Journal articles: 'Claudin-11'

1

Sedwick, Caitlin. "Claudin 11 stops the leaks." Journal of Cell Biology 183, no. 5 (December 1, 2008): 752. http://dx.doi.org/10.1083/jcb.1835iti1.

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Kaitu’u-Lino, Tu’uhevaha J., Pavel Sluka, Caroline F. H. Foo, and Peter G. Stanton. "Claudin-11 expression and localisation is regulated by androgens in rat Sertoli cells in vitro." Reproduction 133, no. 6 (June 2007): 1169–79. http://dx.doi.org/10.1530/rep-06-0385.

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Claudin-11 and occludin are protein components in tight junctions (TJs) between Sertoli cells which are important for the maintenance of the blood–testis barrier. Barrier formation occurs during puberty, with evidence suggesting hormonal regulation of both claudin-11 and occludin. This study aimed to investigate the regulation of claudin-11 and occludin mRNA expression by testosterone (T) and FSH and their immunolocalisation at rat Sertoli cell TJsin vitro, and to correlate any steroid regulation with the functional capacity of TJs. Sertoli cells formed functional TJs within 3 days as assessed by transepithelial electrical resistance (TER). Both T and dihydrotestosterone significantly (P< 0.01) increased TER twofold and claudin-11 mRNA two- to threefold within 3 days. FSH partially stimulated TER and claudin-11 mRNA, but estradiol had no effect. T also promoted claudin-11 localisation into extensive intercellular contacts. In contrast to claudin-11, Tand FSH did not change occludin mRNA expression, however, T promoted localisation of occludin at cell contacts in a similar manner to claudin-11. Addition of flutamide to T-stimulated cells caused a twofold decrease in both TER and claudin-11 mRNA expression, and resulted in the loss of both proteins from cell contacts. This effect was reversible following flutamide removal. It is concluded that androgens i) co-regulate claudin-11 mRNA expression and TER, implicating claudin-11 in TJ formation and ii) promote the localisation of claudin-11 and occludin at Sertoli cell contacts. Hence, the ability of androgens to maintain spermatogenesisin vivois partly via their effects on TJ proteins and regulation of the blood–testis barrier.

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Horné, Fabian, Raimund Dietze, Eniko Berkes, Frank Oehmke, Hans-Rudolf Tinneberg, Ivo Meinhold-Heerlein, and Lutz Konrad. "Impaired Localization of Claudin-11 in Endometriotic Epithelial Cells Compared to Endometrial Cells." Reproductive Sciences 26, no. 9 (December 4, 2018): 1181–92. http://dx.doi.org/10.1177/1933719118811643.

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Claudins are the major components of tight junctions and are often deregulated in human cancer, permitting escape of cancer cells along with the acquisition of invasive properties. Similarly, endometrial cells also show invasive capabilities; however, the role of tight junctions in endometriosis has only rarely been examined. In this study, we analyzed the protein expression and localization of claudin-7 and claudin-11 in human eutopic and ectopic endometrium and endometrial cell lines. We identified claudin-7 primarily at the basolateral junctions of the glandular epithelial cells in eutopic endometrium as well as in the ectopic lesions in nearly all glands and cysts. Quantification of claudin-7 localization by HSCORE showed a slight increase in peritoneal and deep infiltrating endometriosis (DIE) compared to eutopic endometrium. In contrast, claudin-11 was localized mainly in the apicolateral junctions in nearly all glandular epithelial cells of the eutopic endometrium. Interestingly, we observed a deregulation of claudin-11 localization to a basal or basolateral localization in ovarian ( P < .001), peritoneal ( P < .01), and DIE ( P < .05) and a moderately decreased abundance in ovarian endometriosis. In endometrial cell lines, claudin-7 was only present in epithelial Ishikawa cells, and silencing by small-interfering RNA increased cell invasiveness. In contrast, claudin-11 could be demonstrated in Ishikawa and endometriotic 12Z and 49Z cells. Silencing of claudin-11 decreased invasiveness of 12Z slightly but significantly in 49Z. We suggest that although claudin-7 and claudin-11 can be found in nearly all eutopic and ectopic epithelial cells, the impaired localization of claudin-11 in ectopic endometrium might contribute to the pathogenesis of endometriosis.

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Bronstein, J. M., K. Chen, S. Tiwari-Woodruff, and H. I. Kornblum. "Developmental expression of OSP/claudin-11." Journal of Neuroscience Research 60, no. 3 (May 1, 2000): 284–90. http://dx.doi.org/10.1002/(sici)1097-4547(20000501)60:3<284::aid-jnr2>3.0.co;2-t.

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Tiwari-Woodruff, Seema K., Alex G. Buznikov, Trung Q. Vu, Paul E. Micevych, Kendall Chen, Harley I. Kornblum, and Jeff M. Bronstein. "Osp/Claudin-11 Forms a Complex with a Novel Member of the Tetraspanin Super Family and β1 Integrin and Regulates Proliferation and Migration of Oligodendrocytes." Journal of Cell Biology 153, no. 2 (April 16, 2001): 295–306. http://dx.doi.org/10.1083/jcb.153.2.295.

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Oligodendrocyte-specific protein (OSP)/claudin-11 is a major component of central nervous system myelin and forms tight junctions (TJs) within myelin sheaths. TJs are essential for forming a paracellular barrier and have been implicated in the regulation of growth and differentiation via signal transduction pathways. We have identified an OSP/claudin-11–associated protein (OAP)1, using a yeast two-hybrid screen. OAP-1 is a novel member of the tetraspanin superfamily, and it is widely expressed in several cell types, including oligodendrocytes. OAP-1, OSP/claudin-11, and β1 integrin form a complex as indicated by coimmunoprecipitation and confocal immunocytochemistry. Overexpression of OSP/claudin-11 or OAP-1 induced proliferation in an oligodendrocyte cell line. Anti–OAP-1, anti–OSP/claudin-11, and anti–β1 integrin antibodies inhibited migration of primary oligodendrocytes, and migration was impaired in OSP/claudin-11–deficient primary oligodendrocytes. These data suggest a role for OSP/claudin-11, OAP-1, and β1 integrin complex in regulating proliferation and migration of oligodendrocytes, a process essential for normal myelination and repair.

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Morita, Kazumasa, Hiroyuki Sasaki, Kazushi Fujimoto, Mikio Furuse, and Shoichiro Tsukita. "Claudin-11/OSP-based Tight Junctions of Myelin Sheaths in Brain and Sertoli Cells in Testis." Journal of Cell Biology 145, no. 3 (May 3, 1999): 579–88. http://dx.doi.org/10.1083/jcb.145.3.579.

