Regulation of claudins in blood-tissue barriers under physiological and pathological states

References

• Ehrlich P. Das sauerstufbudurfnis des organismus. Eine Farbenanalytische Studie. Berlin: Hirschwald 1885.
   Google Scholar
• Goldman EE. Vitalbarfung am Zentralnervensystem.: Preuss Akad Wiss, 1913.
   Google Scholar
• Cunha-Vaz JG, Maurice DM. The active transport of fluorescein by the retinal vessels and the retina. J Physiol 1967; 191:467 - 86; PMID: 4963870
   PubMed Web of Science ®Google Scholar
• Cunha Vaz JGFD. Permeability of the retinal vessels in health and disease. University of London (Institute of Ophthalmology), 1965.
   Google Scholar
• Cunha-Vaz J, Faria de Abreu JR, Campos AJ. Early breakdown of the blood-retinal barrier in diabetes. Br J Ophthalmol 1975; 59:649 - 56; http://dx.doi.org/10.1136/bjo.59.11.649; PMID: 1203221
   PubMed Web of Science ®Google Scholar
• Cunha-Vaz JG. The blood-retinal barriers. Doc Ophthalmol 1976; 41:287 - 327; http://dx.doi.org/10.1007/BF00146764; PMID: 1009819
   PubMed Web of Science ®Google Scholar
• Hori S, Ohtsuki S, Hosoya K, Nakashima E, Terasaki T. A pericyte-derived angiopoietin-1 multimeric complex induces occludin gene expression in brain capillary endothelial cells through Tie-2 activation in vitro. J Neurochem 2004; 89:503 - 13; http://dx.doi.org/10.1111/j.1471-4159.2004.02343.x; PMID: 15056293
   PubMed Web of Science ®Google Scholar
• Kim JH, Kim JH, Park JA, Lee SW, Kim WJ, Yu YS, et al. Blood-neural barrier: intercellular communication at glio-vascular interface. J Biochem Mol Biol 2006; 39:339 - 45; http://dx.doi.org/10.5483/BMBRep.2006.39.4.339; PMID: 16889675
   PubMedGoogle Scholar
• Sariola H, Saarma M. Novel functions and signalling pathways for GDNF. J Cell Sci 2003; 116:3855 - 62; http://dx.doi.org/10.1242/jcs.00786; PMID: 12953054
   PubMed Web of Science ®Google Scholar
• Anderson JM, Van Itallie CM, Fanning AS. Setting up a selective barrier at the apical junction complex. Curr Opin Cell Biol 2004; 16:140 - 5; http://dx.doi.org/10.1016/j.ceb.2004.01.005; PMID: 15196556
   PubMed Web of Science ®Google Scholar
• Balda MS, Matter K. Tight junctions. J Cell Sci 1998; 111:541 - 7; PMID: 9454728
   PubMed Web of Science ®Google Scholar
• Tsukita S, Furuse M, Itoh M. Multifunctional strands in tight junctions. Nat Rev Mol Cell Biol 2001; 2:285 - 93; http://dx.doi.org/10.1038/35067088; PMID: 11283726
   PubMed Web of Science ®Google Scholar
• Ikenouchi J, Furuse M, Furuse K, Sasaki H, Tsukita S, Tsukita S. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J Cell Biol 2005; 171:939 - 45; http://dx.doi.org/10.1083/jcb.200510043; PMID: 16365161
   PubMed Web of Science ®Google Scholar
• Chiba H, Osanai M, Murata M, Kojima T, Sawada N. Transmembrane proteins of tight junctions. Biochim Biophys Acta 2008; 1778:588 - 600; http://dx.doi.org/10.1016/j.bbamem.2007.08.017; PMID: 17916321
   PubMed Web of Science ®Google Scholar
• Bauer HC, Traweger A, Zweimueller-Mayer J, Lehner C, Tempfer H, Krizbai I, et al. New aspects of the molecular constituents of tissue barriers. J Neural Transm 2011; 118:7 - 21; http://dx.doi.org/10.1007/s00702-010-0484-6; PMID: 20865434
   PubMed Web of Science ®Google Scholar
• Mineta K, Yamamoto Y, Yamazaki Y, Tanaka H, Tada Y, Saito K, et al. Predicted expansion of the claudin multigene family. FEBS Lett 2011; 585:606 - 12; http://dx.doi.org/10.1016/j.febslet.2011.01.028; PMID: 21276448
   PubMed Web of Science ®Google Scholar
• Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol 1998; 141:1539 - 50; http://dx.doi.org/10.1083/jcb.141.7.1539; PMID: 9647647
   PubMed Web of Science ®Google Scholar
• Morita K, Sasaki H, Furuse M, Tsukita S. Endothelial claudin: claudin-5/TMVCF constitutes tight junction strands in endothelial cells. J Cell Biol 1999; 147:185 - 94; http://dx.doi.org/10.1083/jcb.147.1.185; PMID: 10508865
   PubMed Web of Science ®Google Scholar
• Tsukita S, Furuse M. Occludin and claudins in tight-junction strands: leading or supporting players?. Trends Cell Biol 1999; 9:268 - 73; http://dx.doi.org/10.1016/S0962-8924(99)01578-0; PMID: 10370242
   PubMed Web of Science ®Google Scholar
• Furuse M, Hata M, Furuse K, Yoshida Y, Haratake A, Sugitani Y, et al. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice. J Cell Biol 2002; 156:1099 - 111; http://dx.doi.org/10.1083/jcb.200110122; PMID: 11889141
   PubMed Web of Science ®Google Scholar
• Furuse M. Molecular basis of the core structure of tight junctions. Cold Spring Harb Perspect Biol 2010; 2:a002907; http://dx.doi.org/10.1101/cshperspect.a002907; PMID: 20182608
   PubMed Web of Science ®Google Scholar
• Farquhar MG, Palade GE. Junctional complexes in various epithelia. J Cell Biol 1963; 17:375 - 412; http://dx.doi.org/10.1083/jcb.17.2.375; PMID: 13944428
   PubMed Web of Science ®Google Scholar
• Staehelin LA, Mukherjee TM, Williams AW. Freeze-etch appearance of the tight junctions in the epithelium of small and large intestine of mice. Protoplasma 1969; 67:165 - 84; http://dx.doi.org/10.1007/BF01248737; PMID: 5346995
   PubMed Web of Science ®Google Scholar
