Relevant bibliographies by topics / Tight junction

Academic literature on the topic 'Tight junction'

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Published: 4 June 2021
Last updated: 10 March 2023

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Journal articles on the topic "Tight junction"

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Schneeberger, Eveline E., and Robert D. Lynch. "The tight junction: a multifunctional complex." American Journal of Physiology-Cell Physiology 286, no. 6 (June 2004): C1213—C1228. http://dx.doi.org/10.1152/ajpcell.00558.2003.

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Multicellular organisms are separated from the external environment by a layer of epithelial cells whose integrity is maintained by intercellular junctional complexes composed of tight junctions, adherens junctions, and desmosomes, whereas gap junctions provide for intercellular communication. The aim of this review is to present an updated overview of recent developments in the area of tight junction biology. In a relatively short time, our knowledge of the tight junction has evolved from a relatively simple view of it being a permeability barrier in the paracellular space and a fence in the plane of the plasma membrane to one of it acting as a multicomponent, multifunctional complex that is involved in regulating numerous and diverse cell functions. A group of integral membrane proteins—occludin, claudins, and junction adhesion molecules—interact with an increasingly complex array of tight junction plaque proteins not only to regulate paracellular solute and water flux but also to integrate such diverse processes as gene transcription, tumor suppression, cell proliferation, and cell polarity.
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Wolburg, H., J. Neuhaus, U. Kniesel, B. Krauss, E. M. Schmid, M. Ocalan, C. Farrell, and W. Risau. "Modulation of tight junction structure in blood-brain barrier endothelial cells. Effects of tissue culture, second messengers and cocultured astrocytes." Journal of Cell Science 107, no. 5 (May 1, 1994): 1347–57. http://dx.doi.org/10.1242/jcs.107.5.1347.

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Tight junctions between endothelial cells of brain capillaries are the most important structural elements of the blood-brain barrier. Cultured brain endothelial cells are known to loose tight junction-dependent blood-brain barrier characteristics such as macromolecular impermeability and high electrical resistance. We have directly analyzed the structure and function of tight junctions in primary cultures of bovine brain endothelial cells using quantitative freeze-fracture electron microscopy, and ion and inulin permeability. The complexity of tight junctions, defined as the number of branch points per unit length of tight junctional strands, decreased 5 hours after culture but thereafter remained almost constant. In contrast, the association of tight junction particles with the cytoplasmic leaflet of the endothelial membrane bilayer (P-face) decreased continuously with a major drop between 16 hours and 24 hours. The complexity of tight junctions could be increased by elevation of intracellular cAMP levels while phorbol esters had the opposite effect. On the other hand, the P-face association of tight junction particles was enhanced by elevation of cAMP levels and by coculture of endothelial cells with astrocytes or exposure to astrocyte-conditioned medium. The latter effect on P-face association was induced by astrocytes but not fibroblasts. Elevation of cAMP levels together with astrocyte-conditioned medium synergistically increased transendothelial electrical resistance and decreased inulin permeability of primary cultures, thus confirming the effects on tight junction structure and barrier function. P-face association of tight junction particles in brain endothelial cells may therefore be a critical feature of blood-brain barrier function that can be specifically modulated by astrocytes and cAMP levels. Our results suggest an important functional role for the cytoplasmic anchorage of tight junction particles for brain endothelial barrier function in particular and probably paracellular permeability in general.
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Rouaud, Florian, Isabelle Méan, and Sandra Citi. "The ACE2 Receptor for Coronavirus Entry Is Localized at Apical Cell—Cell Junctions of Epithelial Cells." Cells 11, no. 4 (February 11, 2022): 627. http://dx.doi.org/10.3390/cells11040627.

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Transmembrane proteins of adherens and tight junctions are known targets for viruses and bacterial toxins. The coronavirus receptor ACE2 has been localized at the apical surface of epithelial cells, but it is not clear whether ACE2 is localized at apical Cell—Cell junctions and whether it associates with junctional proteins. Here we explored the expression and localization of ACE2 and its association with transmembrane and tight junction proteins in epithelial tissues and cultured cells by data mining, immunoblotting, immunofluorescence microscopy, and co-immunoprecipitation experiments. ACE2 mRNA is abundant in epithelial tissues, where its expression correlates with the expression of the tight junction proteins cingulin and occludin. In cultured epithelial cells ACE2 mRNA is upregulated upon differentiation and ACE2 protein is widely expressed and co-immunoprecipitates with the transmembrane proteins ADAM17 and CD9. We show by immunofluorescence microscopy that ACE2 colocalizes with ADAM17 and CD9 and the tight junction protein cingulin at apical junctions of intestinal (Caco-2), mammary (Eph4) and kidney (mCCD) epithelial cells. These observations identify ACE2, ADAM17 and CD9 as new epithelial junctional transmembrane proteins and suggest that the cytokine-enhanced endocytic internalization of junction-associated protein complexes comprising ACE2 may promote coronavirus entry.
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Gopalakrishnan, Shobha, Kenneth W. Dunn, and James A. Marrs. "Rac1, but not RhoA, signaling protects epithelial adherens junction assembly during ATP depletion." American Journal of Physiology-Cell Physiology 283, no. 1 (July 1, 2002): C261—C272. http://dx.doi.org/10.1152/ajpcell.00604.2001.

