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Occludin: One Protein, Many Forms

Pages 242-250 | Published online: 20 Mar 2023

REFERENCES

  • Aijaz S, Balda MS, Matter K. 2006. Tight junctions: molecular architecture and function. Int. Rev. Cytol. 248:261–298.
  • Alexander JS, Elrod JW. 2002. Extracellular matrix, junctional integrity and matrix metalloproteinase interactions in endothelial permeability regulation. J. Anat. 200:561–574.
  • Ando-Akatsuka Y, et al. 1996. Interspecies diversity of the occludin sequence: cDNA cloning of human, mouse, dog, and rat-kangaroo homologues. J. Cell Biol. 133:43–47.
  • András IE, et al. 2007. The NMDA and AMPA/KA receptors are involved in glutamate-induced alterations of occludin expression and phosphorylation in brain endothelial cells. J. Cereb. Blood Flow Metab. 27:1431–1443.
  • Andreeva AY, Krause E, Müller EC, Blasig IE, Utepbergenov DI. 2001. Protein kinase C regulates the phosphorylation and cellular localization of occludin. J. Biol. Chem. 276:38480–38486.
  • Antonetti DA, Barber AJ, Hollinger LA, Wolpert EB, Gardner TW. 1999. Vascular endothelial growth factor induces rapid phosphorylation of tight junction proteins occludin and zonula occluden 1. A potential mechanism for vascular permeability in diabetic retinopathy and tumors. J. Biol. Chem. 274:23463–23467.
  • Asaka M, Hirase T, Hashimoto-Komatsu A, Node K. 2011. Rab5a-mediated localization of claudin-1 is regulated by proteasomes in endothelial cells. Am. J. Physiol. Cell Physiol. 300:C87–C96.
  • Balda MS, Flores-Maldonado C, Cereijido M, Matter K. 2000. Multiple domains of occludin are involved in the regulation of paracellular permeability. J. Cell. Biochem. 78:85–96.
  • Balda MS, Anderson JM. 1993. Two classes of tight junctions are revealed by ZO-1 isoforms. Am. J. Physiol. 264:C918–C924.
  • Balda MS, Matter K. 2009. Tight junctions and the regulation of gene expression. Biochim. Biophys. Acta 1788:761–767.
  • Basuroy S, Seth A, Elias B, Naren AP, Rao R. 2006. MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide. Biochem. J. 393:69–77.
  • Basuroy S, Sheth P, Mansbach CM, Rao RK. 2005. Acetaldehyde disrupts tight junctions and adherens junctions in human colonic mucosa: protection by EGF and L-glutamine. Am. J. Physiol. Gastrointest. Liver Physiol. 289:G367–G375.
  • Bauer AT, Bürgers HF, Rabie T, Marti HH. 2010. Matrix metalloproteinase-9 mediates hypoxia-induced vascular leakage in the brain via tight junction rearrangement. J. Cereb. Blood Flow Metab. 30:837–848.
  • Beauchesne E, Desjardins P, Hazell AS, Butterworth RF. 2009. Altered expression of tight junction proteins and matrix metalloproteinases in thiamine-deficient mouse brain. Neurochem. Int. 55:275–281.
  • Blecharz KG, et al. 2010. Glucocorticoid effects on endothelial barrier function in the murine brain endothelial cell line cEND incubated with sera from patients with multiple sclerosis. Mult. Scler. 16:293–302.
  • Caron A, Desrosiers RR, Langlois S, Béliveau R. 2005. Ischemia-reperfusion injury stimulates gelatinase expression and activity in kidney glomeruli. Can. J. Physiol. Pharmacol. 83:287–300.
  • Casas E, et al. 2010. Cholesterol efflux stimulates metalloproteinase-mediated cleavage of occludin and release of extracellular membrane particles containing its C-terminal fragments. Exp. Cell Res. 316:353–365.
  • Castro V, et al. 2010. The membrane recruitment of ZO-1 and its interplay with occludin is redox sensitive and relies on the disulfide bridge-mediated homodimerization of occludin, abstr P-5. Abstr. 13th Int. Symp. Signal Transduction Blood-Brain. University Hospital, Zurich, Switzerland.
  • Chen F, Ohashi N, Li W, Eckman C, Nguyen JH. 2009. Disruptions of occludin and claudin-5 in brain endothelial cells in vitro and in brains of mice with acute liver failure. Hepatology 50:1914–1923.