• Krause G, Winkler L, Mueller SL, Haseloff RF, Piontek J, Blasig IE. Structure and function of claudins. Biochim Biophys Acta 2008; 1778:631 - 45; http://dx.doi.org/10.1016/j.bbamem.2007.10.018; PMID: 18036336
   PubMed Web of Science ®Google Scholar
• Lal-Nag M, Morin PJ. The claudins. Genome Biol 2009; 10:235; http://dx.doi.org/10.1186/gb-2009-10-8-235; PMID: 19706201
   PubMed Web of Science ®Google Scholar
• Schulzke JD, Günzel D, John LJ, Fromm M. Perspectives on tight junction research. Ann N Y Acad Sci 2012; 1257:1 - 19; http://dx.doi.org/10.1111/j.1749-6632.2012.06485.x; PMID: 22671584
   PubMed Web of Science ®Google Scholar
• Rüffer C, Gerke V. The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions. Eur J Cell Biol 2004; 83:135 - 44; http://dx.doi.org/10.1078/0171-9335-00366; PMID: 15260435
   PubMed Web of Science ®Google Scholar
• Arabzadeh A, Troy TC, Turksen K. Role of the Cldn6 cytoplasmic tail domain in membrane targeting and epidermal differentiation in vivo. Mol Cell Biol 2006; 26:5876 - 87; http://dx.doi.org/10.1128/MCB.02342-05; PMID: 16847338
   PubMed Web of Science ®Google Scholar
• Müller D, Kausalya PJ, Meij IC, Hunziker W. Familial hypomagnesemia with hypercalciuria and nephrocalcinosis: blocking endocytosis restores surface expression of a novel Claudin-16 mutant that lacks the entire C-terminal cytosolic tail. Hum Mol Genet 2006; 15:1049 - 58; http://dx.doi.org/10.1093/hmg/ddl020; PMID: 16501001
   PubMed Web of Science ®Google Scholar
• Ishizaki T, Chiba H, Kojima T, Fujibe M, Soma T, Miyajima H, et al. Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways. Exp Cell Res 2003; 290:275 - 88; http://dx.doi.org/10.1016/S0014-4827(03)00354-9; PMID: 14567987
   PubMed Web of Science ®Google Scholar
• Soma T, Chiba H, Kato-Mori Y, Wada T, Yamashita T, Kojima T, et al. Thr(207) of claudin-5 is involved in size-selective loosening of the endothelial barrier by cyclic AMP. Exp Cell Res 2004; 300:202 - 12; http://dx.doi.org/10.1016/j.yexcr.2004.07.012; PMID: 15383327
   PubMed Web of Science ®Google Scholar
• Persidsky Y, Heilman D, Haorah J, Zelivyanskaya M, Persidsky R, Weber GA, et al. Rho-mediated regulation of tight junctions during monocyte migration across the blood-brain barrier in HIV-1 encephalitis (HIVE). Blood 2006; 107:4770 - 80; http://dx.doi.org/10.1182/blood-2005-11-4721; PMID: 16478881
   PubMed Web of Science ®Google Scholar
• Fujibe M, Chiba H, Kojima T, Soma T, Wada T, Yamashita T, et al. Thr203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions. Exp Cell Res 2004; 295:36 - 47; http://dx.doi.org/10.1016/j.yexcr.2003.12.014; PMID: 15051488
   PubMed Web of Science ®Google Scholar
• Tanaka M, Kamata R, Sakai R. EphA2 phosphorylates the cytoplasmic tail of Claudin-4 and mediates paracellular permeability. J Biol Chem 2005; 280:42375 - 82; http://dx.doi.org/10.1074/jbc.M503786200; PMID: 16236711
   PubMed Web of Science ®Google Scholar
• D’Souza T, Agarwal R, Morin PJ. Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells. J Biol Chem 2005; 280:26233 - 40; http://dx.doi.org/10.1074/jbc.M502003200; PMID: 15905176
   PubMed Web of Science ®Google Scholar
• Van Itallie CM, Gambling TM, Carson JL, Anderson JM. Palmitoylation of claudins is required for efficient tight-junction localization. J Cell Sci 2005; 118:1427 - 36; http://dx.doi.org/10.1242/jcs.01735; PMID: 15769849
   PubMed Web of Science ®Google Scholar
• Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol 1999; 147:1351 - 63; http://dx.doi.org/10.1083/jcb.147.6.1351; PMID: 10601346
   PubMed Web of Science ®Google Scholar
• Roh MH, Liu CJ, Laurinec S, Margolis B. The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions. J Biol Chem 2002; 277:27501 - 9; http://dx.doi.org/10.1074/jbc.M201177200; PMID: 12021270
   PubMed Web of Science ®Google Scholar
• Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S. Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. J Biol Chem 2002; 277:455 - 61; http://dx.doi.org/10.1074/jbc.M109005200; PMID: 11689568
   PubMed Web of Science ®Google Scholar
• Colegio OR, Van Itallie CM, McCrea HJ, Rahner C, Anderson JM. Claudins create charge-selective channels in the paracellular pathway between epithelial cells. Am J Physiol Cell Physiol 2002; 283:C142 - 7; PMID: 12055082
   PubMed Web of Science ®Google Scholar
• Hou J, Paul DL, Goodenough DA. Paracellin-1 and the modulation of ion selectivity of tight junctions. J Cell Sci 2005; 118:5109 - 18; http://dx.doi.org/10.1242/jcs.02631; PMID: 16234325
   PubMed Web of Science ®Google Scholar
• Alexandre MD, Jeansonne BG, Renegar RH, Tatum R, Chen YH. The first extracellular domain of claudin-7 affects paracellular Cl- permeability. Biochem Biophys Res Commun 2007; 357:87 - 91; http://dx.doi.org/10.1016/j.bbrc.2007.03.078; PMID: 17400193
   PubMed Web of Science ®Google Scholar
• Evans MJ, von Hahn T, Tscherne DM, Syder AJ, Panis M, Wölk B, et al. Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry. Nature 2007; 446:801 - 5; http://dx.doi.org/10.1038/nature05654; PMID: 17325668
   PubMed Web of Science ®Google Scholar