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Members of the newly identified claudin gene family constitute tight junction (TJ) strands, which play a pivotal role in compartmentalization in multicellular organisms. We identified oligodendrocyte-specific protein (OSP) as claudin-11, a new claudin family member, due to its sequence similarity to claudins as well as its ability to form TJ strands in transfected fibroblasts. Claudin-11/OSP mRNA was expressed in the brain and testis. Immunofluorescence microscopy with anti–claudin-11/OSP polyclonal antibody (pAb) and anti-neurofilament mAb revealed that in the brain claudin-11/OSP-positive linear structures run in a gentle spiral around neurofilament-positive axons. At the electron microscopic level, these linear structures were identified as the so-called interlamellar strands in myelin sheaths of oligodendrocytes. In testis, well-developed TJ strands of Sertoli cells were specifically labeled with anti–claudin-11/OSP pAb both at immunofluorescence and electron microscopic levels. These findings indicated that the interlamellar strands of oligodendrocyte myelin sheaths can be regarded as a variant of TJ strands found in many other epithelial cells, and that these strands share a specific claudin species, claudin-11/OSP, with those in Sertoli cells to create and maintain the repeated compartments around axons by oligodendrocytes.

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Florin, Anne, Magali Maire, Aline Bozec, Ali Hellani, Sonia Chater, Remi Bars, Franck Chuzel, and Mohamed Benahmed. "Androgens and Postmeiotic Germ Cells Regulate Claudin-11 Expression in Rat Sertoli Cells." Endocrinology 146, no. 3 (March 1, 2005): 1532–40. http://dx.doi.org/10.1210/en.2004-0834.

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In the present study we investigated whether fetal exposure to flutamide affected messenger and protein levels of claudin-11, a key Sertoli cell factor in the establishment of the hemotesticular barrier, at the time of two key events of postnatal testis development: 1) before puberty (postnatal d 14) during the establishment of the hemotesticular barrier, and 2) at the adult age (postnatal d 90) at the time of full spermatogenesis. The data obtained show that claudin-11 expression was inhibited in prepubertal rat testes exposed in utero to 2 and 10 mg/kg·d flutamide. However, in adult testes, the inhibition was observed only with 2, and not with 10, mg/kg·d of the antiandrogen. It is shown here that these differences between prepubertal and adult testes could be related to dual and opposed regulation of claudin-11 expression resulting from positive control by androgens and an inhibitory effect of postmeiotic germ cells. Indeed, testosterone is shown to stimulate claudin-11 expression in cultured Sertoli cells in a dose- and time-dependent manner (maximum effect with 0.06 μm after 72 h of treatment). In contrast, postmeiotic germ cells potentially exert a negative effect on claudin-11 expression, because adult rat testes depleted in spermatids (after local irradiation) displayed increased claudin-11 expression, whereas in a model of cocultured Sertoli and germ cells, spermatids, but not spermatocytes, inhibited claudin-11 expression. The apparent absence of claudin-11 expression changes in adult rat testes exposed to 10 mg/kg·d flutamide therefore could result from the antagonistic effects of 1) the inhibitory action of the antiandrogen and 2) the stimulatory effect of the apoptotic germ cells on claudin-11 expression. Together, due to the key role of claudin-11 in the hemotesticular barrier, the present findings suggest that such regulatory mechanisms may potentially affect this barrier (re)modeling during spermatogenesis.

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McCabe, M. J., and P. G. Stanton. "116. Contribution of claudin-11 to the inter-Sertoli cell tight junction, in vitro." Reproduction, Fertility and Development 17, no. 9 (2005): 72. http://dx.doi.org/10.1071/srb05abs116.

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The inter-Sertoli cell tight junction (TJ) forms the blood testis barrier (BTB) between Sertoli cells and is composed of three major transmembrane proteins: claudin-11, occludin and junctional adhesion molecule. Formation of the BTB occurs during puberty associating with an increase in circulating gonadotrophins. Claudin-11 and occludin are hormonally regulated in vitro although their importance to the function of the TJ is unknown. The aim of this study was to investigate the contribution of claudin-11 to the inter-Sertoli cell TJ in vitro by blocking gene expression using RNA interference. Two claudin-11-specific siRNA fragments were designed for this purpose. Sertoli cells in primary culture formed stable TJs within 5 days as measured by transepithelial electrical resistance (TER). The addition of siRNA for 2 days resulted in a significant (P < 0.01) 55% (mean, SD, n = 4 cultures) decrease in TER along with a major reduction in claudin-11 localisation to the TJ as assessed by immunocytochemistry. The specificity of the siRNA was shown by the presence of extensive immunostaining of occludin and of the adherens junction protein β-catenin in the same treatments. Similarly, claudin-11 mRNA expression significantly (P < 0.01) decreased by 71% (mean, SD, n = 3 cultures) in response to both claudin-11 siRNA fragments. Occludin mRNA expression was not affected. It is concluded that claudin-11 contributes at least 55% to the function of the rat Sertoli cell TJ in vitro. It is hypothesised that the remaining 45% of TJ function can be attributed to other integral proteins, such as occludin and junctional adhesion molecule. It is expected that claudin-11 and other TJ proteins play a pivotal role in the function of the BTB in vivo with potential implications in fertility and contraception.

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Kiuchi-Saishin, Yumiko, Shimpei Gotoh, Mikio Furuse, Akiko Takasuga, Yasuo Tano, and Shoichiro Tsukita. "Differential Expression Patterns of Claudins, Tight Junction Membrane Proteins, in Mouse Nephron Segments." Journal of the American Society of Nephrology 13, no. 4 (April 2002): 875–86. http://dx.doi.org/10.1681/asn.v134875.

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ABSTRACT. As the first step in understanding the physiologic functions of claudins (tight junction integral membrane proteins) in nephrons, the expression of claudin-1 to -16 in mouse kidneys was examined by Northern blotting. Among these claudins, only claudin-6, -9, -13, and -14 were not detectable. Claudin-5 and -15 were detected only in endothelial cells. Polyclonal antibodies specific for claudin-7 and -12 were not available. Therefore, the distributions of claudin-1, -2, -3, -4, -8, -10, -11, and -16 in nephron segments were examined with immunofluorescence microscopy. For identification of individual segments, antibodies specific for segment markers were used. Immunofluorescence microscopic analyses of serial frozen sections of mouse kidneys with polyclonal antibodies for claudins and segment markers revealed that claudins demonstrated very complicated, segment-specific, expression patterns in nephrons, i.e., claudin-1 and -2 in Bowman’s capsule, claudin-2, -10, and -11 in the proximal tubule, claudin-2 in the thin descending limb of Henle, claudin-3, -4, and -8 in the thin ascending limb of Henle, claudin-3, -10, -11, and -16 in the thick ascending limb of Henle, claudin-3 and -8 in the distal tubule, and claudin-3, -4, and -8 in the collecting duct. These segment-specific expression patterns of claudins are discussed, with special reference to the physiologic functions of tight junctions in nephrons.