  • Chen W, et al. 2009. Matrix metalloproteinases inhibition provides neuroprotection against hypoxia-ischemia in the developing brain. J. Neurochem. 111:726–736.
  • Chen Y, Merzdorf C, Paul DL, Goodenough DA. 1997. COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos. J. Cell Biol. 138:891–899.
  • Chen YH, Lu Q, Goodenough DA, Jeansonne B. 2002. Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells. Mol. Biol. Cell 13:1227–1237.
  • Chen YS, et al. 2007. Propofol-induced vascular permeability change is related to the nitric oxide signaling pathway and occludin phosphorylation. J. Biomed. Sci. 14:629–636.
  • Chun J, Prince A. 2009. TLR2-induced calpain cleavage of epithelial junctional proteins facilitates leukocyte transmigration. Cell Host Microbe 5:47–58.
  • Coëffier M, et al. 2010. Increased proteasome-mediated degradation of occludin in irritable bowel syndrome. Am. J. Gastroenterol. 105:1181–1188.
  • Collins NT, et al. 2006. Cyclic strain-mediated regulation of vascular endothelial occludin and ZO-1: influence on intercellular tight junction assembly and function. Arterioscler. Thromb. Vasc. Biol. 26:62–68.
  • Cordenonsi M, et al. 1997. Occludin dephosphorylation in early development of Xenopus laevis. J. Cell Sci. 110:3131–3139.
  • Cordenonsi M, et al. 1999. Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin. Eur. J. Biochem. 264:374–384.
  • DeMaio L, et al. 2006. Oxidized phospholipids mediate occludin expression and phosphorylation in vascular endothelial cells. Am. J. Physiol. Heart Circ. Physiol. 290:H674–H683.
  • DeMaio L, Chang YS, Gardner TW, Tarbell JM, Antonetti DA. 2001. Shear stress regulates occludin content and phosphorylation. Am. J. Physiol. Heart Circ. Physiol. 281:H105–H113.
  • Dörfel MJ, Westphal JK, Huber O. 2009. Differential phosphorylation of occludin and tricellulin by CK2 and CK1. Ann. N. Y. Acad. Sci. 1165:69–73.
  • Du D, et al. 2010. The tight junction protein, occludin, regulates the directional migration of epithelial cells. Dev. Cell 18:52–63.
  • Elias BC, et al. 2009. Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions. J. Biol. Chem. 284:1559–1569.
  • Farquhar MG, Palade GE. 1963. Junctional complexes in various epithelia. J. Cell Biol. 17:375–412.
  • Farshori P, Kachar B. 1999. Redistribution and phosphorylation of occludin during opening and resealing of tight junctions in cultured epithelial cells. J. Membr. Biol. 170:147–156.
  • Feldman GJ, Mullin JM, Ryan MP. 2005. Occludin: structure, function and regulation. Adv. Drug Deliv. Rev. 57:883–917.
  • Feng S, et al. 2011. Matrix metalloproteinase-2 and -9 secreted by leukemic cells increase the permeability of blood-brain barrier by disrupting tight junction proteins. PLoS One 6:e20599.
  • Förster C. 2008. Tight junctions and the modulation of barrier function in disease. Histochem. Cell Biol. 130:55–70.
  • Furuse M, Sasaki H, Fujimoto K, Tsukita S. 1998. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143:391–401.
  • Furuse M, et al. 1994. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127:1617–1626.
  • Furuse M, et al. 1993. Occludin: a novel integral membrane protein localizing at tight junctions. J. Cell Biol. 123:1777–1788.
  • Ghassemifar MR, et al. 2002. Occludin TM4(−): an isoform of the tight junction protein present in primates lacking the fourth trans-membrane domain. J. Cell Sci. 115:3171–3180.
  • Ghassemifar MR, et al. 2003. Gene expression regulating epithelial intercellular junction biogenesis during human blastocyst development in vitro. Mol. Hum. Reprod. 9:245–252.
  • Giebel SJ, Menicucci G, McGuire PG, Das A. 2005. Matrix metalloproteinases in early diabetic retinopathy and their role in alteration of the blood-retinal barrier. Lab Invest. 85:597–607.
  • Gorodeski GI. 2007. Estrogen decrease in tight junctional resistance involves matrix-metalloproteinase-7-mediated remodeling of occludin. Endocrinology 148:218–231.