• Zheng A, Yuan F, Li Y, Zhu F, Hou P, Li J, et al. Claudin-6 and claudin-9 function as additional coreceptors for hepatitis C virus. J Virol 2007; 81:12465 - 71; http://dx.doi.org/10.1128/JVI.01457-07; PMID: 17804490
   PubMed Web of Science ®Google Scholar
• Piontek J, Winkler L, Wolburg H, Müller SL, Zuleger N, Piehl C, et al. Formation of tight junction: determinants of homophilic interaction between classic claudins. FASEB J 2008; 22:146 - 58; http://dx.doi.org/10.1096/fj.07-8319com; PMID: 17761522
   PubMed Web of Science ®Google Scholar
• Fujita K, Katahira J, Horiguchi Y, Sonoda N, Furuse M, Tsukita S. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein. FEBS Lett 2000; 476:258 - 61; http://dx.doi.org/10.1016/S0014-5793(00)01744-0; PMID: 10913624
   PubMed Web of Science ®Google Scholar
• Katahira J, Sugiyama H, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N. Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo. J Biol Chem 1997; 272:26652 - 8; http://dx.doi.org/10.1074/jbc.272.42.26652; PMID: 9334247
   PubMed Web of Science ®Google Scholar
• Piontek J, Fritzsche S, Cording J, Richter S, Hartwig J, Walter M, et al. Elucidating the principles of the molecular organization of heteropolymeric tight junction strands. Cell Mol Life Sci 2011; 68:3903 - 18; http://dx.doi.org/10.1007/s00018-011-0680-z; PMID: 21533891
   PubMed Web of Science ®Google Scholar
• Furuse M, Sasaki H, Tsukita S. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J Cell Biol 1999; 147:891 - 903; http://dx.doi.org/10.1083/jcb.147.4.891; PMID: 10562289
   PubMed Web of Science ®Google Scholar
• Daugherty BL, Ward C, Smith T, Ritzenthaler JD, Koval M. Regulation of heterotypic claudin compatibility. J Biol Chem 2007; 282:30005 - 13; http://dx.doi.org/10.1074/jbc.M703547200; PMID: 17699514
   PubMed Web of Science ®Google Scholar
• Mitic LL, Unger VM, Anderson JM. Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4. Protein Sci 2003; 12:218 - 27; http://dx.doi.org/10.1110/ps.0233903; PMID: 12538885
   PubMed Web of Science ®Google Scholar
• Coyne CB, Gambling TM, Boucher RC, Carson JL, Johnson LG. Role of claudin interactions in airway tight junctional permeability. Am J Physiol Lung Cell Mol Physiol 2003; 285:L1166 - 78; PMID: 12909588
   PubMed Web of Science ®Google Scholar
• Van Itallie CM, Mitic LL, Anderson JM. Claudin-2 forms homodimers and is a component of a high molecular weight protein complex. J Biol Chem 2011; 286:3442 - 50; http://dx.doi.org/10.1074/jbc.M110.195578; PMID: 21098027
   PubMed Web of Science ®Google Scholar
• Blasig IE, Winkler L, Lassowski B, Mueller SL, Zuleger N, Krause E, et al. On the self-association potential of transmembrane tight junction proteins. Cell Mol Life Sci 2006; 63:505 - 14; http://dx.doi.org/10.1007/s00018-005-5472-x; PMID: 16456617
   PubMed Web of Science ®Google Scholar
• Hou J, Renigunta A, Yang J, Waldegger S. Claudin-4 forms paracellular chloride channel in the kidney and requires claudin-8 for tight junction localization. Proc Natl Acad Sci U S A 2010; 107:18010 - 5; http://dx.doi.org/10.1073/pnas.1009399107; PMID: 20921420
   PubMed Web of Science ®Google Scholar
• Hou J, Renigunta A, Gomes AS, Hou M, Paul DL, Waldegger S, et al. Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium. Proc Natl Acad Sci U S A 2009; 106:15350 - 5; http://dx.doi.org/10.1073/pnas.0907724106; PMID: 19706394
   PubMed Web of Science ®Google Scholar
• Ohtsuki S, Yamaguchi H, Katsukura Y, Asashima T, Terasaki T. mRNA expression levels of tight junction protein genes in mouse brain capillary endothelial cells highly purified by magnetic cell sorting. J Neurochem 2008; 104:147 - 54; PMID: 17971126
   PubMed Web of Science ®Google Scholar
• Amasheh S, Meiri N, Gitter AH, Schöneberg T, Mankertz J, Schulzke JD, et al. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J Cell Sci 2002; 115:4969 - 76; http://dx.doi.org/10.1242/jcs.00165; PMID: 12432083
   PubMed Web of Science ®Google Scholar
• Krug SM, Günzel D, Conrad MP, Rosenthal R, Fromm A, Amasheh S, et al. Claudin-17 forms tight junction channels with distinct anion selectivity. Cell Mol Life Sci 2012; 69:2765 - 78; http://dx.doi.org/10.1007/s00018-012-0949-x; PMID: 22402829
   PubMed Web of Science ®Google Scholar
• Rosenthal R, Milatz S, Krug SM, Oelrich B, Schulzke JD, Amasheh S, et al. Claudin-2, a component of the tight junction, forms a paracellular water channel. J Cell Sci 2010; 123:1913 - 21; http://dx.doi.org/10.1242/jcs.060665; PMID: 20460438
   PubMed Web of Science ®Google Scholar
• Günzel D, Stuiver M, Kausalya PJ, Haisch L, Krug SM, Rosenthal R, et al. Claudin-10 exists in six alternatively spliced isoforms that exhibit distinct localization and function. J Cell Sci 2009; 122:1507 - 17; http://dx.doi.org/10.1242/jcs.040113; PMID: 19383724
   PubMed Web of Science ®Google Scholar
• Hadj-Rabia S, Baala L, Vabres P, Hamel-Teillac D, Jacquemin E, Fabre M, et al. Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: a tight junction disease. Gastroenterology 2004; 127:1386 - 90; http://dx.doi.org/10.1053/j.gastro.2004.07.022; PMID: 15521008
   PubMed Web of Science ®Google Scholar
