The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.
Tight junction-based epithelial microenvironment and cell proliferation
Open accessAbstract
Belt-like tight junctions (TJs), referred to as zonula occludens, have long been regarded as a specialized differentiation of epithelial cell membranes. They are required for cell adhesion and paracellular barrier functions, and are now thought to be partly involved in fence functions and in cell polarization. Recently, the molecular bases of TJs have gradually been unveiled. TJs are constructed by TJ strands, whose basic frameworks are composed of integral membrane proteins with four transmembrane domains, designated claudins. The claudin family is supposedly composed of at least 24 members in mice and humans. Other types of integral membrane proteins with four transmembrane domains, namely occludin and tricellulin, as well as the single transmembrane proteins, JAMs (junctional adhesion molecules) and CAR (coxsackie and adenovirus receptor), are associated with TJ strands, and the high-level organization of TJ strands is likely to be established by membrane-anchored scaffolding proteins, such as ZO-1/2. Recent functional analyses of claudins in cell cultures and in mice have suggested that claudin-based TJs may have pivotal functions in the regulation of the epithelial microenvironment, which is critical for various biological functions such as control of cell proliferation. These represent the dawn of ‘Barriology’ (defined by Shoichiro Tsukita as the science of barriers in multicellular organisms). Taken together with recent reports regarding changes in claudin expression levels, understanding the regulation of the TJ-based microenvironment system will provide new insights into the regulation of polarization in the respect of epithelial microenvironment system and new viewpoints for developing anticancer strategies.
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Cites
JUNCTIONAL COMPLEXES IN VARIOUS EPITHELIA
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Occludin: a novel integral membrane protein localizing at tight junctions.
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Self-citationMultifunctional strands in tight junctions
Tsukita, S., Furuse, M., & Itoh, M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35067088 · Cited by 2,509
Self-citationSize-selective loosening of the blood-brain barrier in claudin-5–deficient mice
Nitta, T., Hata, M., Gotoh, S., Seo, Y., Sasaki, H., Hashimoto, N., Furuse, M., & Tsukita, S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302070 · Cited by 1,917
Self-citationAdherens and tight junctions: Structure, function and connections to the actin cytoskeleton
Hartsock, A., & Nelson, W. J. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.07.012 · Cited by 1,559
Claudin-based tight junctions are crucial for the mammalian epidermal barrier
Furuse, M., Hata, M., Furuse, K., Yoshida, Y., Haratake, A., Sugitani, Y., Noda, T., Kubo, A., & Tsukita, S. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110122 · Cited by 1,512
Self-citationComplex Phenotype of Mice Lacking Occludin, a Component of Tight Junction Strands
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Self-citationParacellin-1, a Renal Tight Junction Protein Required for Paracellular Mg 2+ Resorption
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CLAUDINS AND EPITHELIAL PARACELLULAR TRANSPORT
Van Itallie, C. M., & Anderson, J. M. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.68.040104.131404 · Cited by 1,131
Cited by
Physiology and function of the tight junction
Anderson, J. M., & Van Itallie, C. M. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a002584 · Cited by 1,059
Klaassen, I., Van Noorden, C. J. F., & Schlingemann, R. O. (2013) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2013.02.001 · Cited by 722
Epidermal barrier dysfunction and cutaneous sensitization in atopic diseases
Kubo, A., Nagao, K., & Amagai, M. (2012) · Journal of Clinical Investigation · doi:10.1172/jci57416 · Cited by 378
Regulation of blood-retinal barrier cell-junctions in diabetic retinopathy
Rudraraju, M., Narayanan, S. P., & Somanath, P. R. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105115 · Cited by 217
Luna, J. M., Barajas, J. M., Teng, K.-Y., Sun, H.-L., Moore, M. J., Rice, C. M., Darnell, R. B., & Ghoshal, K. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.025 · Cited by 80
Metadata
- Authors
- Tsukita, S., Yamazaki, Y., Katsuno, T., Tamura, A., & Tsukita, S.
- Venue
- Oncogene
- Published
- 2008-11-24
- Volume
- 27
- Issue
- 55
- Pages
- 6930-6938
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2037524252
- Cited by
- 375
- References
- 79
- FWCI
- 15.73
- Type
- journal article
- Language
- en
- Open access
- green
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