  • Gu JM, Lim SO, Park YM, Jung G. 2008. A novel splice variant of occludin deleted in exon 9 and its role in cell apoptosis and invasion. FEBS J. 275:3145–3156.
  • Gurney KJ, Estrada EY, Rosenberg GA. 2006. Blood-brain barrier disruption by stromelysin-1 facilitates neutrophil infiltration in neuroinflammation. Neurobiol. Dis. 23:87–96.
  • Han M, et al. 2010. Ascorbate protects endothelial barrier function during septic insult: role of protein phosphatase type 2A. Free Radic. Biol. Med. 48:128–135.
  • Harhaj NS, et al. 2006. VEGF activation of protein kinase C stimulates occludin phosphorylation and contributes to endothelial permeability. Invest. Ophthalmol. Vis. Sci. 47:5106–5115.
  • Hawkins BT, Lundeen TF, Norwood KM, Brooks HL, Egleton RD. 2007. Increased blood-brain barrier permeability and altered tight junctions in experimental diabetes in the rat: contribution of hyperglycaemia and matrix metalloproteinases. Diabetologia 50:202–211.
  • Higashida T, et al. 2011. The role of hypoxia-inducible factor-1alpha, aquaporin-4, and matrix metalloproteinase-9 in blood-brain barrier disruption and brain edema after traumatic brain injury. J. Neurosurg. 114:92–101.
  • Hirase T, et al. 2001. Regulation of tight junction permeability and occludin phosphorylation by Rhoa-p160ROCK-dependent and -independent mechanisms. J. Biol. Chem. 276:10423–10431.
  • Huang W, Eum SY, András IE, Hennig B, Toborek M. 2009. PPARalpha and PPARgamma attenuate HIV-induced dysregulation of tight junction proteins by modulations of matrix metalloproteinase and proteasome activities. FASEB J. 23:1596–1606.
  • Ichikawa Y, et al. 2006. Matrilysin (MMP-7) degrades VE-cadherin and accelerates accumulation of beta-catenin in the nucleus of human umbilical vein endothelial cells. Oncol. Rep. 15:311–315.
  • Ishihara H, et al. 2008. Endothelial cell barrier impairment induced by glioblastomas and transforming growth factor beta2 involves matrix metalloproteinases and tight junction proteins. J. Neuropathol. Exp. Neurol. 67:435–448.
  • Kago T, et al. 2006. Cerebral ischemia enhances tyrosine phosphorylation of occludin in brain capillaries. Biochem. Biophys. Res. Commun. 339:1197–1203.
  • Kale G, Naren AP, Sheth P, Rao RK. 2003. Tyrosine phosphorylation of occludin attenuates its interactions with ZO-1, ZO-2, and ZO-3. Biochem. Biophys. Res. Commun. 302:324–329.
  • Kawedia JD, et al. 2008. The protein kinase A pathway contributes to Hg2+-induced alterations in phosphorylation and subcellular distribution of occludin associated with increased tight junction permeability of salivary epithelial cell monolayers. J. Pharmacol. Exp. Ther. 326:829–837.
  • Kurihara H, Anderson JM, Farquhar MG. 1992. Diversity among tight junctions in rat kidney: glomerular slit diaphragms and endothelial junctions express only one isoform of the tight junction protein ZO-1. Proc. Natl. Acad. Sci. U. S. A. 89:7075–7079.
  • Kuwabara H, et al. 2001. Occludin regulates actin cytoskeleton in endothelial cells. Cell Struct. Funct. 26:109–116.
  • Lacaz-Vieira F, Jaeger MM, Farshori P, Kachar B. 1999. Small synthetic peptides homologous to segments of the first external loop of occludin impair tight junction resealing. J. Membr. Biol. 168:289–297.
  • Li W, et al. 2010. Adaptive cerebral neovascularization in a model of type 2 diabetes: relevance to focal cerebral ischemia. Diabetes 59:228–235.
  • Li Y, Fanning AS, Anderson JM, Lavie A. 2005. Structure of the conserved cytoplasmic C-terminal domain of occludin: identification of the ZO-1 binding surface. J. Mol. Biol. 352:151–164.
  • Lischper M, Beuck S, Thanabalasundaram G, Pieper C, Galla HJ. 2010. Metalloproteinase mediated occludin cleavage in the cerebral microcapillary endothelium under pathological conditions. Brain Res. 1326:114–127.