• Nitta T, Hata M, Gotoh S, Seo Y, Sasaki H, Hashimoto N, et al. Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice. J Cell Biol 2003; 161:653 - 60; http://dx.doi.org/10.1083/jcb.200302070; PMID: 12743111
   PubMed Web of Science ®Google Scholar
• Gow A, Southwood CM, Li JS, Pariali M, Riordan GP, Brodie SE, et al. CNS myelin and sertoli cell tight junction strands are absent in Osp/claudin-11 null mice. Cell 1999; 99:649 - 59; http://dx.doi.org/10.1016/S0092-8674(00)81553-6; PMID: 10612400
   PubMed Web of Science ®Google Scholar
• Ben-Yosef T, Belyantseva IA, Saunders TL, Hughes ED, Kawamoto K, Van Itallie CM, et al. Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration. Hum Mol Genet 2003; 12:2049 - 61; http://dx.doi.org/10.1093/hmg/ddg210; PMID: 12913076
   PubMed Web of Science ®Google Scholar
• Weber S, Schneider L, Peters M, Misselwitz J, Rönnefarth G, Böswald M, et al. Novel paracellin-1 mutations in 25 families with familial hypomagnesemia with hypercalciuria and nephrocalcinosis. J Am Soc Nephrol 2001; 12:1872 - 81; PMID: 11518780
   PubMed Web of Science ®Google Scholar
• Müller D, Kausalya PJ, Claverie-Martin F, Meij IC, Eggert P, Garcia-Nieto V, et al. A novel claudin 16 mutation associated with childhood hypercalciuria abolishes binding to ZO-1 and results in lysosomal mistargeting. Am J Hum Genet 2003; 73:1293 - 301; http://dx.doi.org/10.1086/380418; PMID: 14628289
   PubMed Web of Science ®Google Scholar
• Konrad M, Schaller A, Seelow D, Pandey AV, Waldegger S, Lesslauer A, et al. Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement. Am J Hum Genet 2006; 79:949 - 57; http://dx.doi.org/10.1086/508617; PMID: 17033971
   PubMed Web of Science ®Google Scholar
• Abbott NJ, Patabendige AA, Dolman DE, Yusof SR, Begley DJ. Structure and function of the blood-brain barrier. Neurobiol Dis 2010; 37:13 - 25; http://dx.doi.org/10.1016/j.nbd.2009.07.030; PMID: 19664713
   PubMed Web of Science ®Google Scholar
• Butt AM, Jones HC, Abbott NJ. Electrical resistance across the blood-brain barrier in anaesthetized rats: a developmental study. J Physiol 1990; 429:47 - 62; PMID: 2277354
   PubMed Web of Science ®Google Scholar
• Crone C, Christensen O. Electrical resistance of a capillary endothelium. J Gen Physiol 1981; 77:349 - 71; http://dx.doi.org/10.1085/jgp.77.4.349; PMID: 7241087
   PubMed Web of Science ®Google Scholar
• Liebner S, Fischmann A, Rascher G, Duffner F, Grote EH, Kalbacher H, et al. Claudin-1 and claudin-5 expression and tight junction morphology are altered in blood vessels of human glioblastoma multiforme. Acta Neuropathol 2000; 100:323 - 31; http://dx.doi.org/10.1007/s004010000180; PMID: 10965803
   PubMed Web of Science ®Google Scholar
• Wolburg H, Wolburg-Buchholz K, Kraus J, Rascher-Eggstein G, Liebner S, Hamm S, et al. Localization of claudin-3 in tight junctions of the blood-brain barrier is selectively lost during experimental autoimmune encephalomyelitis and human glioblastoma multiforme. Acta Neuropathol 2003; 105:586 - 92; PMID: 12734665
   PubMed Web of Science ®Google Scholar
• Ohtsuki S, Sato S, Yamaguchi H, Kamoi M, Asashima T, Terasaki T. Exogenous expression of claudin-5 induces barrier properties in cultured rat brain capillary endothelial cells. J Cell Physiol 2007; 210:81 - 6; http://dx.doi.org/10.1002/jcp.20823; PMID: 16998798
   PubMed Web of Science ®Google Scholar
• Wolburg H, Wolburg-Buchholz K, Liebner S, Engelhardt B. Claudin-1, claudin-2 and claudin-11 are present in tight junctions of choroid plexus epithelium of the mouse. Neurosci Lett 2001; 307:77 - 80; http://dx.doi.org/10.1016/S0304-3940(01)01927-9; PMID: 11427304
   PubMed Web of Science ®Google Scholar
• Kratzer I, Vasiljevic A, Rey C, Fevre-Montange M, Saunders N, Strazielle N, et al. Complexity and developmental changes in the expression pattern of claudins at the blood-CSF barrier. Histochem Cell Biol 2012; 138:861 - 79; http://dx.doi.org/10.1007/s00418-012-1001-9; PMID: 22886143
   PubMed Web of Science ®Google Scholar
• Luo Y, Xiao W, Zhu X, Mao Y, Liu X, Chen X, et al. Differential expression of claudins in retinas during normal development and the angiogenesis of oxygen-induced retinopathy. Invest Ophthalmol Vis Sci 2011; 52:7556 - 64; http://dx.doi.org/10.1167/iovs.11-7185; PMID: 21862644
   PubMed Web of Science ®Google Scholar
• Morcos Y, Hosie MJ, Bauer HC, Chan-Ling T. Immunolocalization of occludin and claudin-1 to tight junctions in intact CNS vessels of mammalian retina. J Neurocytol 2001; 30:107 - 23; http://dx.doi.org/10.1023/A:1011982906125; PMID: 11577249
   PubMedGoogle Scholar
• Klaassen I, Hughes JM, Vogels IM, Schalkwijk CG, Van Noorden CJ, Schlingemann RO. Altered expression of genes related to blood-retina barrier disruption in streptozotocin-induced diabetes. Exp Eye Res 2009; 89:4 - 15; http://dx.doi.org/10.1016/j.exer.2009.01.006; PMID: 19284967
   PubMed Web of Science ®Google Scholar
• Rahner C, Fukuhara M, Peng S, Kojima S, Rizzolo LJ. The apical and basal environments of the retinal pigment epithelium regulate the maturation of tight junctions during development. J Cell Sci 2004; 117:3307 - 18; http://dx.doi.org/10.1242/jcs.01181; PMID: 15226402
   PubMed Web of Science ®Google Scholar
