Occludin: a novel integral membrane protein localizing at tight junctions

@article{Furuse1993OccludinAN,
  title={Occludin: a novel integral membrane protein localizing at tight junctions},
  author={Mikio Furuse and Tetsuaki Hirase and Masahiko Itoh and Akira Nagafuchi and Shigenobu Yonemura and Sachiko Tsukita},
  journal={The Journal of Cell Biology},
  year={1993},
  volume={123},
  pages={1777 - 1788},
  url={https://api.semanticscholar.org/CorpusID:428210}
}
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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66 References

The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy

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Investigation of the relative localization of ZO-1 and cingulin in Madin-Darby canine kidney cells, chicken small intestine, rat kidney distal convoluted tubule, and a hepatoma cell line demonstrated that they are immunologically unrelated and that, in the colon, cedulin is a single polypeptide with a molecular mass of 140 kDa.

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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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Structure, biochemistry, and assembly of epithelial tight junctions.

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Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1.

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The molecular organization of tight junctions

The cloning of a 220-kD protein, originally identified at the undercoat of cadherin-containing cell-cell contact sites, in nonepithelial cells and its characterization as the mouse homologue of ZO-1 raises new questions about the roles of these proteins in TJ assembly and function.

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