Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function: lessons from mutant animals and proteins.

@article{Mitic2000MolecularPA,
  title={Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function: lessons from mutant animals and proteins.},
  author={Laura L. Mitic and Christina M Van Itallie and James Melvin Anderson},
  journal={American journal of physiology. Gastrointestinal and liver physiology},
  year={2000},
  volume={279 2},
  pages={
          G250-4
        }
}
Tight junctions form the major paracellular barrier in epithelial tissues. Barrier-sealing properties are quite variable among cell types in terms of electrical resistance, solute and water flux, and charge selectivity. A molecular explanation for this variability appears closer following identification of the transmembrane proteins occludin and members of the claudin multigene family. For example, the human phenotype of mutations in claudin-16 suggests that it creates a channel that allows… 
The role of claudins in determining paracellular charge selectivity.
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Evidence that claudins are functional components of the barrier in tight junctions in the lung is highlighted and Alterations in claudin expression profiles may contribute to epithelial lung dysfunction during infection and inflammation.
Paracellular barrier and channel functions of TJ claudins in organizing biological systems: advances in the field of barriology revealed in knockout mice.
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How, sometimes in concert with canonical transporters and channels, the paracellular barrier and channel functions of claudins sophisticatedly organize biological systems are described.
Functions of claudin tight junction proteins and their complex interactions in various physiological systems.
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The complex interactions of claudins in various physiological systems are highlighted and a possible role for a coregulation mechanism is suggested.
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TLDR
These results provide the first direct demonstration of the ability of a claudin to influence paracellular ion selectivity and support a role for the claudins in creating selective channels through the tight-junction barrier.
Overexpression of claudin-7 decreases the paracellular Cl– conductance and increases the paracellular Na+ conductance in LLC-PK1 cells
TLDR
The studies demonstrated for the first time that the effect of claudin-7 overexpression in LLC-PK1 cells on paracellular transport is mediated through a concurrent decrease in the parACEllular conductance to Cl– and an increase in theParacellular conductances to Na+.
Tight junctions contain oligomeric protein assembly critical for maintaining blood–brain barrier integrity in vivo
TLDR
This study investigates the constitutive trafficking of the TJ transmembrane proteins occludin and claudin‐5 that are essential for forming the TJ seal between microvascular endothelial cells that inhibits paracellular diffusion and suggests that oligomerization of occluda involves disulfide bond formation within trans Membrane regions.
Tight junctions of the blood-brain barrier: development, composition and regulation.
TLDR
Crosstalk between components of the tight junction- and the cadherin-catenin system of the adherens junction suggests a close functional interdependence of the two cell-cell contact systems.
MicroRNAs regulate tight junction proteins and modulate epithelial/endothelial barrier functions
TLDR
This review summarizes available data on the role and targeting of miRNAs in the maintenance of epithelial and/or endothelial barriers and describes how these barriers need to be tightly regulated and controlled.
Tight junction proteins: a novel class of integral membrane proteins
TLDR
The results indicate that occludin, claudin 1 andClaudin 3 are involved in cell-to-cell contacts between keratinocytes in human epidermis, although their functional importance remains unknown.
Molecular perspective on tight-junction assembly and epithelial polarity.
TLDR
How these adhesion systems interact with each other to form apical junctional complexes, and how they reorganize the actin cytoskeleton in a multistage process of cell adhesion, migration, and polarization is discussed.
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References

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TLDR
Insight is provided into Mg2+ homeostasis, the role of a tight junction protein in human disease is demonstrated, and an essential component of a selective paracellular conductance is identified.
Occludin and claudins in tight-junction strands: leading or supporting players?
TLDR
This review discusses current understanding of the molecular architecture of tight-junction strands, focusing on the recent discovery of two distinct types of Tight-Junction-specific integral membrane proteins, occludin and claudins.
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TLDR
Results suggest that claudin-1 is involved in the barrier function at TJs, and introduced claudIn-1 can form TJ-like networks in fibroblasts.
CNS Myelin and Sertoli Cell Tight Junction Strands Are Absent in Osp/Claudin-11 Null Mice
TLDR
It is demonstrated that OSP is the mediator of parallel-array tight junction strands and distinguishes this protein from other intrinsic membrane proteins in tight junctions, providing direct evidence of the pivotal role of the claudin family in generating the paracellular physical barrier of tight junications necessary for spermatogenesis and normal CNS function.
A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells
TLDR
A cDNA clone from a human intestinal cDNA library encoding a small GTPase, rab13, closely related to the yeast Sec4 protein is isolated and it is confirmed that rab13 localized to the junctional complex region of a variety of epithelia, including intestine, kidney, liver, and of endothelial cells.
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TLDR
The results suggest that tight junctions may participate in vesicle targeting at the plasma membrane or alternatively VAP-33 may regulate the localization of occludin.
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TLDR
In vitro binding assays with purified recombinant proteins and immunoprecipitation analyses elucidate direct binding interactions among tight junction-associated proteins, giving insight into their organization as a multimolecular structure.
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TLDR
It is shown that the C-terminal cytoplasmic domain of occludin, the only known transmembrane protein of tight junctions, was sufficient to mediate basolateral expression of a chimeric protein and appears to govern intracellular transport of occLudin.
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TLDR
Findings indicated that the interlamellar strands of oligodendrocyte myelin sheaths can be regarded as a variant of TJ strands found in many other epithelial cells, and that these strands share a specific claudin species, claud in-11/OSP, with those in Sertoli cells to create and maintain the repeated compartments around axons by oligodendedrocytes.
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TLDR
A role for a protein complex containing ASIP and aPKC in the establishment and/or maintenance of epithelial cell polarity is suggested and its asymmetric distribution in polarized cells from worm embryo to mammalian-differentiated cells may mean that the complex functions generally in the organization of cellular asymmetry.
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