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Devaux, Jerome, and Alexander Gow. "Tight junctions potentiate the insulative properties of small CNS myelinated axons." Journal of Cell Biology 183, no. 5 (December 1, 2008): 909–21. http://dx.doi.org/10.1083/jcb.200808034.

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Claudin family proteins form the physical barriers of tight junctions (TJs) and regulate paracellular diffusion across polarized epithelia. In addition to these heterotypic TJs, claudin 11 forms autotypic TJs comprising the radial component of central nervous system myelin. The exact function of these TJs has been unclear, although their location at the membrane perimeter is well sited to regulate diffusion between the interstitium and intramyelinic space. In this study, we demonstrate that claudin 11 affords rapid nerve conduction principally for small diameter myelinated axons. Claudin 11–null mice have preserved myelin and axonal architecture, but as much as a 60% decrease in conduction. They also have increased action potential thresholds and activated internodal potassium channels. These data indicate that TJs modulate the biophysical properties of myelin. Computational modeling reveals that claudin 11 reduces current flow through myelin and moderates its capacitive charging. Together, our data shed new light on myelin structural components and our understanding of the biology and pathophysiology of this membrane.

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11

Wolburg, Hartwig, Karen Wolburg-Buchholz, Stefan Liebner, and Britta Engelhardt. "Claudin-1, claudin-2 and claudin-11 are present in tight junctions of choroid plexus epithelium of the mouse." Neuroscience Letters 307, no. 2 (July 2001): 77–80. http://dx.doi.org/10.1016/s0304-3940(01)01927-9.

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Kim, Nah Ihm, Ga-Eon Kim, and Ji Shin Lee. "Diagnostic Usefulness of Claudin-3 and Claudin-4 for Immunocytochemical Differentiation between Metastatic Adenocarcinoma Cells and Reactive Mesothelial Cells in Effusion Cell Blocks." Acta Cytologica 60, no. 3 (2016): 232–39. http://dx.doi.org/10.1159/000447008.

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Objective: Claudin-3 and claudin-4 have recently been reported as promising targets for the detection and diagnosis of cancer. This study was designed to evaluate the diagnostic value of claudin-3 and claudin-4 immunoreactivity to distinguish metastatic adenocarcinoma cells (MAC) from reactive mesothelial cells (RMC) in effusions. Study Design: Claudin-3 and claudin-4 immunocytochemical staining was performed on 234 cell block specimens, including 194 malignant effusions with MAC and 40 benign effusions with RMC. Any degree of membranous staining was considered positive. Results: Claudin-3 was positive in 190 (97.9%) out of 194 cases with MAC and in 3 (7.5%) out of 40 cases with RMC. Claudin-4 immunoreactivity was seen in all 194 (100%) cases with MAC and in 11 (27.5%) out of 40 cases with RMC. In all claudin-3- or claudin-4-positive RMC samples, the area of positive staining was <25% of the cells. Claudin-3 and claudin-4 efficiently discriminated between MAC and RMC (p < 0.001 for both), and claudin-3 was more specific than claudin-4 in differentiating between MAC and RMC (p < 0.05). Conclusion: These results suggest that claudin-3 and claudin-4 are good candidates to be included as MAC markers in the panel of antibodies to distinguish MAC from RMC in effusion specimens.

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Van Itallie, Christina M., Alan S. Fanning, and James M. Anderson. "Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins." American Journal of Physiology-Renal Physiology 285, no. 6 (December 2003): F1078—F1084. http://dx.doi.org/10.1152/ajprenal.00116.2003.

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Tight junctions (TJ) regulate paracellular ionic charge selectivity and conductance across epithelial tissues and cell lines. These properties vary among epithelia, and recent evidence implicates the claudins, a family of TJ transmembrane proteins, as important determinants of both characteristics. To test the hypothesis that each claudin contributes a characteristic charge discrimination to the TJ, we expressed claudins-2, -4, -11, and -15 in both cation-selective Madin-Darby canine kidney (MDCK) II cells and in anion-selective LLC-PK1 cells and examined changes in transepithelial electrical resistance (TER) and paracellular charge selectivity. Regulated expression and localization were verified by immunoblot analysis and immunofluorescence microscopy, respectively. Expression of claudin-4 increased TER in both cell lines, whereas effects of the others on TER were variable. Claudin-4 and -11 decreased paracellular permeability for Na+ in MDCK II cells, whereas neither claudin-2 nor -15 had an effect. Conversely, in LLC-PK1 cells, claudin-2 and -15 increased the permeability for Na+, whereas claudin-4 and -11 were without effect. We conclude that the contribution of each claudin is most easily detectable when it reverses the direction of monolayer charge selectivity. These results are consistent with a model in which exogenous claudins add new charge-selective pores, leading to a physiological phenotype that combines endogenous and exogenous contributions. Additionally, it is possible to rationalize the direction of charge selectivity conferred by the individual claudins on the basis of electrostatic effects of the charged amino acids in their first extracellular loops.

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Elkouby-Naor, Liron, Zaid Abassi, Ayala Lagziel, Alexander Gow, and Tamar Ben-Yosef. "Double gene deletion reveals lack of cooperation between claudin 11 and claudin 14 tight junction proteins." Cell and Tissue Research 333, no. 3 (July 29, 2008): 427–38. http://dx.doi.org/10.1007/s00441-008-0621-9.

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Chiba, Koji, Kohei Yamaguchi, Makoto Ando, Hideaki Miyake, and Masato Fujisawa. "Expression Pattern of Testicular claudin-11 in Infertile Men." Urology 80, no. 5 (November 2012): 1161.e13–1161.e17. http://dx.doi.org/10.1016/j.urology.2012.06.036.

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Ahn, C., J. S. Lee, and E. B. Jeung. "128 EXPRESSIONS OF MOUSE TIGHT JUNCTION MOLECULES IN PLACENTA – CLAUDINS AND OTHER PARACELLULAR TRANSPORT MOLECULES." Reproduction, Fertility and Development 26, no. 1 (2014): 178. http://dx.doi.org/10.1071/rdv26n1ab128.

