Regulation of Tight Junction Permeability by Intestinal Bacteria and Dietary Components
Dulantha Ulluwishewa,Rachel C. Anderson,Warren C. McNabb,Warren C. McNabb,Paul J. Moughan,Jerry M. Wells,Nicole C. Roy +6 more
TLDR
The human intestinal epithelium is formed by a single layer of epithelial cells that separates the intestinal lumen from the underlying lamina propria, which is sealed by tight junctions (TJ), which regulate the permeability of the intestinal barrier.Abstract:
The human intestinal epithelium is formed by a single layer of epithelial cells that separates the intestinal lumen from the underlying lamina propria. The space between these cells is sealed by tight junctions (TJ), which regulate the permeability of the intestinal barrier. TJ are complex protein structures comprised of transmembrane proteins, which interact with the actin cytoskeleton via plaque proteins. Signaling pathways involved in the assembly, disassembly, and maintenance of TJ are controlled by a number of signaling molecules, such as protein kinase C, mitogen-activated protein kinases, myosin light chain kinase, and Rho GTPases. The intestinal barrier is a complex environment exposed to many dietary components and many commensal bacteria. Studies have shown that the intestinal bacteria target various intracellular pathways, change the expression and distribution of TJ proteins, and thereby regulate intestinal barrier function. The presence of some commensal and probiotic strains leads to an increase in TJ proteins at the cell boundaries and in some cases prevents or reverses the adverse effects of pathogens. Various dietary components are also known to regulate epithelial permeability by modifying expression and localization of TJ proteins.read more
Citations
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References
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Journal ArticleDOI
Junctional complexes in various epithelia
TL;DR: The tight junction is impervious to concentrated protein solutions and appears to function as a diffusion barrier or "seal," and the desmosome and probably also the zonula adhaerens may represent intercellular attachment devices.
Journal ArticleDOI
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TL;DR: Rho appears to inhibit myosin phosphatase through the action of Rho-kinase, which is activated by GTP·RhoA, phosphorylation of MBS and MLC in NIH 3T3 cells.
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Occludin: a novel integral membrane protein localizing at tight junctions.
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Journal ArticleDOI
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