Occludin is a transmembrane protein that regulates the permeability of epithelial and endothelial barriers. It was first identified in epithelial cells as a 65 kDa integral plasma-membrane protein localized at the tight junctions.[5] Together with Claudins, and zonula occludens-1 (ZO-1), occludin has been considered a staple of tight junctions, and although it was shown to regulate the formation, maintenance, and function of tight junctions, its precise mechanism of action remained elusive and most of its actions were initially attributed to conformational changes following selective phosphorylation,[6] and its redox-sensitive dimerization.[7][8] However, mounting evidence demonstrated that occludin is not only present in epithelial/endothelial cells, but is also expressed in large quantities in cells that do not have tight junctions but have very active metabolism: pericytes,[9] neurons and astrocytes,[10] oligodendrocytes,[11] dendritic cells,[12] monocytes/macrophages[13] lymphocytes,[14] and myocardium.[15] Recent work, using molecular modeling, supported by biochemical and live-cell experiments in human cells demonstrated that occludin is a NADH oxidase that influences critical aspects of cell metabolism like glucose uptake, ATP production and gene expression.[16] Furthermore, manipulation of occludin content in human cells is capable of influencing the expression of glucose transporters,[16] and the activation of transcription factors like NFkB, and histone deacetylases like sirtuins, which proved capable of diminishing HIV replication rates in infected human macrophages under laboratory conditions.[9]
^ abcGRCm38: Ensembl release 89: ENSMUSG00000021638 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Furuse M, Hirase T, Itoh M, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S (December 1993). "Occludin: a novel integral membrane protein localizing at tight junctions". The Journal of Cell Biology. 123 (6 Pt 2): 1777–88. doi:10.1083/jcb.123.6.1777. PMC 2290891. PMID 8276896.
^Blasig IE, Bellmann C, Cording J, Del Vecchio G, Zwanziger D, Huber O, Haseloff RF (September 2011). "Occludin protein family: oxidative stress and reducing conditions". Antioxidants & Redox Signaling. 15 (5): 1195–219. doi:10.1089/ars.2010.3542. PMID 21235353.
^Walter JK, Castro V, Voss M, Gast K, Rueckert C, Piontek J, Blasig IE (November 2009). "Redox-sensitivity of the dimerization of occludin". Cellular and Molecular Life Sciences. 66 (22): 3655–62. doi:10.1007/s00018-009-0150-z. PMC 11115754. PMID 19756380. S2CID 23090886.
^Villela C, Manuel V (2011). "The interplay between occludin and ZO-1 is redox sensitive". doi:10.17169/refubium-12742. {{cite journal}}: Cite journal requires |journal= (help)
^ abCastro V, Bertrand L, Luethen M, Dabrowski S, Lombardi J, Morgan L, et al. (March 2016). "Occludin controls HIV transcription in brain pericytes via regulation of SIRT-1 activation". FASEB Journal. 30 (3): 1234–46. doi:10.1096/fj.15-277673. PMC 4750406. PMID 26601824.
^Bauer H, Stelzhammer W, Fuchs R, Weiger TM, Danninger C, Probst G, Krizbai IA (August 1999). "Astrocytes and neurons express the tight junction-specific protein occludin in vitro". Experimental Cell Research. 250 (2): 434–8. doi:10.1006/excr.1999.4558. PMID 10413597.
^Romanitan MO, Popescu BO, Winblad B, Bajenaru OA, Bogdanovic N (2007). "Occludin is overexpressed in Alzheimer's disease and vascular dementia". Journal of Cellular and Molecular Medicine. 11 (3): 569–79. doi:10.1111/j.1582-4934.2007.00047.x. PMC 3922362. PMID 17635647.
^Rescigno M, Rotta G, Valzasina B, Ricciardi-Castagnoli P (December 2001). "Dendritic cells shuttle microbes across gut epithelial monolayers". Immunobiology. 204 (5): 572–81. doi:10.1078/0171-2985-00094. PMID 11846220.
^Castro V, Bertrand L, Luethen M, Dabrowski S, Lombardi J, Morgan L, et al. (March 2016). "Occludin controls HIV transcription in brain pericytes via regulation of SIRT-1 activation". FASEB Journal. 30 (3): 1234–46. doi:10.1096/fj.15-277673. PMC 4750406. PMID 26601824.
