential roles for apoptosis of jejunal Mucosal cells and intestinal microbiota. A total of 24 crossbred barrows weaned at 21 d of age were assigned randomly to 1 of 2 diets: the basal diet and LGG supplementing diet. On day 11, all pigs were orally infused RV or the sterile essential medium. RV infusion increased the diarrhea rate, increased the RV-Ab, NSP4 and IL-2 concentrations and the Bax mRNA levels of jejunal Mucosa (P<0.05), decreased the villus height, villus height: crypt depth, the sIgA, IL-4 and mucin 1 concentrations and the ZO-1, occludin and Bcl-2 mRNA levels of jejunal Mucosa (P<0.05), and affected the microbiota of ileum and cecum (P<0.05) in the weaned pigs. Dietary LGG supplementation increased the villus height and villus height: crypt depth, the sIgA, IL-4, mucin 1 and mucin 2 concentrations, and the ZO-1, occludin and Bcl-2 mRNA levels of the jejunal Mucosa (P<0.05) reduced the Bax mRNA levels of the jejunal Mucosa (P<0.05) in weaned pigs. Furthermore, dietary LGG supplementation alleviated the increase of diarrhea rate in the weaned pigs challenged by RV (P<0.05), and relieve the effect of RV infection on the villus height, crypt depth and the villus height: crypt depth of the jejunal Mucosa (P<0.05), the NSP4, sIgA, IL-2, IL-4, mucin 1 and mucin 2 concentrations of jejunal Mucosa (P<0.05), the ZO-1, occludin, Bax and Bcl-2 mRNA levels of the jejunal Mucosa (P<0.05), and the microbiota of ileum and cecum (P<0.05) in the weaned pigs challenged by RV. These results suggest that supplementing LGG in diets alleviated the diarrhea of weaned piglets challenged by RV via inhibiting the virus multiplication and improving the jejunal Mucosal barrier function, which was possibly due to the decreasing apoptosis of jejunal Mucosal cells and the improvement of intestinal microbiota.
Daniel K Podolsky - One of the best experts on this subject based on the ideXlab platform.
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Selective reduction of intestinal trefoil factor in untreated coeliac disease
Clinical and Experimental Immunology, 2002Co-Authors: Carolina Ciacci, Daniel K Podolsky, Dolores Di Vizio, R. Seth, G. Insabato, Gabriele Mazzacca, Yashwant R MahidaAbstract:The trefoil factor family (TFF) encompasses small peptides of which intestinal trefoil factor (ITF) is expressed specifically in goblet cells of the small and large intestine. Previous studies have shown that ITF plays an important role in Mucosal protection and repair. Coeliac disease represents a model of immune-mediated small intestinal inflammation and damage, with recovery on gluten-free diet. The aim of this study was to investigate the expression of ITF in the distal duodenal Mucosa of subjects with coeliac disease, before and after treatment with a gluten-free diet. Expression of ITF and mucin in the distal duodenal biopsies from treated (n = 11) and untreated (n = 9) coeliac subjects and controls (n = 8) was investigated by immunohistochemistry and semiquantitative PCR. In untreated coeliac disease, there was reduction of ITF immunoreactivity in goblet cells but mucin expression was preserved. Mucosal recovery on gluten-free diet was associated with increased ITF immunoreactivity in goblet cells. There was also reduction in the expression of ITF transcripts, relative to MUC2 mRNA, in untreated coeliac duodenal samples, with recovery on gluten-free diet. Our study suggests that there is a selective reduction in the expression of the ITF gene in untreated coeliac disease. Recovery of ITF expression on a gluten-free diet suggests that the Mucosal immune system regulates goblet cell differentiation and ITF expression in the human intestinal Mucosa.