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Tight junctions (TJ) are composed of a branching network of sealing strands. Tight junctions regulate paracellular conductance and ionic selectivity. The TJ components include the peripheral protein ZO-1, junctional adhesion molecules (JAM), and integral proteins, such as occludin and claudin. Claudins, a family of proteins, are the most important components in TJ. They establish paracellular transport barriers, which control transportation of molecules within intercellular space. The current study focused on expression of claudin, suggesting claudin as a major working molecule in the paracellular transport system. In order to study the mechanisms and roles of the claudin family, the expression levels of claudin family in various organs should be determined. In this study, we examined expression of the mouse placental claudin family. Pregnant C57/BL6 mice (n = 5) were used in this study, and compared with β-actin, expression of TJ proteins, including Claudin-1 to Claudin-24, JAM-a, Zo-1, and occludin, tricellulin, and MarvelD3 was examined. In the transcription levels, Claudin-1 and -4 proteins were predominantly expressed. Claudin-1 and -4 have been known as a responsive gene for a direct decrease in paracellular conductance by selective reduction of the permeability of Na+ ions. On the other hand, Claudin-2, Claudin-3, Claudin-5, Cludin-11, and Claudin-12 showed ~33% expression compared with Claudin-1. Claudin-6 and Claudin-7 showed ~20% relative expression compared to Claudin 1. Claudin-10a and Claudin-16 were not detectable by real-time RT-PCR under our experimental conditions. Other claudin proteins showed low expression. Because the transcriptional levels of TJ genes were expressed variously, protein levels and their localization in the placenta will be further evaluated by immunostaining and Western blot assay. This study will provide data on expression of TJ genes and their localization in the mouse placenta, which may contribute to assuming the roles of these TJ genes regarding maternal-fetal ion transportation in the placenta.

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Tarulli, Gerard A., Sarah J. Meachem, Stefan Schlatt, and Peter G. Stanton. "Regulation of testicular tight junctions by gonadotrophins in the adult Djungarian hamster in vivo." REPRODUCTION 135, no. 6 (June 2008): 867–77. http://dx.doi.org/10.1530/rep-07-0572.

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This study aimed to assess the effect of gonadotrophin suppression and FSH replacement on testicular tight junction dynamics and blood–testis barrier (BTB) organisation in vivo, utilising the seasonal breeding Djungarian hamster. Confocal immunohistology was used to assess the cellular organisation of tight junction proteins and real-time PCR to quantify tight junction mRNA. The effect of tight junction protein organisation on the BTB permeability was also investigated using a biotin-linked tracer. Tight junction protein (claudin-3, junctional adhesion molecule (JAM)-A and occludin) localisation was present but disorganised after gonadotrophin suppression, while mRNA levels (claudin-11, claudin-3 and occludin) were significantly (two- to threefold) increased. By contrast, both protein localisation and mRNA levels for the adaptor protein zona occludens-1 decreased after gonadotrophin suppression. FSH replacement induced a rapid reorganisation of tight junction protein localisation. The functionality of the BTB (as inferred by biotin tracer permeation) was found to be strongly associated with the organisation and localisation of claudin-11. Surprisingly, JAM-A was also recognised on spermatogonia, suggesting an additional novel role for this protein in trans-epithelial migration of germ cells across the BTB. It is concluded that gonadotrophin regulation of tight junction proteins forming the BTB occurs primarily at the level of protein organisation and not gene transcription in this species, and that immunolocalisation of the organised tight junction protein claudin-11 correlates with BTB functionality.

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Borovac, Jelena, Reid S. Barker, Juraj Rievaj, Andrew Rasmussen, Wanling Pan, Rachel Wevrick, and R. Todd Alexander. "Claudin-4 forms a paracellular barrier, revealing the interdependence of claudin expression in the loose epithelial cell culture model opossum kidney cells." American Journal of Physiology-Cell Physiology 303, no. 12 (December 15, 2012): C1278—C1291. http://dx.doi.org/10.1152/ajpcell.00434.2011.

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The effect of claudins on paracellular fluxes has been predominantly studied in either Madin-Darby canine kidney (MDCK) or LLCPK cells. Neither model system has a very low transepithelial resistance (TER) as observed in leaky epithelia. Moreover, results from one model system are not always consistent with another. Opossum kidney (OK) cells form tight junctions yet have a very low TER. We therefore set out to characterize the paracellular transport properties of this cell culture model. Ussing chamber dilution potential measurements revealed that OK cells exhibit a very low TER (11.7 ± 1.4 Ω·cm2), slight cation selectivity ( PNa/ PCl = 1.10 ± 0.01), and the Eisenman permeability sequence IV; the permeability of monovalent cations ranking K+ > Cs+ > Rb+ > Na+ > Li+. Quantitative real-time PCR studies found that OK cells endogenously express claudin-4 > -1 > -6 > -20 > -9 > -12 > -11 > -15. Overexpression of claudin-4 significantly increased TER, decreased Na+ and Cl− permeability, and increased levels of claudin-1, -6, and -9 mRNA. Knockdown of claudin-4 in the overexpressing cells significantly decreased TER without altering claudin expression; thus claudin-4 forms a barrier in OK cells. Knockdown of endogenous claudin-4 decreased claudin-1, -9, and -12 expression without altering TER. Claudin-2 overexpression decreased TER, significantly increased Na+ and Cl− permeability, and decreased claudin-12 and -6 expression. Together these results demonstrate that claudin expression is tightly coupled in OK cells.

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Abuazza, Ghazala, Amy Becker, Scott S. Williams, Sumana Chakravarty, Hoang-Trang Truong, Fangming Lin, and Michel Baum. "Claudins 6, 9, and 13 are developmentally expressed renal tight junction proteins." American Journal of Physiology-Renal Physiology 291, no. 6 (December 2006): F1132—F1141. http://dx.doi.org/10.1152/ajprenal.00063.2006.

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The adult proximal tubule is a low-resistance epithelium where there are high rates of both active transcellular and passive paracellular NaCl transport. We have previously demonstrated that the neonatal rabbit and rat proximal tubule have substantively different passive paracellular transport properties than the adult proximal tubule, which results in a maturational change in the paracellular passive flux of ions. Neonatal proximal tubules have a higher PNa/PCl ratio and lower chloride and bicarbonate permeabilities than adult proximal tubules. Claudins are a large family of proteins which are the gate keepers of the paracellular pathway, and claudin isoform expression determines the permeability characteristics of the paracellular pathway. Previous studies have shown that claudins 1, 2, 3, 4, 5, 7, 8, 10, 11, 12, 15, and 16 are expressed in the adult mouse kidney. To determine whether there are developmental claudin isoforms, we compared the claudin isoforms present in the neonatal and adult kidney using RT-PCR to detect mRNA of claudin isoforms. Claudin 6, claudin 9, and claudin 13 were either not expressed or barely detectable in the adult mouse kidney using traditional PCR, but were expressed in the neonatal mouse kidney. Using real-time RT-PCR, we were able to detect a low level of claudin 6 mRNA expression in the adult kidney compared with the neonate, but claudin 9 and claudin 13 were only detected in the neonatal kidney. There was the same maturational decrease in these claudin proteins with Western blot analysis. Immunohistochemistry showed high levels of expression of claudin 6 in neonatal proximal tubules, thick ascending limb, distal convoluted tubules, and collecting ducts in a paracellular distribution but there was no expression of claudin 6 in the adult kidney. Using real-time RT-PCR claudin 6 and 9 mRNA were present in 1-day-old proximal convoluted tubules and were virtually undetectable in proximal convoluted tubules from adults. Claudin 13 was not detectable in neonatal or adult proximal convoluted tubules. In summary, we have identified developmentally expressed claudin isoforms, claudin 6, claudin 9, and claudin 13. These paracellular proteins may play a role in the maturational changes in paracellular permeability.