^Alexander JS, Dayton T, Davis C, Hill S, Jackson TH, Blaschuk O, et al. (December 1998). "Activated T-lymphocytes express occludin, a component of tight junctions". Inflammation. 22 (6): 573–82. doi:10.1023/a:1022310429868. PMID 9824772. S2CID 23713562.
^Qiu L, Chen C, Ding G, Zhou Y, Zhang M (August 2011). "The effects of electromagnetic pulse on the protein levels of tight junction associated-proteins in the cerebral cortex, hippocampus, heart, lung, and testis of rats". Biomedical and Environmental Sciences. 24 (4): 438–44. Bibcode:2011BioES..24..438Q. doi:10.3967/0895-3988.2011.04.016. PMID 22108334.
^ abCastro V, Skowronska M, Lombardi J, He J, Seth N, Velichkovska M, Toborek M (February 2018). "Occludin regulates glucose uptake and ATP production in pericytes by influencing AMP-activated protein kinase activity". Journal of Cerebral Blood Flow and Metabolism. 38 (2): 317–332. doi:10.1177/0271678X17720816. PMC 5951017. PMID 28718701.
Occludin is a transmembrane protein that regulates the permeability of epithelial and endothelial barriers. It was first identified in epithelial cells...
transmembrane and cytoplasmic proteins. The three major transmembrane proteins are occludin, claudins, and junction adhesion molecule (JAM) proteins. These associate...
mutant occludin in epithelial cells leads to break down the barrier function of tight junction and changes in a migration of neutrophils. Occludin cooperates...
Claudins are a family of proteins which, along with occludin, are the most important components of the tight junctions (zonulae occludentes). Tight junctions...
initially anchored to neighboring cells by tight junction proteins such as occludin and cell adhesion molecules such as NCAM and N-Cadherin. Dorsally expressed...
mice were shown to have lower claudin-5 and occludin levels than the KO mice after TBI. Claudin and occludin are proteins that are essential for the formation...
targeting. Transmembrane proteins – including junctional adhesion molecule, occludin, and claudin. It is believed that claudin is the protein molecule responsible...
epithelial features, by stopping the expression of occludin, a tight junction protein. Loss of occludin causes a loss of the previous tight junction seals...
cell-surface molecules CD81, LDL receptor, SR-BI, DC-SIGN, Claudin-1, and Occludin. The envelope of HCV is similar to very low-density lipoproteins (VLDL)...
associated with this condition are Junctional adhesion molecule C (JAM3) and Occludin (OCLN).[citation needed] The most commonly affected region of the brain...
of kiwifruit (Actinidia deliciosa) cysteine protease actinidin on the occludin tight junction network in T84 intestinal epithelial cells". Food and Chemical...
permiability and the expression of tightly bound proteins - e-cadherin and occludin. Both of them increase the tight junctions between cells, strengthen the...
function. These complexes, formed primarily of members of the claudin and the occludin families, consist of about 35 different proteins, form a ring shaped continuous...
Tight junction is formed by transmembrane proteins, including claudins, occludins and tricellulins, that bind closely to each other on adjacent membranes...
2 has been shown to interact with tight junction protein 1, band 4.1, occludin and USP53. GRCh38: Ensembl release 89: ENSG00000119139 – Ensembl, May 2017...
or transection. PMP22 has shown association with zonula-occludens 1 and occludin, proteins that are involved in adhesion with other cells and the extracellular...
epithelium-mesenchyme transition: direct repression of the gene expression of claudins/occludin by Snail". Journal of Cell Science. 116 (Pt 10): 1959–67. doi:10.1242/jcs...
OCEL1, also called Occludin//ELL Domain Containing 1, is a protein encoding gene located at chromosome 19p13.11 in the human genome. Other aliases for...
II and several TJ proteins including ZO-1, ZO-2, ZO-3, paracingulin and occludin. Moreover, cingulin forms a complex with JAM-A, a tight junction membrane...
to normal endothelial cells, the cells lining the BBB are connected by occludin and claudin which form tight junctions in order to create a barrier to...
Global Information