  • Liu W, Hendren J, Qin XJ, Shen J, Liu KJ. 2009. Normobaric hyperoxia attenuates early blood-brain barrier disruption by inhibiting MMP-9-mediated occludin degradation in focal cerebral ischemia. J. Neurochem. 108:811–820.
  • Lohmann C, Krischke M, Wegener J, Galla HJ. 2004. Tyrosine phosphatase inhibition induces loss of blood-brain barrier integrity by matrix metalloproteinase-dependent and -independent pathways. Brain Res. 995:184–196.
  • Louboutin JP, Agrawal L, Reyes BA, Van Bockstaele EJ, Strayer DS. 2010. HIV-1 gp120-induced injury to the blood-brain barrier: role of metalloproteinases 2 and 9 and relationship to oxidative stress. J. Neuropathol. Exp. Neurol. 69:801–816.
  • Lui WY, Lee WM. 2005. cAMP perturbs inter-Sertoli tight junction permeability barrier in vitro via its effect on proteasome-sensitive ubiquitination of occludin. J. Cell. Physiol. 203:564–572.
  • Lynch RD, et al. 2007. Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin. Exp. Cell Res. 313:2597–2610.
  • Mankertz J, et al. 2002. Gene expression of the tight junction protein occludin includes differential splicing and alternative promoter usage. Biochem. Biophys. Res. Commun. 298:657–666.
  • Martin TA, Mansel RE, Jiang WG. 2010. Loss of occludin leads to the progression of human breast cancer. Int. J. Mol. Med. 26:723–734.
  • Martínez-Contreras R, Galindo JM, Aguilar-Rojas A, Valdés J. 2003. Two exonic elements in the flanking constitutive exons control the alternative splicing of the alpha exon of the ZO-1 pre-mRNA. Biochim. Biophys. Acta 1630:71–83.
  • Matter K, Aijaz S, Tsapara S, Balda MS. 2005. Mammalian tight junctions in the regulation of epithelial differentiation and proliferation. Curr. Opin. Cell Biol. 17:453–458.
  • McCaffrey G, et al. 2008. Occludin oligomeric assembly at tight junctions of the blood-brain barrier is disrupted by peripheral inflammatory hyperalgesia. J. Neurochem. 106:2395–2409.
  • McCarthy KM, et al. 1996. Occludin is a functional component of the tight junction. J. Cell Sci. 109:2287–2298.
  • McKenzie JA, Riento K, Ridley AJ. 2006. Casein kinase I epsilon associates with and phosphorylates the tight junction protein occludin. FEBS Lett. 580:2388–2394.
  • Morgan L, et al. 2007. Inflammation and dephosphorylation of the tight junction protein occludin in an experimental model of multiple sclerosis. Neuroscience 147:664–673.
  • Murakami T, Felinski EA, Antonetti DA. 2009. Occludin phosphorylation and ubiquitination regulate tight junction trafficking and vascular endothelial growth factor-induced permeability. J. Biol. Chem. 284:21036–21046.
  • Muresan Z, Paul DL, Goodenough DA. 2000. Occludin 1B, a variant of the tight jnction protein occludin. Mol. Cell. Biol. 11:627–634.
  • Navaratna D, McGuire PG, Menicucci G, Das A. 2007. Proteolytic degradation of VE-cadherin alters the blood-retinal barrier in diabetes. Diabetes 56:2380–2387.
  • Nunbhakdi-Craig V, et al. 2002. Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex. J. Cell Biol. 158:967–978.
  • Ohtake K, et al. 2003. Poly-l-arginine enhances paracellular permeability via serine/threonine phosphorylation of ZO-1 and tyrosine dephosphorylation of occludin in rabbit nasal epithelium. Pharm. Res. 20:1838–1845.
  • Olivera D, Knall C, Boggs S, Seagrave J. 2010. Cytoskeletal modulation and tyrosine phosphorylation of tight junction proteins are associated with mainstream cigarette smoke-induced permeability of airway epithelium. Exp. Toxicol. Pathol. 62:133–143.
  • Osanai M, et al. 2006. Epigenetic silencing of occludin promotes tumorigenic and metastatic properties of cancer cells via modulations of unique sets of apoptosis-associated genes. Cancer Res. 66:9125–9133.
