Occludin: a novel integral membrane protein localizing at tight junctions.
Open accessAbstract
Recently, we found that ZO-1, a tight junction-associated protein, was concentrated in the so called isolated adherens junction fraction from the liver (Itoh, M., A. Nagafuchi, S. Yonemura, T. Kitani-Yasuda, Sa. Tsukita, and Sh. Tsukita. 1993. J. Cell Biol. 121:491-502). Using this fraction derived from chick liver as an antigen, we obtained three monoclonal antibodies specific for a approximately 65-kD protein in rats. This antigen was not extractable from plasma membranes without detergent, suggesting that it is an integral membrane protein. Immunofluorescence and immunoelectron microscopy with these mAbs showed that this approximately 65-kD membrane protein was exclusively localized at tight junctions of both epithelial and endothelial cells: at the electron microscopic level, the labels were detected directly over the points of membrane contact in tight junctions. To further clarify the nature and structure of this membrane protein, we cloned and sequenced its cDNA. We found that the cDNA encoded a 504-amino acid polypeptide with 55.9 kDa. A search of the data base identified no proteins with significant homology to this membrane protein. A most striking feature of its primary structure was revealed by a hydrophilicity plot: four putative membrane-spanning segments were included in the NH2-terminal half. This hydrophilicity plot was very similar to that of connexin, an integral membrane protein in gap junctions. These findings revealed that an integral membrane protein localizing at tight junctions is now identified, which we designated as "occludin."
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Claudins and occludins are major tight junction proteins; claudins display essential barrier function and occludins ensure tightness of tight junctions.
“Claudins and occludins that situate in two-cell contacts are the major tight junction proteins.95,96 Claudins display essential barrier function and occludins ensure the tightness of the tight junctions.97”
From The blood–brain barrier: Structure, regulation and drug delivery (2023) · cites this paper as [96]
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- Authors
- Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S.
- Affiliations
- National Institute for Physiological Sciences (JP)
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1993-12-15
- Volume
- 123
- Issue
- 6
- Pages
- 1777-1788
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2290891
- OpenAlex
- W2103831817
- Cited by
- 2,580
- References
- 2
- Citations by year
- 2026: 44 · 2025: 54 · 2024: 50 · 2023: 64 · 2022: 64 · 2021: 82 · 2020: 84 · 2019: 98 · 2018: 86 · 2017: 91 · 2016: 91 · 2015: 94 · 2014: 102 · 2013: 97 · 2012: 115
- FWCI
- 19.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connexins and lens biology
- Keywords
- occludin, tight junctions, integral membrane proteins, ZO-1, adherens junctions, monoclonal antibodies, cDNA cloning, membrane-spanning segments, liver, epithelial cells, endothelial cells, protein localization
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Base Sequence, Brain, Chickens, Epithelial Cells, Epithelium, Intercellular Junctions, Intestines, Liver, Membrane Proteins, Molecular Sequence Data, Myocardium, Organ Specificity, Phosphoproteins, Protein Conformation, Restriction Mapping, Protein Structure, Secondary, DNA, Complementary, Occludin, Zonula Occludens-1 Protein
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