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identification of human intestinal trefoil factor goblet cell specific expression of a peptide targeted for apical secretion
Journal of Biological Chemistry, 1993Co-Authors: Daniel K Podolsky, Kathryn Lynchdevaney, Jennifer L Stow, Philip Oates, Bernadette Murgue, Michelle Debeaumont, Bruce E Sands, Yashwant R MahidaAbstract:Abstract Trefoil peptides are a recently recognized group of small peptides abundantly produced at Mucosal surfaces that offer the opportunity to define mechanisms of Mucosal cell-specific differentiation and to illuminate new mechanisms for the preservation of Mucosal integrity. We report the cDNA cloning of a 75-amino acid human trefoil factor expressed in small and large intestinal Mucosas that is highly homologous to the intestinal trefoil factor, with 70% identity at the amino acid level of the predicted mature protein. This human intestinal trefoil factor is also homologous, although to a lesser extent, to trefoil peptides expressed at other sites in the gastrointestinal tract in man, exhibiting absolute conservation of the P domain motif (CX9CX9CX4CCX9WCF) that defines this family of peptides. These findings indicate a high degree of evolutionary conservation of organ/region-specific members of this peptide family. In situ hybridization of intestinal trefoil factor demonstrates a high degree of expression in mature small intestine villus and colonic epithelial goblet cells. Immunogold staining demonstrates high concentrations of intestinal trefoil factor in the rough endoplasmic reticulum and theca of goblet cells as well as throughout the Mucosal surface, consistent with vectorial secretion of this factor by goblet cells onto the intestinal luminal surface. In addition, intestinal trefoil factor was also localized within columnar epithelial cells by immunogold labeling despite the absence of mRNA. These observations suggest that peptide secreted by goblet cells might be taken up from the luminal surface and transcytosed by enterocytes. Human intestinal trefoil factor expression was also detected in the HT-29N2 and HT-29H2 subclones in conjunction with the emergence of the goblet cell phenotype, but not in the CaCO2 cell line that exhibits enterocytic phenotype. In summary, these findings confirm the existence of a highly conserved family of peptides that are abundantly expressed in distinctive regions throughout the gastrointestinal tract in a highly cell-specific pattern reflecting a goblet cell differentiation pathway. They form one of the more abundant constituents of the interface between the Mucosa and "outside" environment and may provide a new paradigm of regulation of the integrity of epithelial surfaces as well as a previously unrecognized dimension of goblet cell function.
Volker Gross - One of the best experts on this subject based on the ideXlab platform.
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nuclear factor κb is activated in macrophages and epithelial cells of inflamed intestinal Mucosa
Gastroenterology, 1998Co-Authors: Gerhard Rogler, Korbinian Brand, Daniela Vogl, Sharon Page, Robert Hofmeister, Tilo Andus, Ruth Knuechel, Patrick A Baeuerle, Jurgen Scholmerich, Volker GrossAbstract:Abstract Background & Aims: Transcription factors of the nuclear factor κB (NF-κB) family play an important role in the regulation of genes involved in inflammation. In inflammatory bowel diseases, proinflammatory cytokines known to be regulated by NF-κB are involved. The aim of this study was to investigate the role of NF-κB activation during Mucosal inflammation in situ. Methods: A monoclonal antibody, α-p65mAb, was applied for immunofluorescence and immunohistochemical analysis that recognizes activated NF-κB. Electrophoretic mobility shift assay was used to directly demonstrate the presence of active DNA-binding NF-κB. Results: Using the α-p65mAb antibody, activated NF-κB could be found in biopsy specimens from inflamed Mucosa but was almost absent in uninflamed Mucosa. The number of cells showing NF-κB activation correlated with the degree of Mucosal inflammation but was not significantly different between inflamed Mucosa from patients with Crohn's disease, ulcerative colitis, and nonspecific colitis or diverticulitis. NF-κB activation was localized in macrophages and in epithelial cells as identified by double-labeling techniques. Electrophoretic mobility shift assay with isolated lamina propria mononuclear cells and epithelial cells confirmed these results. Conclusions: This study shows for the first time the activation of NF-κB during human Mucosal inflammation in situ. In addition to macrophages, epithelial cells contained activated NF-κB, indicating an involvement in the inflammatory process. GASTROENTEROLOGY 1998;115:357-369