  • Pang Z, Antonetti DA, Tarbell JM. 2005. Shear stress regulates HUVEC hydraulic conductivity by occludin phosphorylation. Ann. Biomed. Eng. 33:1536–1545.
  • Pelletier RM, Okawara Y, Vitale ML, Anderson JM. 1997. Differential distribution of the tight-junction-associated protein ZO-1 isoforms alpha+ and alpha− in guinea pig Sertoli cells: a possible association with F-actin and G-actin. Biol. Reprod. 57:367–376.
  • Raikwar NS, Vandewalle A, Thomas CP. 2010. Nedd4-2 interacts with occludin to inhibit tight junction formation and enhance paracellular conductance in collecting duct epithelia. Am. J. Physiol. Renal Physiol. 299:F436–F444.
  • Rajasekaran SA, et al. 2007. Na-K-ATPase regulates tight junction permeability through occludin phosphorylation in pancreatic epithelial cells. Am. J. Physiol. Gastrointest. Liver Physiol. 292:G124–133.
  • Raleigh DR, et al. 2010. Tight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functions. Mol. Biol. Cell 21:1200–1213.
  • Rao R. 2009. Occludin phosphorylation in regulation of epithelial tight junctions. Ann. N. Y. Acad. Sci. 1165:62–68.
  • Rao RK, Basuroy S, Rao VU, Karnaky KJJr, Gupta A. 2002. Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress. Biochem. J. 368:471–481.
  • Reijerkerk A, et al. 2006. Diapedesis of monocytes is associated with MMP-mediated occludin disappearance in brain endothelial cells. FASEB J. 20:2550–2552.
  • Rosenberg GA, Yang Y. 2007. Vasogenic edema due to tight junction disruption by matrix metalloproteinases in cerebral ischemia. Neurosurg. Focus 22:E4.
  • Runswick S, Mitchell T, Davies P, Robinson C, Garrod DR. 2007. Pollen proteolytic enzymes degrade tight junctions. Respirology 12:834–842.
  • Saitou M, et al. 2000. Complex phenotype of mice lacking occludin, a component of tight junction strands. Mol. Biol. Cell 11:4131–4142.
  • Saitou M, et al. 1997. Mammalian occludin in epithelial cells: its expression and subcellular distribution. Eur. J. Cell Biol. 73:222–231.
  • Sakakibara A, Furuse M, Saitou M, Ando-Akatsuka Y, Tsukita S. 1997. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 137:1393–1401.
  • Sallee JL, Burridge K. 2009. Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J. Biol. Chem. 284:14997–15006.
  • Salomons FA, Acs K, Dantuma NP. 2010. Illuminating the ubiquitin/proteasome system. Exp. Cell Res. 316:1289–1295.
  • Schubert-Unkmeir A, et al. 2010. Neisseria meningitidis induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role for MMP-8. PLoS Pathog. 6:e1000874.
  • Seth A, Sheth P, Elias BC, Rao R. 2007. Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer. J. Biol. Chem. 282:11487–11498.
  • Sheth B, et al. 1997. Tight junction assembly during mouse blastocyst formation is regulated by late expression of ZO-1 alpha+ isoform. Development 124:2027–2037.
  • Sheth P, Basuroy S, Li C, Naren AP, Rao RK. 2003. Role of phosphatidylinositol 3-kinase in oxidative stress-induced disruption of tight junctions. J. Biol. Chem. 278:49239–49245.
  • Simonovic I, Rosenberg J, Koutsouris A, Hecht G. 2000. Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions. Cell. Microbiol. 2:305–315.
  • Smales C, et al. 2003. Occludin phosphorylation: identification of an occludin kinase in brain and cell extracts as CK2. FEBS Lett. 545:161–166.
  • Steed E, Balda MS, Matter K. 2010. Dynamics and functions of tight junctions. Trends Cell Biol. 20:142–149.
  • Steed E, Rodrigues NT, Balda MS, Matter K. 2009. Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family. BMC Cell. Biol. 10:95.
  • Sumitomo T, et al. 2011. Streptolysin S contributes to group A streptococcal translocation across an epithelial barrier. J. Biol. Chem. 286:2750–2761.
  • Sundstrom JM, et al. 2009. Identification and analysis of occludin phosphosites: a combined mass spectrometry and bioinformatics approach. J. Proteome Res. 8:808–817.
