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Journal ArticleDOI

Claudins and epithelial paracellular transport.

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TLDR
Information is reviewed on the structure, function, and transcriptional and posttranslational regulation of the claudin family as well as of their evolutionarily distant relatives called the PMP22/EMP/MP20/claudin, or pfam00822, superfamily.
Abstract
▪ Abstract Tight junctions form continuous intercellular contacts controlling solute movement through the paracellular pathway across epithelia. Paracellular barriers vary among epithelia in electrical resistance and behave as if they are lined with pores that have charge and size selectivity. Recent evidence shows that claudins, a large family (at least 24 members) of intercellular adhesion molecules, form the seal and its variable pore-like properties. This evidence comes from the study of claudins expressed in cultured epithelial cell models, genetically altered mice, and human mutants. We review information on the structure, function, and transcriptional and posttranslational regulation of the claudin family as well as of their evolutionarily distant relatives called the PMP22/EMP/MP20/claudin, or pfam00822, superfamily.

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Citations
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The Blood–Brain Barrier

TL;DR: Understanding how these different cell populations interact to regulate the barrier properties is essential for understanding how the brain functions during health and disease.
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The skin: an indispensable barrier

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Adherens and tight junctions: structure, function and connections to the actin cytoskeleton.

TL;DR: The binding interactions of the most studied proteins that occur within each junctional complexes and possible modes of regulation of these interactions are discussed, and the different mechanisms that connect and regulate interactions with the actin cytoskeleton are discussed.
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Intestinal barrier function: molecular regulation and disease pathogenesis.

TL;DR: Clinical and experimental evidence demonstrating intestinal epithelial barrier dysfunction as a major factor contributing to the predisposition to inflammatory diseases, including food allergy, inflammatory bowel diseases, and celiac disease is summarized.
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Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry.

TL;DR: Using an iterative expression cloning approach, claudin-1 (CLDN1), a tight junction component that is highly expressed in the liver, is identified as essential for HCV entry and a new target for antiviral drug development.
References
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Journal ArticleDOI

Occludin: a novel integral membrane protein localizing at tight junctions.

TL;DR: An integral membrane protein localizing at tight junctions is now identified, which is designated as "occludin," which was revealed by a hydrophilicity plot that was very similar to that of connexin, an integral membraneprotein in gap junctions.
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Multifunctional strands in tight junctions.

TL;DR: New insights into the molecular architecture of tight junctions allow us to now discuss the structure and functions of this unique cell–cell adhesion apparatus in molecular terms.
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Claudin-1 and -2: Novel Integral Membrane Proteins Localizing at Tight Junctions with No Sequence Similarity to Occludin

TL;DR: It is indicated that multiple integral membrane proteins with four putative transmembrane domains, occludin and claudins, constitute TJ strands.
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Size-selective loosening of the blood-brain barrier in claudin-5–deficient mice

TL;DR: In claudin-5–deficient mice, the size-selective loosening of the blood-brain barrier was selectively affected, which provides new insight into the basic molecular physiology of BBB and opens a new way to deliver potential drugs across the BBB into the central nervous system.
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Identification of ZO-1 : a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia

TL;DR: Immunoblot analysis of Madin-Darby canine kidney cells demonstrates the presence of a polypeptide similar in molecular weight to that detected in liver, suggesting that this protein is potentially a ubiquitous component of all mammalian tight junctions.
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