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Chiba, K., K. Yamaguchi, K. Okada, K. Matsushita, F. Li, M. Ando, H. Miyake, and M. Fujisawa. "51 Expression pattern of testicular claudin-11 in infertile men." European Urology Supplements 11, no. 1 (February 2012): e51-e51a. http://dx.doi.org/10.1016/s1569-9056(12)60050-5.

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Nah, Won Heum, Jae Eun Lee, Hyun Jun Park, Nam Cheol Park, and Myung Chan Gye. "Claudin-11 expression increased in spermatogenic defect in human testes." Fertility and Sterility 95, no. 1 (January 2011): 385–88. http://dx.doi.org/10.1016/j.fertnstert.2010.08.023.

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Li, Ching-Fei, Jia-Yang Chen, Yang-Hui Ho, Wen-Hao Hsu, Liang-Chun Wu, Hsin-Yi Lan, Dennis Shin-Shian Hsu, Shyh-Kuan Tai, Ying-Chih Chang, and Muh-Hwa Yang. "Snail-induced claudin-11 prompts collective migration for tumour progression." Nature Cell Biology 21, no. 2 (January 21, 2019): 251–62. http://dx.doi.org/10.1038/s41556-018-0268-z.

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Ahmed, Yasser N., Ghassan A. Al-Shamma, and Abdullah Salih Hassen. "Evaluation of Serum Level of Claudin‐ 3 and Its Association with Disease Severity in Patients with Psoriasis in Iraqi patients." Journal of University of Shanghai for Science and Technology 23, no. 09 (September 21, 2021): 1031–39. http://dx.doi.org/10.51201/jusst/21/09648.

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Background Psoriasis is a prevalent inflammatory skin disease. Psoriasis is a complex illness in which environmental variables acting on individuals with unique genetic predisposition causing immunological dysregulation. Claudins are transmembrane proteins that help to generate tight junctions by binding to the actin cytoskeleton. Claudin 3 in the blood is thought to be a good indicator of intestinal permeability. Objective: The aim of this study was to detect of the alteration of claudin-3 in psoriasis patient and find the correlation between severity and concentration of the claudin-3. Patients and methods: forty psoriatic patients (25males and 15 females) and thirty normal healthy controls (19 men and 11 females) who were age and sex matched to the cases group were included in this study. They were chosen at random from Al Fallujah hospital Dermatology Department outpatient clinic. Result: When compared to the control group, the psoriasis group had substantially greater levels of claudin-3 (mean=2.18 ± 0.16 versus 1.27 ± 0.03; p0.0001). Furthermore, the amount of claudin-3 rose progressively as the severity grade increased (001). There were no significant correlations between claudin-3 levels and gender, dietary status, or family history in the psoriasis group (p>0.05 for each). Conclusion: Claudin-3 levels were considerably greater in psoriasis patients than in healthy controls. PASI levels were shown to be linked to claudin-3 levels.

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McCabe, Mark J., Gerard A. Tarulli, Sarah J. Meachem, David M. Robertson, Peter M. Smooker, and Peter G. Stanton. "Gonadotropins Regulate Rat Testicular Tight Junctions in Vivo." Endocrinology 151, no. 6 (March 31, 2010): 2911–22. http://dx.doi.org/10.1210/en.2009-1278.

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Sertoli cell tight junctions (TJs) are an essential component of the blood-testis barrier required for spermatogenesis; however, the role of gonadotropins in their maintenance is unknown. This study aimed to investigate the effect of gonadotropin suppression and short-term replacement on TJ function and TJ protein (occludin and claudin-11) expression and localization, in an adult rat model in vivo. Rats (n = 10/group) received the GnRH antagonist, acyline, for 7 wk to suppress gonadotropins. Three groups then received for 7 d: 1) human recombinant FSH, 2) human chorionic gonadotropin (hCG) and rat FSH antibody (to study testicular androgen stimulation alone), and 3) hCG alone (to study testicular androgen and pituitary FSH production). TJ proteins were assessed by real-time PCR, Western blot analysis, and immunohistochemistry, whereas TJ function was assessed with a biotin permeation tracer. Acyline treatment significantly reduced testis weights, serum androgens, LH and FSH, and adluminal germ cells (pachytene spermatocyte, round and elongating spermatids). In contrast to controls, acyline induced seminiferous tubule permeability to biotin, loss of tubule lumens, and loss of occludin, but redistribution of claudin-11, immunostaining. Short-term hormone replacement stimulated significant recoveries in adluminal germ cell numbers. In hCG ± FSH antibody-treated rats, occludin and claudin-11 protein relocalized at the TJ, but such relocalization was minimal with FSH alone. Tubule lumens also reappeared, but most tubules remained permeable to biotin tracer, despite the presence of occludin. It is concluded that gonadotropins maintain Sertoli cell TJs in the adult rat via a mechanism that includes the localization of occludin and claudin-11 at functional TJs.

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Arcidiacono, Teresa, Marco Simonini, Chiara Lanzani, Lorena Citterio, Erika Salvi, Cristina Barlassina, Donatella Spotti, Daniele Cusi, Paolo Manunta, and Giuseppe Vezzoli. "Claudin-14 Gene Polymorphisms and Urine Calcium Excretion." Clinical Journal of the American Society of Nephrology 13, no. 10 (September 19, 2018): 1542–49. http://dx.doi.org/10.2215/cjn.01770218.