• Rizzolo LJ, Chen X, Weitzman M, Sun R, Zhang H. Analysis of the RPE transcriptome reveals dynamic changes during the development of the outer blood-retinal barrier. Mol Vis 2007; 13:1259 - 73; PMID: 17679949
   PubMed Web of Science ®Google Scholar
• Sun R, Peng S, Chen X, Zhang H, Rizzolo LJ. Diffusible retinal secretions regulate the expression of tight junctions and other diverse functions of the retinal pigment epithelium. Mol Vis 2008; 14:2237 - 62; PMID: 19057659
   PubMed Web of Science ®Google Scholar
• Peng S, Rao VS, Adelman RA, Rizzolo LJ. Claudin-19 and the barrier properties of the human retinal pigment epithelium. Invest Ophthalmol Vis Sci 2011; 52:1392 - 403; http://dx.doi.org/10.1167/iovs.10-5984; PMID: 21071746
   PubMed Web of Science ®Google Scholar
• Peng S, Adelman RA, Rizzolo LJ. Minimal effects of VEGF and anti-VEGF drugs on the permeability or selectivity of RPE tight junctions. Invest Ophthalmol Vis Sci 2010; 51:3216 - 25; http://dx.doi.org/10.1167/iovs.09-4162; PMID: 20042644
   PubMed Web of Science ®Google Scholar
• Strunnikova NV, Maminishkis A, Barb JJ, Wang F, Zhi C, Sergeev Y, et al. Transcriptome analysis and molecular signature of human retinal pigment epithelium. Hum Mol Genet 2010; 19:2468 - 86; http://dx.doi.org/10.1093/hmg/ddq129; PMID: 20360305
   PubMed Web of Science ®Google Scholar
• Kröll S, El-Gindi J, Thanabalasundaram G, Panpumthong P, Schrot S, Hartmann C, et al. Control of the blood-brain barrier by glucocorticoids and the cells of the neurovascular unit. Ann N Y Acad Sci 2009; 1165:228 - 39; http://dx.doi.org/10.1111/j.1749-6632.2009.04040.x; PMID: 19538311
   PubMed Web of Science ®Google Scholar
• Ronaldson PT, Demarco KM, Sanchez-Covarrubias L, Solinsky CM, Davis TP. Transforming growth factor-beta signaling alters substrate permeability and tight junction protein expression at the blood-brain barrier during inflammatory pain. J Cereb Blood Flow Metab 2009; 29:1084 - 98; http://dx.doi.org/10.1038/jcbfm.2009.32; PMID: 19319146
   PubMed Web of Science ®Google Scholar
• Argaw AT, Gurfein BT, Zhang Y, Zameer A, John GR. VEGF-mediated disruption of endothelial CLN-5 promotes blood-brain barrier breakdown. Proc Natl Acad Sci U S A 2009; 106:1977 - 82; http://dx.doi.org/10.1073/pnas.0808698106; PMID: 19174516
   PubMed Web of Science ®Google Scholar
• Carvey PM, Hendey B, Monahan AJ. The blood-brain barrier in neurodegenerative disease: a rhetorical perspective. J Neurochem 2009; 111:291 - 314; http://dx.doi.org/10.1111/j.1471-4159.2009.06319.x; PMID: 19659460
   PubMed Web of Science ®Google Scholar
• Coisne C, Engelhardt B. Tight junctions in brain barriers during central nervous system inflammation. Antioxid Redox Signal 2011; 15:1285 - 303; http://dx.doi.org/10.1089/ars.2011.3929; PMID: 21338320
   PubMed Web of Science ®Google Scholar
• Grammas P, Martinez J, Miller B. Cerebral microvascular endothelium and the pathogenesis of neurodegenerative diseases. Expert Rev Mol Med 2011; 13:e19; http://dx.doi.org/10.1017/S1462399411001918; PMID: 21676288
   PubMed Web of Science ®Google Scholar
• Hawkins BT, Davis TP. The blood-brain barrier/neurovascular unit in health and disease. Pharmacol Rev 2005; 57:173 - 85; http://dx.doi.org/10.1124/pr.57.2.4; PMID: 15914466
   PubMed Web of Science ®Google Scholar
• Petty MA, Lo EH. Junctional complexes of the blood-brain barrier: permeability changes in neuroinflammation. Prog Neurobiol 2002; 68:311 - 23; http://dx.doi.org/10.1016/S0301-0082(02)00128-4; PMID: 12531232
   PubMed Web of Science ®Google Scholar
• Leal EC, Manivannan A, Hosoya K, Terasaki T, Cunha-Vaz J, Ambrósio AF, et al. Inducible nitric oxide synthase isoform is a key mediator of leukostasis and blood-retinal barrier breakdown in diabetic retinopathy. Invest Ophthalmol Vis Sci 2007; 48:5257 - 65; http://dx.doi.org/10.1167/iovs.07-0112; PMID: 17962481
   PubMed Web of Science ®Google Scholar
• Trudeau K, Roy S, Guo W, Hernández C, Villarroel M, Simó R, et al. Fenofibric acid reduces fibronectin and collagen type IV overexpression in human retinal pigment epithelial cells grown in conditions mimicking the diabetic milieu: functional implications in retinal permeability. Invest Ophthalmol Vis Sci 2011; 52:6348 - 54; http://dx.doi.org/10.1167/iovs.11-7282; PMID: 21715349
   PubMed Web of Science ®Google Scholar
• Nabeshima T, Nitta A. Memory impairment and neuronal dysfunction induced by beta-amyloid protein in rats. Tohoku J Exp Med 1994; 174:241 - 9; http://dx.doi.org/10.1620/tjem.174.241; PMID: 7761989
   PubMed Web of Science ®Google Scholar
• Thal DR, Griffin WS, Braak H. Parenchymal and vascular Abeta-deposition and its effects on the degeneration of neurons and cognition in Alzheimer’s disease. J Cell Mol Med 2008; 12:5B 1848 - 62; http://dx.doi.org/10.1111/j.1582-4934.2008.00411.x; PMID: 18624777
   PubMed Web of Science ®Google Scholar
• Marco S, Skaper SD. Amyloid beta-peptide1-42 alters tight junction protein distribution and expression in brain microvessel endothelial cells. Neurosci Lett 2006; 401:219 - 24; http://dx.doi.org/10.1016/j.neulet.2006.03.047; PMID: 16644119
   PubMed Web of Science ®Google Scholar