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Rho family GTPase signaling regulates actin cytoskeleton and junctional complex assembly. Our previous work showed that RhoA signaling protects tight junctions from damage during ATP depletion. Here, we examined whether RhoA GTPase signaling protects adherens junction assembly during ATP depletion. Despite specific RhoA signaling- and ATP depletion-induced effects on adherens junction assembly, RhoA signaling did not alter adherens junction disassembly rates during ATP depletion. This shows that RhoA signaling specifically protects tight junctions from damage during ATP depletion. Rac1 GTPase signaling also regulates adherens junction assembly and therefore may regulate adherens junction assembly during ATP depletion. Indeed, we found that Rac1 signaling protects adherens junctions from damage during ATP depletion. Adherens junctions are regulated by various GTPases, including RhoA and Rac1, but adherens junctions are specifically protected by Rac1 signaling.
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Satterfield, M. Carey, Kathrin A. Dunlap, Kanako Hayashi, Robert C. Burghardt, Thomas E. Spencer, and Fuller W. Bazer. "Tight and Adherens Junctions in the Ovine Uterus: Differential Regulation by Pregnancy and Progesterone." Endocrinology 148, no. 8 (August 1, 2007): 3922–31. http://dx.doi.org/10.1210/en.2007-0321.

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In species with noninvasive implantation by conceptus trophectoderm, fetal/maternal communications occur across the endometrial epithelia. The present studies identified changes in junctional complexes in the ovine endometrium that regulate paracellular trafficking of water, ions, and other molecules, and the secretory capacity of the uterine epithelia. Distinct temporal and spatial alterations in occludin, tight junction protein 2, and claudin 1–4 proteins were observed in the endometrium of cyclic and early pregnant ewes. Dynamic changes in tight junction formation were characterized by an abundance of tight junction proteins on d 10 of the estrous cycle and pregnancy that substantially decreased by d 12. Early progesterone administration advanced conceptus development on d 9 and 12 that was associated with loss of tight-junction-associated proteins. Pregnancy increased tight-junction-associated proteins between d 14–16. Cadherin 1 and β-catenin, which form adherens junctions, were abundant in the endometrial glands, but decreased after d 10 of pregnancy in the luminal epithelium and then increased by d 16 with the onset of implantation. Results support the ideas that progesterone elicits transient decreases in tight and adherens junctions in the endometrial luminal epithelium between d 10–12 that increases selective serum and tissue fluid transudation to enhance blastocyst elongation, which is subsequently followed by an increase in tight and adherens junctions between d 14–16 that may be required for attachment and adherence of the trophectoderm for implantation. The continuous presence of tight and adherens junctions in the uterine glands would allow for vectorial secretion of trophic substances required for conceptus elongation and survival.
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Chalmers, Andrew D., and Paul Whitley. "Continuous endocytic recycling of tight junction proteins: how and why?" Essays in Biochemistry 53 (August 28, 2012): 41–54. http://dx.doi.org/10.1042/bse0530041.

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Tight junctions consist of many proteins, including transmembrane and associated cytoplasmic proteins, which act to provide a barrier regulating transport across epithelial and endothelial tissues. These junctions are dynamic structures that are able to maintain barrier function during tissue remodelling and rapidly alter it in response to extracellular signals. Individual components of tight junctions also show dynamic behaviour, including migration within the junction and exchange in and out of the junctions. In addition, it is becoming clear that some tight junction proteins undergo continuous endocytosis and recycling back to the plasma membrane. Regulation of endocytic trafficking of junctional proteins may provide a way of rapidly remodelling junctions and will be the focus of this chapter.
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Haas, Alexis J., Ceniz Zihni, Susanne M. Krug, Riccardo Maraspini, Tetsuhisa Otani, Mikio Furuse, Alf Honigmann, Maria S. Balda, and Karl Matter. "ZO-1 Guides Tight Junction Assembly and Epithelial Morphogenesis via Cytoskeletal Tension-Dependent and -Independent Functions." Cells 11, no. 23 (November 25, 2022): 3775. http://dx.doi.org/10.3390/cells11233775.