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Background and objectivesClaudin-16 and -19 are proteins forming pores for the paracellular reabsorption of divalent cations in the ascending limb of Henle loop; conversely, claudin-14 decreases ion permeability of these pores. Single-nucleotide polymorphisms in gene coding for claudin-14 were associated with kidney stones and calcium excretion. This study aimed to explore the association of claudin-14, claudin-16, and claudin-19 single-nucleotide polymorphisms with calcium excretion.Design, setting, participants, & measurementsWe performed a retrospective observational study of 393 patients with hypertension who were naïve to antihypertensive drugs, in whom we measured 24-hour urine calcium excretion; history of kidney stones was ascertained by interview; 370 of these patients underwent an intravenous 0.9% sodium chloride infusion (2 L in 2 hours) to evaluate the response of calcium excretion in three different 2-hour urine samples collected before, during, and after saline infusion. Genotypes of claudin-14, claudin-16, and claudin-19 were obtained from data of a previous genome-wide association study in the same patients.ResultsThirty-one single-nucleotide polymorphisms of the 3′ region of the claudin-14 gene were significantly associated with 24-hour calcium excretion and calcium excretion after saline infusion. The most significant associated single-nucleotide polymorphism was rs219755 (24-hour calcium excretion in GG, 225±124 mg/24 hours; 24-hour calcium excretion in GA, 194±100 mg/24 hours; 24-hour calcium excretion in AA, 124±73 mg/24 hours; P<0.001; calcium excretion during saline infusion in GG, 30±21 mg/2 hours; calcium excretion during saline infusion in GA, 29±18 mg/2 hours; calcium excretion during saline infusion in AA, 17±11 mg/2 hours; P=0.03). No significant associations were found among claudin-16 and claudin-19 single-nucleotide polymorphisms and calcium excretion and between claudin-14, claudin-16, and claudin-19 single-nucleotide polymorphisms and stones. Bioinformatic analysis showed that one single-nucleotide polymorphism at claudin-14 among those associated with calcium excretion may potentially influence splicing of transcript.ConclusionsClaudin-14 genotype at the 3′ region is associated with calcium excretion in 24-hour urine and after the calciuretic stimulus of saline infusion.

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Yamada, Nami O., Kazuki Heishima, Yukihiro Akao, and Takao Senda. "Extracellular Vesicles Containing MicroRNA-92a-3p Facilitate Partial Endothelial-Mesenchymal Transition and Angiogenesis in Endothelial Cells." International Journal of Molecular Sciences 20, no. 18 (September 7, 2019): 4406. http://dx.doi.org/10.3390/ijms20184406.

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Extracellular vesicles (EVs) are nanometer-sized membranous vesicles used for primitive cell-to-cell communication. We previously reported that colon cancer-derived EVs contain abundant miR-92a-3p and have a pro-angiogenic function. We previously identified Dickkopf-3 (Dkk-3) as a direct target of miR-92a-3p; however, the pro-angiogenic function of miR-92a-3p cannot only be attributed to downregulation of Dkk-3. Therefore, the complete molecular mechanism by which miR-92a-3p exerts pro-angiogenic effects is still unclear. Here, we comprehensively analyzed the gene sets affected by ectopic expression of miR-92a-3p in endothelial cells to elucidate processes underlying EV-induced angiogenesis. We found that the ectopic expression of miR-92a-3p upregulated cell cycle- and mitosis-related gene expression and downregulated adhesion-related gene expression in endothelial cells. We also identified a novel target gene of miR-92a-3p, claudin-11. Claudin-11 belongs to the claudin gene family, which encodes essential components expressed at tight junctions (TJs). Disruption of TJs with a concomitant loss of claudin expression is a significant event in the process of epithelial-to-mesenchymal transition. Our findings have unveiled a new EV-mediated mechanism for tumor angiogenesis through the induction of partial endothelial-to-mesenchymal transition in endothelial cells.

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Kondo, Y., T. Ishikawa, K. Yamaguchi, T. Haraguchi, Y. Sakamoto, and M. Fujisawa. "Mono-(2-ethylhexyl) Phthalate rapidly decreases claudin-11 in Sertoli cells." Fertility and Sterility 88 (September 2007): S369. http://dx.doi.org/10.1016/j.fertnstert.2007.07.1230.

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Mitic, Laura L., Christina M. Van Itallie, and James M. Anderson. "Molecular Physiology and Pathophysiology of Tight Junctions I. Tight junction structure and function: lessons from mutant animals and proteins." American Journal of Physiology-Gastrointestinal and Liver Physiology 279, no. 2 (August 1, 2000): G250—G254. http://dx.doi.org/10.1152/ajpgi.2000.279.2.g250.

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Tight junctions form the major paracellular barrier in epithelial tissues. Barrier-sealing properties are quite variable among cell types in terms of electrical resistance, solute and water flux, and charge selectivity. A molecular explanation for this variability appears closer following identification of the transmembrane proteins occludin and members of the claudin multigene family. For example, the human phenotype of mutations in claudin-16 suggests that it creates a channel that allows magnesium to diffuse through renal tight junctions. Similarly, a mouse knockout of claudin-11 reveals its role in formation of tight junctions in myelin and between Sertoli cells in testis. The study of other claudins is expected to elucidate their contributions to creating junction structure and physiology in all epithelial tissues.

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Niimi, Tomoaki, Kunio Nagashima, Jerrold M. Ward, Parviz Minoo, Drazen B. Zimonjic, Nicholas C. Popescu, and Shioko Kimura. "claudin-18, a Novel Downstream Target Gene for the T/EBP/NKX2.1 Homeodomain Transcription Factor, Encodes Lung- and Stomach-Specific Isoforms through Alternative Splicing." Molecular and Cellular Biology 21, no. 21 (November 1, 2001): 7380–90. http://dx.doi.org/10.1128/mcb.21.21.7380-7390.2001.

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ABSTRACT T/EBP/NKX2.1, a member of the NKX family of homeodomain-containing transcription factors, regulates the expression of a number of genes in lung and thyroid. Here we describe the isolation and characterization of a novel target gene, termed claudin-18, that is down-regulated in the lungs of T/ebp/Nkx2.1-null mouse embryos. The gene product exhibits an amino acid sequence similar to those of the claudin multigene family of proteins that constitute tight junction strands in epithelial cells. The gene was localized by fluorescence in situ hybridization to mouse chromosome 9 at region 9E3-F1 and to human chromosome 3 at region 3q21–23. Theclaudin-18 gene has two promoters, each with its own unique exon 1 that is spliced to common exons 2 through 5. Alternative usage of these promoters leads to production of lung and stomach-specific transcripts. The downstream lung-specific promoter contains two T/EBP/NKX2.1 binding sites responsible for trans activation of the gene by T/EBP/NKX2.1 in lung cells. Only claudin-18was down-regulated in T/ebp/Nkx2.1-null embryo lungs among 11 claudin transcripts examined. Furthermore, theclaudin-18 transcript has an alternative 12-bp insertion derived from the 5′ end of intron 4, which produces a C-terminally truncated isoform in lung and stomach. Immunohistochemistry demonstrated complete membrane localization of claudin-18 with small focal dots in the lung and stomach epithelial cells. Immunogold electron microscopy analysis revealed that claudin-18 is concentrated at the cell-cell borders of epithelial cells. These unique features suggest a potentially important role for claudin-18 in the structure and function of tight junctions in lung and stomach.

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Sadalla, José Carlos, Sílvia Vanessa Lourenço, Mirian Nacagami Sotto, Edmund Chada Baracat, and Jesus Paula Carvalho. "Claudin and p53 expression in vulvar lichen sclerosus and squamous-cell carcinoma." Journal of Clinical Pathology 64, no. 10 (June 4, 2011): 853–57. http://dx.doi.org/10.1136/jclinpath-2011-200103.