• Kook SY, Hong HS, Moon M, Ha CM, Chang S, Mook-Jung I. Aβ₁₋₄₂-RAGE interaction disrupts tight junctions of the blood-brain barrier via Ca²⁺-calcineurin signaling. J Neurosci 2012; 32:8845 - 54; http://dx.doi.org/10.1523/JNEUROSCI.6102-11.2012; PMID: 22745485
   PubMed Web of Science ®Google Scholar
• Starr JM, Farrall AJ, Armitage P, McGurn B, Wardlaw J. Blood-brain barrier permeability in Alzheimer’s disease: a case-control MRI study. Psychiatry Res 2009; 171:232 - 41; http://dx.doi.org/10.1016/j.pscychresns.2008.04.003; PMID: 19211227
   PubMed Web of Science ®Google Scholar
• Ujiie M, Dickstein DL, Carlow DA, Jefferies WA. Blood-brain barrier permeability precedes senile plaque formation in an Alzheimer disease model. Microcirculation 2003; 10:463 - 70; PMID: 14745459
   PubMed Web of Science ®Google Scholar
• Viggars AP, Wharton SB, Simpson JE, Matthews FE, Brayne C, Savva GM, et al. Alterations in the blood brain barrier in ageing cerebral cortex in relationship to Alzheimer-type pathology: a study in the MRC-CFAS population neuropathology cohort. Neurosci Lett 2011; 505:25 - 30; http://dx.doi.org/10.1016/j.neulet.2011.09.049; PMID: 21970975
   PubMed Web of Science ®Google Scholar
• Krizbai IA, Bauer H, Bresgen N, Eckl PM, Farkas A, Szatmári E, et al. Effect of oxidative stress on the junctional proteins of cultured cerebral endothelial cells. Cell Mol Neurobiol 2005; 25:129 - 39; http://dx.doi.org/10.1007/s10571-004-1378-7; PMID: 15962510
   PubMed Web of Science ®Google Scholar
• Nunomura A, Castellani RJ, Zhu X, Moreira PI, Perry G, Smith MA. Involvement of oxidative stress in Alzheimer disease. J Neuropathol Exp Neurol 2006; 65:631 - 41; http://dx.doi.org/10.1097/01.jnen.0000228136.58062.bf; PMID: 16825950
   PubMed Web of Science ®Google Scholar
• Nunomura A, Hofer T, Moreira PI, Castellani RJ, Smith MA, Perry G. RNA oxidation in Alzheimer disease and related neurodegenerative disorders. Acta Neuropathol 2009; 118:151 - 66; http://dx.doi.org/10.1007/s00401-009-0508-1; PMID: 19271225
   PubMed Web of Science ®Google Scholar
• Nunomura A, Perry G, Aliev G, Hirai K, Takeda A, Balraj EK, et al. Oxidative damage is the earliest event in Alzheimer disease. J Neuropathol Exp Neurol 2001; 60:759 - 67; PMID: 11487050
   PubMed Web of Science ®Google Scholar
• Simpson JE, Ince PG, Lace G, Forster G, Shaw PJ, Matthews F, et al, MRC Cognitive Function and Ageing Neuropathology Study Group. Astrocyte phenotype in relation to Alzheimer-type pathology in the ageing brain. Neurobiol Aging 2010; 31:578 - 90; http://dx.doi.org/10.1016/j.neurobiolaging.2008.05.015; PMID: 18586353
   PubMed Web of Science ®Google Scholar
• Romanitan MO, Popescu BO, Spulber S, Băjenaru O, Popescu LM, Winblad B, et al. Altered expression of claudin family proteins in Alzheimer’s disease and vascular dementia brains. J Cell Mol Med 2010; 14:1088 - 100; PMID: 20041969
   PubMed Web of Science ®Google Scholar
• Romanitan MO, Popescu BO, Winblad B, Bajenaru OA, Bogdanovic N. Occludin is overexpressed in Alzheimer’s disease and vascular dementia. J Cell Mol Med 2007; 11:569 - 79; http://dx.doi.org/10.1111/j.1582-4934.2007.00047.x; PMID: 17635647
   PubMed Web of Science ®Google Scholar
• Furuse M, Furuse K, Sasaki H, Tsukita S. Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol 2001; 153:263 - 72; http://dx.doi.org/10.1083/jcb.153.2.263; PMID: 11309408
   PubMed Web of Science ®Google Scholar
• Furuse M, Tsukita S. Claudins in occluding junctions of humans and flies. Trends Cell Biol 2006; 16:181 - 8; http://dx.doi.org/10.1016/j.tcb.2006.02.006; PMID: 16537104
   PubMed Web of Science ®Google Scholar
• Lassmann H, Brück W, Lucchinetti C. Heterogeneity of multiple sclerosis pathogenesis: implications for diagnosis and therapy. Trends Mol Med 2001; 7:115 - 21; http://dx.doi.org/10.1016/S1471-4914(00)01909-2; PMID: 11286782
   PubMed Web of Science ®Google Scholar
• Couraud PO. Infiltration of inflammatory cells through brain endothelium. Pathol Biol (Paris) 1998; 46:176 - 80; PMID: 9769913
   PubMed Web of Science ®Google Scholar
• Errede M, Girolamo F, Ferrara G, Strippoli M, Morando S, Boldrin V, et al. Blood-brain barrier alterations in the cerebral cortex in experimental autoimmune encephalomyelitis. J Neuropathol Exp Neurol 2012; 71:840 - 54; http://dx.doi.org/10.1097/NEN.0b013e31826ac110; PMID: 23001217
   PubMed Web of Science ®Google Scholar
• Förster C, Kahles T, Kietz S, Drenckhahn D. Dexamethasone induces the expression of metalloproteinase inhibitor TIMP-1 in the murine cerebral vascular endothelial cell line cEND. J Physiol 2007; 580:937 - 49; http://dx.doi.org/10.1113/jphysiol.2007.129007; PMID: 17317742
   PubMed Web of Science ®Google Scholar
• Engelhardt B. Molecular mechanisms involved in T cell migration across the blood-brain barrier. J Neural Transm 2006; 113:477 - 85; http://dx.doi.org/10.1007/s00702-005-0409-y; PMID: 16550326
   PubMed Web of Science ®Google Scholar
• Yednock TA, Cannon C, Fritz LC, Sanchez-Madrid F, Steinman L, Karin N. Prevention of experimental autoimmune encephalomyelitis by antibodies against alpha 4 beta 1 integrin. Nature 1992; 356:63 - 6; http://dx.doi.org/10.1038/356063a0; PMID: 1538783