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Formation and maintenance of tissue barriers require the coordination of cell mechanics and cell–cell junction assembly. Here, we combined methods to modulate ECM stiffness and to measure mechanical forces on adhesion complexes to investigate how tight junctions regulate cell mechanics and epithelial morphogenesis. We found that depletion of the tight junction adaptor ZO-1 disrupted junction assembly and morphogenesis in an ECM stiffness-dependent manner and led to a stiffness-dependant reorganisation of active myosin. Both junction formation and morphogenesis were rescued by inhibition of actomyosin contractility. ZO-1 depletion also impacted mechanical tension at cell-matrix and E-cadherin-based cell–cell adhesions. The effect on E-cadherin also depended on ECM stiffness and correlated with effects of ECM stiffness on actin cytoskeleton organisation. However, ZO-1 knockout also revealed tension-independent functions of ZO-1. ZO-1-deficient cells could assemble functional barriers at low tension, but their tight junctions remained corrupted with strongly reduced and discontinuous recruitment of junctional components. Our results thus reveal that reciprocal regulation between ZO-1 and cell mechanics controls tight junction assembly and epithelial morphogenesis, and that, in a second, tension-independent step, ZO-1 is required to assemble morphologically and structurally fully assembled and functionally normal tight junctions.
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Chen, Yan-hua, Christa Merzdorf, David L. Paul, and Daniel A. Goodenough. "COOH Terminus of Occludin Is Required for Tight Junction Barrier Function in Early Xenopus Embryos." Journal of Cell Biology 138, no. 4 (August 25, 1997): 891–99. http://dx.doi.org/10.1083/jcb.138.4.891.

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Occludin is the only known integral membrane protein localized at the points of membrane– membrane interaction of the tight junction. We have used the Xenopus embryo as an assay system to examine: (a) whether the expression of mutant occludin in embryos will disrupt the barrier function of tight junctions, and (b) whether there are signals within the occludin structure that are required for targeting to the sites of junctional interaction. mRNAs transcribed from a series of COOH-terminally truncated occludin mutants were microinjected into the antero–dorsal blastomere of eight-cell embryos. 8 h after injection, the full-length and the five COOH-terminally truncated proteins were all detected at tight junctions as defined by colocalization with both endogenous occludin and zonula occludens-1 demonstrating that exogenous occludin correctly targeted to the tight junction. Importantly, our data show that tight junctions containing four of the COOH-terminally truncated occludin proteins were leaky; the intercellular spaces between the apical cells were penetrated by sulfosuccinimidyl-6-(biotinamido) Hexanoate (NHS-LC-biotin). In contrast, embryos injected with mRNAs coding for the full-length, the least truncated, or the soluble COOH terminus remained impermeable to the NHS-LC-biotin tracer. The leakage induced by the mutant occludins could be rescued by coinjection with full-length occludin mRNA. Immunoprecipitation analysis of detergent-solubilized embryo membranes revealed that the exogenous occludin was bound to endogenous Xenopus occludin in vivo, indicating that occludin oligomerized during tight junction assembly. Our data demonstrate that the COOH terminus of occludin is required for the correct assembly of tight junction barrier function. We also provide evidence for the first time that occludin forms oligomers during the normal process of tight junction assembly. Our data suggest that mutant occludins target to the tight junction by virtue of their ability to oligomerize with full-length endogenous molecules.
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Gopalakrishnan, Shobha, Narayan Raman, Simon J. Atkinson, and James A. Marrs. "Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion." American Journal of Physiology-Cell Physiology 275, no. 3 (September 1, 1998): C798—C809. http://dx.doi.org/10.1152/ajpcell.1998.275.3.c798.