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AimsVulvar squamous-cell carcinoma (SCC) is a rare gynaecological cancer. Vulvar SCC has been shown to develop from vulvar intraepithelial neoplasias, which are related to lichen sclerosus (LS). Most studies to date have compared vulvar SCC with LS only morphologically, but no detailed molecular analysis has been performed. The objective was to compare claudin and p53 expression in these diseases and determine if there was any association with expression and vulvar SCC progression.MethodsImmunohistochemical analysis was performed in order to determine expression of p53 and claudin 1, 2, 3, 4, 5, 7 and 11 in human vulvar tissue samples from LS, SCC and control patients.ResultsClaudin 1, 2, 3, 4 and 5 were expressed comparably in the three groups. Claudin 7 and 11 expression was significantly decreased in LS and SCC samples compared with the control group. Expression of p53 was significantly increased in SCC and LS patient samples compared with the control group.ConclusionsClaudin 7 and 11 were not expressed in LS and SCC. However, there was no significant difference in expression of any of the claudins between the LS and SCC samples. Furthermore, p53 expression is the highest in SCC patients and lowest in the control group. However, expression of p53 did not vary between samples from isolated LS and LS associated SCC patients, suggesting that increased p53 expression is not the determining factor in the progression of LS lesions to SCC.

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Van den Bossche, J., D. Laoui, Y. Morias, K. Movahedi, G. Raes, P. De Baetselier, and J. A. Van Ginderachter. "Claudin-1, Claudin-2 and Claudin-11 Genes Differentially Associate with Distinct Types of Anti-inflammatory Macrophages In vitro and with Parasite- and Tumour-elicited Macrophages In vivo." Scandinavian Journal of Immunology 75, no. 6 (May 22, 2012): 588–98. http://dx.doi.org/10.1111/j.1365-3083.2012.02689.x.

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Li, Jinyun, Chongchang Zhou, Shumin Ni, Shaomin Wang, Chao Ni, Ping Yang, and Meng Ye. "Methylated claudin-11 associated with metastasis and poor survival of colorectal cancer." Oncotarget 8, no. 56 (October 23, 2017): 96249–62. http://dx.doi.org/10.18632/oncotarget.21997.

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Tiwari-Woodruff, Seema, Luis Beltran-Parrazal, Andrew Charles, Thomas Keck, Trung Vu, and Jeff Bronstein. "K+ channel KV3.1 associates with OSP/claudin-11 and regulates oligodendrocyte development." American Journal of Physiology-Cell Physiology 291, no. 4 (October 2006): C687—C698. http://dx.doi.org/10.1152/ajpcell.00510.2005.

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K+ channels are differentially expressed throughout oligodendrocyte (Olg) development. KV1 family voltage-sensitive K+ channels have been implicated in proliferation and migration of Olg progenitor cell (OPC) stage, and inward rectifier K+ channels (KIR)4.1 are required for OPC differentiation to myelin-forming Olg. In this report we have identified a Shaw family K+ channel, KV3.1, that is involved in proliferation and migration of OPC and axon myelination. Application of anti-KV3.1 antibody or knockout of Kv3.1 gene decreased the sustained K+ current component of OPC by 50% and 75%, respectively. In functional assays block of KV3.1-specific currents or knockout of Kv3.1 gene inhibited proliferation and migration of OPC. Adult Kv3.1 gene-knockout mice had decreased diameter of axons and decreased thickness of myelin in optic nerves compared with age-matched wild-type littermates. Additionally, KV3.1 was identified as an associated protein of Olg-specific protein (OSP)/claudin-11 via yeast two-hybrid analysis, which was confirmed by coimmunoprecipitation and coimmunohistochemistry. In summary, the KV3.1 K+ current accounts for a significant component of the total K+ current in cells of the Olg lineage and, in association with OSP/claudin-11, plays a significant role in OPC proliferation and migration and myelination of axons.

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Kondo, Yutaka, Tomomoto Ishikawa, Kohei Yamaguchi, Yuichi Sakamoto, Takeshi Ooba, and Masato Fujisawa. "1865: Mono-(2-Ethylhexyl) Phthalate Rapidly Decreases Claudin-11 in Sertoli Cells." Journal of Urology 177, no. 4S (April 2007): 619. http://dx.doi.org/10.1016/s0022-5347(18)32038-x.

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Stammler, Angelika, Benjamin Udo Lüftner, Sabine Kliesch, Wolfgang Weidner, Martin Bergmann, Ralf Middendorff, and Lutz Konrad. "Highly Conserved Testicular Localization of Claudin-11 in Normal and Impaired Spermatogenesis." PLOS ONE 11, no. 8 (August 3, 2016): e0160349. http://dx.doi.org/10.1371/journal.pone.0160349.

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Ulfig, Norbert, Michael Briese, and Jürgen Bohl. "Expression of Oligodendrocyte-Specific Protein/Claudin-11 in the Human Fetal Forebrain." Neuroembryology 1, no. 2 (2002): 48–53. http://dx.doi.org/10.1159/000054263.

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Cong, X., Y. Zhang, L. Shi, L. L. Wu, and G. Y. Yu. "Activation of vanilloid receptor upregulates expression of tight junction protein zonula occludens-1, claudin-3 and claudin-11 in rabbit submandibular gland." International Journal of Oral and Maxillofacial Surgery 38, no. 5 (May 2009): 489. http://dx.doi.org/10.1016/j.ijom.2009.03.331.

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Shen, Zhisen, Bing Cao, Lexi Lin, Chongchang Zhou, Dong Ye, Shijie Qiu, Qun Li, and Xiang Cui. "The Clinical Signification of Claudin-11 Promoter Hypermethylation for Laryngeal Squamous Cell Carcinoma." Medical Science Monitor 23 (July 26, 2017): 3635–40. http://dx.doi.org/10.12659/msm.904751.

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Agarwal, Rachana, Yuriko Mori, Yulan Cheng, Zhe Jin, Alexandru V. Olaru, James P. Hamilton, Stefan David, et al. "Silencing of Claudin-11 Is Associated with Increased Invasiveness of Gastric Cancer Cells." PLoS ONE 4, no. 11 (November 24, 2009): e8002. http://dx.doi.org/10.1371/journal.pone.0008002.

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Benvenga, Salvatore, Antonio Micali, Giovanni Pallio, Roberto Vita, Consuelo Malta, Domenico Puzzolo, Natasha Irrera, Francesco Squadrito, Domenica Altavilla, and Letteria Minutoli. "Effects of Myo-inositol Alone and in Combination with Seleno-Lmethionine on Cadmium-Induced Testicular Damage in Mice." Current Molecular Pharmacology 12, no. 4 (October 15, 2019): 311–23. http://dx.doi.org/10.2174/1874467212666190620143303.