   PubMed Web of Science ®Google Scholar
• Minagar A, Alexander JS. Blood-brain barrier disruption in multiple sclerosis. Mult Scler 2003; 9:540 - 9; http://dx.doi.org/10.1191/1352458503ms965oa; PMID: 14664465
   PubMed Web of Science ®Google Scholar
• Szczuciński A, Losy J. Chemokines and chemokine receptors in multiple sclerosis. Potential targets for new therapies. Acta Neurol Scand 2007; 115:137 - 46; http://dx.doi.org/10.1111/j.1600-0404.2006.00749.x; PMID: 17295707
   PubMed Web of Science ®Google Scholar
• Körner H, Sedgwick JD. Tumour necrosis factor and lymphotoxin: molecular aspects and role in tissue-specific autoimmunity. Immunol Cell Biol 1996; 74:465 - 72; http://dx.doi.org/10.1038/icb.1996.77; PMID: 8912010
   PubMed Web of Science ®Google Scholar
• Beck J, Rondot P, Catinot L, Falcoff E, Kirchner H, Wietzerbin J. Increased production of interferon gamma and tumor necrosis factor precedes clinical manifestation in multiple sclerosis: do cytokines trigger off exacerbations?. Acta Neurol Scand 1988; 78:318 - 23; http://dx.doi.org/10.1111/j.1600-0404.1988.tb03663.x; PMID: 3146861
   PubMed Web of Science ®Google Scholar
• Sharief MK, Hentges R. Association between tumor necrosis factor-alpha and disease progression in patients with multiple sclerosis. N Engl J Med 1991; 325:467 - 72; http://dx.doi.org/10.1056/NEJM199108153250704; PMID: 1852181
   PubMed Web of Science ®Google Scholar
• Hofman FM, Hinton DR, Johnson K, Merrill JE. Tumor necrosis factor identified in multiple sclerosis brain. J Exp Med 1989; 170:607 - 12; http://dx.doi.org/10.1084/jem.170.2.607; PMID: 2754393
   PubMed Web of Science ®Google Scholar
• Wang C, Wang C, Dong H, Wu XM, Wang C, Xia F, et al. Immune-related GTPase Irgm1 exacerbates experimental auto-immune encephalomyelitis by promoting the disruption of blood-brain barrier and blood-cerebrospinal fluid barrier. Mol Immunol 2013; 53:43 - 51; http://dx.doi.org/10.1016/j.molimm.2012.06.009; PMID: 22796503
   PubMed Web of Science ®Google Scholar
• Blecharz KG, Haghikia A, Stasiolek M, Kruse N, Drenckhahn D, Gold R, et al. Glucocorticoid effects on endothelial barrier function in the murine brain endothelial cell line cEND incubated with sera from patients with multiple sclerosis. Mult Scler 2010; 16:293 - 302; http://dx.doi.org/10.1177/1352458509358189; PMID: 20203147
   PubMed Web of Science ®Google Scholar
• The Diabetes Control and Complications Trial Research Group. The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus. N Engl J Med 1993; 329:977 - 86; http://dx.doi.org/10.1056/NEJM199309303291401; PMID: 8366922
   PubMed Web of Science ®Google Scholar
• Fernandes R, Gonçalves A, Cunha-Vaz J. Blood–Retinal Barrier: The Fundamentals. In: Thassu D, Chader G, eds. Ocular Drug Delivery Systems: Barriers and Application of Nanoparticulate Systems: CRC Press, 2012:111-32.
   Google Scholar
• Antonetti DA, Barber AJ, Hollinger LA, Wolpert EB, Gardner TW. 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 1999; 274:23463 - 7; http://dx.doi.org/10.1074/jbc.274.33.23463; PMID: 10438525
   PubMed Web of Science ®Google Scholar
• Antonetti DA, Barber AJ, Khin S, Lieth E, Tarbell JM, Gardner TW, Penn State Retina Research Group. Vascular permeability in experimental diabetes is associated with reduced endothelial occludin content: vascular endothelial growth factor decreases occludin in retinal endothelial cells. Diabetes 1998; 47:1953 - 9; http://dx.doi.org/10.2337/diabetes.47.12.1953; PMID: 9836530
   PubMed Web of Science ®Google Scholar
• Barber AJ, Antonetti DA. Mapping the blood vessels with paracellular permeability in the retinas of diabetic rats. Invest Ophthalmol Vis Sci 2003; 44:5410 - 6; http://dx.doi.org/10.1167/iovs.03-0244; PMID: 14638745
   PubMed Web of Science ®Google Scholar
• Barber AJ, Antonetti DA, Gardner TW, The Penn State Retina Research Group. Altered expression of retinal occludin and glial fibrillary acidic protein in experimental diabetes. Invest Ophthalmol Vis Sci 2000; 41:3561 - 8; PMID: 11006253
   PubMed Web of Science ®Google Scholar
• Gonçalves A, Leal E, Paiva A, Teixeira Lemos E, Teixeira F, Ribeiro CF, et al. Protective effects of the dipeptidyl peptidase IV inhibitor sitagliptin in the blood-retinal barrier in a type 2 diabetes animal model. Diabetes Obes Metab 2012; 14:454 - 63; http://dx.doi.org/10.1111/j.1463-1326.2011.01548.x; PMID: 22151893
   PubMed Web of Science ®Google Scholar
• Kowluru RA, Odenbach S. Role of interleukin-1beta in the pathogenesis of diabetic retinopathy. Br J Ophthalmol 2004; 88:1343 - 7; http://dx.doi.org/10.1136/bjo.2003.038133; PMID: 15377563
   PubMed Web of Science ®Google Scholar
• Joussen AM, Murata T, Tsujikawa A, Kirchhof B, Bursell SE, Adamis AP. Leukocyte-mediated endothelial cell injury and death in the diabetic retina. Am J Pathol 2001; 158:147 - 52; http://dx.doi.org/10.1016/S0002-9440(10)63952-1; PMID: 11141487
   PubMed Web of Science ®Google Scholar
• Joussen AM, Poulaki V, Mitsiades N, Kirchhof B, Koizumi K, Döhmen S, et al. Nonsteroidal anti-inflammatory drugs prevent early diabetic retinopathy via TNF-alpha suppression. FASEB J 2002; 16:438 - 40; PMID: 11821258