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Tight junctions control paracellular permeability and cell polarity. Rho GTPase regulates tight junction assembly, and ATP depletion of Madin-Darby canine kidney (MDCK) cells (an in vitro model of renal ischemia) disrupts tight junctions. The relationship between Rho GTPase signaling and ATP depletion was examined. Rho inhibition resulted in decreased localization of zonula occludens-1 (ZO-1) and occludin at cell junctions; conversely, constitutive Rho signaling caused an accumulation of ZO-1 and occludin at cell junctions. Inhibiting Rho before ATP depletion resulted in more extensive loss of junctional components between transfected cells than control junctions, whereas cells expressing activated Rho better maintained junctions during ATP depletion than control cells. ATP depletion and Rho signaling altered phosphorylation signaling mechanisms. ZO-1 and occludin exhibited rapid decreases in phosphoamino acid content following ATP depletion, which was restored on recovery. Expression of Rho mutant proteins in MDCK cells also altered levels of occludin serine/threonine phosphorylation, indicating that occludin is a target for Rho signaling. We conclude that Rho GTPase signaling induces posttranslational effects on tight junction components. Our data also demonstrate that activating Rho signaling protects tight junctions from damage during ATP depletion.
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Stevenson, B. R., J. D. Siliciano, M. S. Mooseker, and D. A. Goodenough. "Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia." Journal of Cell Biology 103, no. 3 (September 1, 1986): 755–66. http://dx.doi.org/10.1083/jcb.103.3.755.

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A tight junction-enriched membrane fraction has been used as immunogen to generate a monoclonal antiserum specific for this intercellular junction. Hybridomas were screened for their ability to both react on an immunoblot and localize to the junctional complex region on frozen sections of unfixed mouse liver. A stable hybridoma line has been isolated that secretes an antibody (R26.4C) that localizes in thin section images of isolated mouse liver plasma membranes to the points of membrane contact at the tight junction. This antibody recognizes a polypeptide of approximately 225,000 D, detectable in whole liver homogenates as well as in the tight junction-enriched membrane fraction. R26.4C localizes to the junctional complex region of a number of other epithelia, including colon, kidney, and testis, and to arterial endothelium, as assayed by immunofluorescent staining of cryostat sections of whole tissue. This antibody also stains the junctional complex region in confluent monolayers of the Madin-Darby canine kidney epithelial cell line. Immunoblot analysis of Madin-Darby canine kidney cells demonstrates the presence of a polypeptide similar in molecular weight to that detected in liver, suggesting that this protein is potentially a ubiquitous component of all mammalian tight junctions. The 225-kD tight junction-associated polypeptide is termed "ZO-1."
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Dissertations / Theses on the topic "Tight junction"

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Morgan, Sarah V. "Tight junction protein expression in human astrocytes." Thesis, University of Sheffield, 2016. http://etheses.whiterose.ac.uk/14403/.

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Tight junctions are formed from a complex of different individual proteins. These complexes are expressed by epithelial cells and form an intercellular barrier which restricts and regulates paracellular permeability. Tight junction proteins have also been shown to be expressed in non-epithelial cells which do not form tight junctions, including astrocytes. The function(s) of these proteins within non-epithelial cells, however, remains unclear. This study aims to characterise the expression of tight junction proteins in astrocytes and investigate the function(s) of these proteins in these cells. The expression of the tight junction proteins occludin, claudin-5 and zonula occludens-1 (ZO-1) was characterised in vitro in both human primary astrocytes and the 1321N1 human astrocytoma cell line and in vivo in human autopsy brain samples. The function(s) of occludin was investigated using a pull-down protein binding assay and mass spectrometry analysis to identify putative binding partners for this protein in astrocytes. The current study demonstrates astrocytic and nuclear expression of occludin and ZO-1 in vitro and in vivo. The expression of claudin 5 in astrocytes remains difficult to determine due to contradictory evidence in which the astrocytic expression of this protein in vitro is not supported in vivo. Putative binding partners were also identified for the N- and C-terminal domains of occludin. Many of these proteins have functions in RNA metabolic processes, consequently their identification as putative occludin binding partners implicates occludin in functions beyond the formation of the tight junction complex. Although these interactions have not yet been validated, this study’s findings provide a platform upon which future research can be constructed.
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Chan, Wing-lim, and 陳穎廉. "The SARS coronavirus envelope protein E targets the PALS1 tight junction factor and alters formation of tight junctions of epithelialcells." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2011. http://hub.hku.hk/bib/B47169242.