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Background: Cadmium (Cd) impairs gametogenesis and damages the blood-testis barrier. Objective: As the primary mechanism of Cd-induced damage is oxidative stress, the effects of two natural antioxidants, myo-inositol (MI) and seleno-L-methionine (Se), were evaluated in mice testes. Methods: Eighty-four male C57 BL/6J mice were divided into twelve groups: 0.9% NaCl (vehicle; 1 ml/kg/day i.p.); Se (0.2 mg/kg/day per os); Se (0.4 mg/kg/day per os); MI (360 mg/kg/day per os); MI plus Se (0.2 mg/kg/day); MI plus Se (0.4 mg/kg/day); CdCl2 (2 mg/kg/day i.p.) plus vehicle; CdCl2 plus MI; CdCl2 plus Se (0.2 mg/kg/day); CdCl2 plus Se (0.4 mg/kg/day); CdCl2 plus MI plus Se (0.2 mg/kg/day); and CdCl2 plus MI plus Se (0.4 mg/kg/day). After 14 days, testes were processed for biochemical, structural and immunohistochemical analyses. Results: CdCl2 increased iNOS and TNF-α expression and Malondialdehyde (MDA) levels, lowered glutathione (GSH) and testosterone, induced testicular lesions, and almost eliminated claudin-11 immunoreactivity. Se administration at 0.2 or 0.4 mg/kg significantly reduced iNOS and TNF-α expression, maintained GSH, MDA and testosterone levels, structural changes and low claudin-11 immunoreactivity. MI alone or associated with Se at 0.2 or 0.4 mg/kg significantly reduced iNOS and TNF-α expression and MDA levels, increased GSH and testosterone levels, ameliorated structural organization and increased claudin-11 patches number. Conclusion: We demonstrated a protective effect of MI, a minor role of Se and an evident positive role of the association between MI and Se on Cd-induced damages of the testis. MI alone or associated with Se might protect testes in subjects exposed to toxicants, at least to those with behavior similar to Cd.

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Park, C. J., J. E. Lee, Y. S. Oh, S. Shim, W. H. Nah, K. J. Choi, and M. C. Gye. "Expression of claudin-1 and -11 in immature and mature pheasant (Phasianus colchicus) testes." Theriogenology 75, no. 3 (February 2011): 445–58. http://dx.doi.org/10.1016/j.theriogenology.2010.09.012.

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Chiba, K., Y. Kondo, F. Li, M. Ando, K. Yamaguchi, T. Ishikawa, and M. Fujisawa. "683 MONO-(2-ETHYLHEXYL) PHTHALATE DECREASES CLAUDIN-11 AND OCCLUDIN IN RAT SERTOLI CELLS." European Urology Supplements 10, no. 2 (March 2011): 219. http://dx.doi.org/10.1016/s1569-9056(11)60671-4.

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Yang, Qiaozhen, Jie Hao, Maoxin Chen, and Gang Li. "Dermatopontin is a novel regulator of the CdCl2-induced decrease in claudin-11 expression." Toxicology in Vitro 28, no. 6 (September 2014): 1158–64. http://dx.doi.org/10.1016/j.tiv.2014.05.013.

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Bronstein, Jeff M., Seema Tiwari-Woodruff, Alexei G. Buznikov, and David B. Stevens. "Involvement of OSP/claudin-11 in oligodendrocyte membrane interactions: Role in biology and disease." Journal of Neuroscience Research 59, no. 6 (March 15, 2000): 706–11. http://dx.doi.org/10.1002/(sici)1097-4547(20000315)59:6<706::aid-jnr2>3.0.co;2-d.

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Morrow, Carla M. K., Dolores Mruk, C. Yan Cheng, and Rex A. Hess. "Claudin and occludin expression and function in the seminiferous epithelium." Philosophical Transactions of the Royal Society B: Biological Sciences 365, no. 1546 (May 27, 2010): 1679–96. http://dx.doi.org/10.1098/rstb.2010.0025.

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Integral membrane proteins that contribute to function of the blood–testes barrier (BTB) in mice include claudins 3, 5 and 11 and occludin. Although claudin 11 is expressed throughout all stages of the seminiferous epithelial cycle, claudins 3 and 5 have specific expression at stage VIII. These differences in protein expression suggest that the interactions among, and functions of, these integral membrane proteins may shift over the course of the seminiferous epithelial cycle. Also, differences in expression among rodent species and men may make interpretation of studies across species challenging. This review will discuss the characteristics of claudins and occludin; the expression, regulation and function of these integral membrane proteins in the seminiferous epithelium; and how these properties relate to the unique features of BTB.

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Yang, Peng, Mei Zhang, Xiting Liu, and Huayun Pu. "MicroRNA-421 promotes the proliferation and metastasis of gastric cancer cells by targeting claudin-11." Experimental and Therapeutic Medicine 14, no. 3 (July 17, 2017): 2625–32. http://dx.doi.org/10.3892/etm.2017.4798.

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Stanton, PeterG, MarkJ McCabe, CarolineFH Foo, MarcelE Dinger, and PeterM Smooker. "Claudin-11 and occludin are major contributors to Sertoli cell tight junction function, in vitro." Asian Journal of Andrology 18, no. 4 (2016): 620. http://dx.doi.org/10.4103/1008-682x.163189.

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Guo, Qing Yun, Zhen Zhen Gao, Li Zhao, Jun Ping He, and Cheng Sheng Dong. "Expression of growth differentiation factor 9 (GDF9), ALK5, and claudin-11 in adult alpaca testis." Acta Histochemica 115, no. 1 (January 2013): 16–21. http://dx.doi.org/10.1016/j.acthis.2012.02.007.

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Chow, E., J. Mottahedeh, M. Prins, W. Ridder, S. Nusinowitz, and J. M. Bronstein. "Disrupted compaction of CNS myelin in an OSP/Claudin-11 and PLP/DM20 double knockout mouse." Molecular and Cellular Neuroscience 29, no. 3 (July 2005): 405–13. http://dx.doi.org/10.1016/j.mcn.2005.03.007.

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Gow, Alexander, Cherie M. Southwood, Jing Song Li, Milena Pariali, Gavin P. Riordan, Scott E. Brodie, John Danias, Jeff M. Bronstein, Bechara Kachar, and Robert A. Lazzarini. "CNS Myelin and Sertoli Cell Tight Junction Strands Are Absent in Osp/Claudin-11 Null Mice." Cell 99, no. 6 (December 1999): 649–59. http://dx.doi.org/10.1016/s0092-8674(00)81553-6.

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Journal articles on the topic 'Claudin-11'

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