  • Suzuki T, et al. 2009. PKC eta regulates occludin phosphorylation and epithelial tight junction integrity. Proc. Natl. Acad. Sci. U. S. A. 106:61–66.
  • Tada Y, et al. 2010. Reduction of endothelial tight junction proteins is related to cerebral aneurysm formation in rats. J. Hypertens. 28:1883–1891.
  • Takahashi S, et al. 2009. The E3 ubiquitin ligase LNX1p80 promotes the removal of claudins from tight junctions in MDCK cells. J. Cell Sci. 122:985–994.
  • Takenaga Y, Takagi N, Murotomi K, Tanonaka K, Takeo S. 2009. Inhibition of Src activity decreases tyrosine phosphorylation of occludin in brain capillaries and attenuates increase in permeability of the blood-brain barrier after transient focal cerebral ischemia. J. Cereb. Blood Flow Metab. 29:1099–1108.
  • Tang C, Xue H, Bai C, Fu R, Wu A. 2010. The effects of Tanshinone IIA on blood-brain barrier and brain edema after transient middle cerebral artery occlusion in rats. Phytomedicine 17:1145–1149.
  • Thanabalasundaram G, Pieper C, Lischper M, Galla HJ. 2010. Regulation of the blood-brain barrier integrity by pericytes via matrix metalloproteinases mediated activation of vascular endothelial growth factor in vitro. Brain Res. 1347:1–10.
  • Traweger A, et al. 2002. The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch. J. Biol. Chem. 277:10201–10208.
  • Tsukamoto T, Nigam SK. 1999. Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins. Am. J. Physiol. 276:F737–F750.
  • Verma S, Kumar M, Gurjav U, Lum S, Nerurkar VR. 2010. Reversal of West Nile virus-induced blood-brain barrier disruption and tight junction proteins degradation by matrix metalloproteinases inhibitor. Virology 397:130–138.
  • Vikström E, Bui L, Konradsson P, Magnusson KE. 2009. The junctional integrity of epithelial cells is modulated by Pseudomonas aeruginosa quorum sensing molecule through phosphorylation-dependent mechanisms. Exp. Cell Res. 315:313–326.
  • Wachtel M, et al. 1999. Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition. J. Cell Sci. 112:4347–4356.
  • Walsh TG, et al. 2011. Stabilization of brain microvascular endothelial barrier function by shear stress involves VE-cadherin signaling leading to modulation of pTyr-occludin levels. J. Cell. Physiol. 226:3053–3063
  • Walter JK, et al. 2009. The oligomerization of the coiled coil-domain of occludin is redox sensitive. Ann. N. Y. Acad. Sci. 1165:19–27.
  • Walter JK, et al. 2009. Redox-sensitivity of the dimerization of occludin. Cell. Mol. Life Sci. 66:3655–3662.
  • Wan H, et al. 2000. Quantitative structural and biochemical analyses of tight junction dynamics following exposure of epithelial cells to house dust mite allergen Der p 1. Clin. Exp. Allergy 30:685–698.
  • Willott E, Balda MS, Heintzelman M, Jameson B, Anderson JM. 1992. Localization and differential expression of two isoforms of the tight junction protein ZO-1. Am. J. Physiol. 262:C1119–C1124.
  • Wong V, Gumbiner BM. 1997. A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J. Cell Biol. 136:399–409.
  • Yamamoto M, et al. 2008. Phosphorylation of claudin-5 and occludin by rho kinase in brain endothelial cells. Am. J. Pathol. 172:521–533.
  • Yang Y, Estrada EY, Thompson JF, Liu W, Rosenberg GA. 2007. Matrix metalloproteinase-mediated disruption of tight junction proteins in cerebral vessels is reversed by synthetic matrix metalloproteinase inhibitor in focal ischemia in rat. J. Cereb. Blood Flow Metab. 27:697–709.
  • Zeiller C, et al. 2009. Phospholipase D2 regulates endothelial permeability through cytoskeleton reorganization and occludin downregulation. Biochim. Biophys. Acta 1793:1236–1249.
  • Zhu L, Li X, Zeng R, Gorodeski GI. 2006. Changes in tight junctional resistance of the cervical epithelium are associated with modulation of content and phosphorylation of occludin 65-kilodalton and 50-kilodalton forms. Endocrinology 147:977–989.

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