   PubMed Web of Science ®Google Scholar
• Leal EC, Martins J, Voabil P, Liberal J, Chiavaroli C, Bauer J, et al. Calcium dobesilate inhibits the alterations in tight junction proteins and leukocyte adhesion to retinal endothelial cells induced by diabetes. Diabetes 2010; 59:2637 - 45; http://dx.doi.org/10.2337/db09-1421; PMID: 20627932
   PubMed Web of Science ®Google Scholar
• Bucolo C, Ward KW, Mazzon E, Cuzzocrea S, Drago F. Protective effects of a coumarin derivative in diabetic rats. Invest Ophthalmol Vis Sci 2009; 50:3846 - 52; http://dx.doi.org/10.1167/iovs.08-3328; PMID: 19279317
   PubMed Web of Science ®Google Scholar
• Deissler H, Deissler H, Lang S, Lang GE. VEGF-induced effects on proliferation, migration and tight junctions are restored by ranibizumab (Lucentis) in microvascular retinal endothelial cells. Br J Ophthalmol 2008; 92:839 - 43; http://dx.doi.org/10.1136/bjo.2007.135640; PMID: 18511543
   PubMed Web of Science ®Google Scholar
• Murakami T, Felinski EA, Antonetti DA. Occludin phosphorylation and ubiquitination regulate tight junction trafficking and vascular endothelial growth factor-induced permeability. J Biol Chem 2009; 284:21036 - 46; http://dx.doi.org/10.1074/jbc.M109.016766; PMID: 19478092
   PubMed Web of Science ®Google Scholar
• Adachi T, Yasuda H, Nakamura S, Kamiya T, Hara H, Hara H, et al. Endoplasmic reticulum stress induces retinal endothelial permeability of extracellular-superoxide dismutase. Free Radic Res 2011; 45:1083 - 92; http://dx.doi.org/10.3109/10715762.2011.595408; PMID: 21736484
   PubMed Web of Science ®Google Scholar
• Yoshikawa T, Ogata N, Izuta H, Shimazawa M, Hara H, Takahashi K. Increased expression of tight junctions in ARPE-19 cells under endoplasmic reticulum stress. Curr Eye Res 2011; 36:1153 - 63; http://dx.doi.org/10.3109/02713683.2011.606592; PMID: 21978097
   PubMed Web of Science ®Google Scholar
• Darlow BA, Hutchinson JL, Henderson-Smart DJ, Donoghue DA, Simpson JM, Evans NJ, Australian and New Zealand Neonatal Network. Prenatal risk factors for severe retinopathy of prematurity among very preterm infants of the Australian and New Zealand Neonatal Network. Pediatrics 2005; 115:990 - 6; http://dx.doi.org/10.1542/peds.2004-1309; PMID: 15805375
   PubMed Web of Science ®Google Scholar
• Hartnett ME, Penn JS. Mechanisms and management of retinopathy of prematurity. N Engl J Med 2012; 367:2515 - 26; http://dx.doi.org/10.1056/NEJMra1208129; PMID: 23268666
   PubMed Web of Science ®Google Scholar
• Smith LE, Wesolowski E, McLellan A, Kostyk SK, D’Amato R, Sullivan R, et al. Oxygen-induced retinopathy in the mouse. Invest Ophthalmol Vis Sci 1994; 35:101 - 11; PMID: 7507904
   PubMed Web of Science ®Google Scholar
• Zhang S, Leske DA, Holmes JM. Neovascularization grading methods in a rat model of retinopathy of prematurity. Invest Ophthalmol Vis Sci 2000; 41:887 - 91; PMID: 10711709
   PubMed Web of Science ®Google Scholar
• Abe T, Sugano E, Saigo Y, Tamai M. Interleukin-1beta and barrier function of retinal pigment epithelial cells (ARPE-19): aberrant expression of junctional complex molecules. Invest Ophthalmol Vis Sci 2003; 44:4097 - 104; http://dx.doi.org/10.1167/iovs.02-0867; PMID: 12939333
   PubMed Web of Science ®Google Scholar
• Luo Y, Zhuo Y, Fukuhara M, Rizzolo LJ. Effects of culture conditions on heterogeneity and the apical junctional complex of the ARPE-19 cell line. Invest Ophthalmol Vis Sci 2006; 47:3644 - 55; http://dx.doi.org/10.1167/iovs.06-0166; PMID: 16877439
   PubMed Web of Science ®Google Scholar
• Maminishkis A, Chen S, Jalickee S, Banzon T, Shi G, Wang FE, et al. Confluent monolayers of cultured human fetal retinal pigment epithelium exhibit morphology and physiology of native tissue. Invest Ophthalmol Vis Sci 2006; 47:3612 - 24; http://dx.doi.org/10.1167/iovs.05-1622; PMID: 16877436
   PubMed Web of Science ®Google Scholar
• Shi G, Maminishkis A, Banzon T, Jalickee S, Li R, Hammer J, et al. Control of chemokine gradients by the retinal pigment epithelium. Invest Ophthalmol Vis Sci 2008; 49:4620 - 30; http://dx.doi.org/10.1167/iovs.08-1816; PMID: 18450597
   PubMed Web of Science ®Google Scholar
• Li R, Maminishkis A, Banzon T, Wan Q, Jalickee S, Chen S, et al. IFNgamma regulates retinal pigment epithelial fluid transport. Am J Physiol Cell Physiol 2009; 297:C1452 - 65; http://dx.doi.org/10.1152/ajpcell.00255.2009; PMID: 19794146
   PubMedGoogle Scholar
• Peng S, Gan G, Rao VS, Adelman RA, Rizzolo LJ. Effects of proinflammatory cytokines on the claudin-19 rich tight junctions of human retinal pigment epithelium. Invest Ophthalmol Vis Sci 2012; 53:5016 - 28; http://dx.doi.org/10.1167/iovs.11-8311; PMID: 22761260
   PubMed Web of Science ®Google Scholar
• Lippoldt A, Liebner S, Andbjer B, Kalbacher H, Wolburg H, Haller H, et al. Organization of choroid plexus epithelial and endothelial cell tight junctions and regulation of claudin-1, -2 and -5 expression by protein kinase C. Neuroreport 2000; 11:1427 - 31; http://dx.doi.org/10.1097/00001756-200005150-00015; PMID: 10841351
   PubMed Web of Science ®Google Scholar