PLoS One

2012,7(7):e39855 PubMedCentralPubMedCrossRef Com

PLoS One

2012,7(7):e39855.PubMedCentralPubMedCrossRef Competing interests None of the investigators has any financial interest or financial Selleck EPZ015938 conflict with the subject matter or materials discussed in this report. All authors read and approved the final manuscript. Authors’ contributions SS and JD contributed to the study design, AC, MS design and the development of the pyrosequencing technique, CM, MJI, MAL, MAV, MF facilitate the background and support the mycobacterial isolates genotyping studies. AC and SS analysed data and drafted the manuscript. All authors read and approved the final manuscript.”
“Background Celiac disease (CD) is a chronic inflammatory disease in the small intestine of genetically predisposed individuals triggered by the gluten fraction of wheat, rich in glutamine and proline, or the homologous Foretinib mw proteins from barley and rye. The major part of toxic components is contained

in gliadin, the alcohol-soluble fraction of gluten. In humans, the undigested molecules of gliadin are resistant to degradation by gastric, pancreatic, and intestinal brush-border membrane proteases and thus remain in the intestinal lumen after gluten ingestion [1]. CD is characterized by enhanced paracellular permeability and an impairment in the integrity of the intestinal barrier [2] that allows the interactions of gluten peptides with antigen-presenting cells in the lamina propria. Gliadin is rich in glutamine and the presence of numerous glutamine acceptor proteins in the extracellular

matrix could be responsible for the formation of cross-links between gliadin and matrix proteins. In turn, this gliadin immobilization to extracellular matrix proteins could provide a long-term availability of toxic gliadin fractions in the mucosa [3]. However, there is still much debate about the possible interactions of gliadin (and/or its peptide derivatives) with intestinal epithelia and the mechanism(s) through which it crosses the epithelial barrier to reach the submucosa [4]. Integrity of the intestinal barrier depends on a complex of proteins composing different intercellular junctions, including tight junctions (TJs) and adherens Amobarbital junctions [5]. Major transmembrane and cytosolic TJ proteins in the mammalian epithelium include Zonula Occludens ZO-1 and ZO-2, Occludin and Claudins. These proteins are thought to constitute the backbone of TJ strands and to modulate some functions of TJs, respectively [6]. ZO-1 and ZO-2 are the cytoplasmic faces of TJs and directly bind to the COOH terminus of intracellular domain of Occludin. The interaction between Occludin and ZO-1 or ZO-2 protein is crucial for maintaining normal structure of the TJs and epithelial barrier function [6]. Occludin is a 65-kDa integral plasma-membrane protein.

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