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Tight junctions, as zones of close contact between epithelial and endothelial cells, form a physical barrier as one of the first host defense strategies that prevent the intrusion of pathogens across epithelia and endothelia. Recently, an interaction between the Severe Acute Respiratory Syndrome-Coronavirus (SARS-CoV) envelope protein (E) and PALS1, a member of the CRB tight junction complex, was identified in the Virus-Host Interaction group at HKU-Pasteur Research Centre (Teoh et al, 2010). In this report, I present in vitro data which helps to better understand how this protein-protein interaction could interfere with the formation and maintenance of tight junctions at the apical domain of epithelial cells. In previous research, the interaction between E and PALS1 was identified through a yeast two-hybrid screen and confirmed in vitro. A PDZ-binding motif (PBM) was identified at the C-terminal end of E, which interacts with the PDZ domain of PALS1. The objective of my research was to further enhance the knowledge of this interaction by studying the effect of E expression on PALS1 localization and tight junction structure in epithelial cells. I have shown that expression of E is associated with a partial relocalization of PALS1 to the Golgi compartment. Also, I discovered that when wild-type E, E(wt), was expressed in the MDCKII cell model, the time required for tight junction formation was extended to 6-8 hours, while normal cells only required two hours. Interestingly, expression of the E protein with a deletion of the PBM, E(ΔPBM) did not affect the timing of tight junction formation. This finding indicates that the PBM plays a critical role in the process of alteration of tight junctions mediated by E, most likely through its interaction with PALS1. Furthermore, the localization pattern of E was altered when its PBM was deleted. In the MDCKII model, E(wt) located, as expected, at membranes of the Golgi compartment, whereas E(ΔPBM) had a diffused distribution in the cytosol. This observation suggests that the PBM acts as a localization signal for the E protein to the Golgi region, which is the assembly site of the virus. Finally, to examine the role of the PBM in the context of the whole virus, I participated in the production of SARS-CoV recombinant viruses, with mutations in the PBM of E. Though this work is still in progress, the use of these viruses should help to delineate the role of E PBM in SARS-CoV induced pathogenesis in vitro and ultimately in vivo.
published_or_final_version
Pathology
Master
Master of Philosophy
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Thomas, Fay Christina. "Tight junction biogenesis in the mouse preimplantation embryo." Thesis, University of Southampton, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270661.

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Ackerman, Margaret E. "Targeting the tight junction : immunotherapy of colon cancer." Thesis, Massachusetts Institute of Technology, 2009. http://hdl.handle.net/1721.1/63023.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, February 2010.
"February 2010." Cataloged from PDF version of thesis.
Includes bibliographical references.
A33 is a cell surface glycoprotein of colon epithelium with a long clinical history as a target in antibody-based cancer therapy. Despite being present in normal colon, radio-labeled antibodies against A33 are selectively retained by tumors at long time points. Accordingly, we have studied the trafficking and kinetic properties of the antigen to determine its promise in multi-step, pretargeted immunotherapy. In vitro, the localization, mobility, and persistence of the antigen were investigated, and this work has demonstrated that the antigen is both highly immobile and extremely persistent, properties which may contribute to the prolonged retention of the clinically administered antibodies, and their uncommon ability to penetrate solid tumors. Secondly, because poor tissue penetration is a significant obstacle to the development of successful antibody drugs for immunotherapy of solid tumors, we assess the contribution of antigen density and turnover rate by evaluating the distance to which antibodies penetrate spheroids when these properties are systematically varied. The results agree well with the quantitative modeling predictions, and demonstrate that dosing distal regions of tumors is best achieved by selecting slowly internalized targets that are not expressed above the level necessary for recruiting a toxic dose of therapeutic. Lastly, we describe the in vitro characteristics and report the promising in vivo biodistribution of a multi-step tumor targeting therapy utilizing a novel bispecific antibody which recognizes both the A33 antigen and a small molecule radiometal chelate. Following these studies, several protein engineering techniques are presented. First, a new method of conducting de novo protein engineering utilizing highly avid magnetic beads is described, in which extremely weak interactions can be captured from large library populations. Secondly, an in vitro assay which utilizes these highly avid magnetic beads is used to score the clinical immunogenicity of therapeutic protein drugs is presented. Finally, the use of sortase A as a means to generate fusion proteins posttranslationally is described. Taken together, this additional work demonstrates a productive intersection of basic research and protein engineering methods.
by Margaret E. Ackerman.
Ph.D.
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Althubaiti, Suha. "Characterisation of epidermal tight junction proteins in ageing." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/characterisation-of-epidermal-tight-junction-proteins-in-ageing(a3a50284-018e-45f9-bdcf-a5ad004a0084).html.

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The epidermal tight junction (TJ) plays an important role as a barrier which protects the skin against dehydration and infection. Skin barrier function is known to decline with increasing age (Rabe et al., 2006). Human skin is subject to intrinsic (i.e. chronological) ageing and extrinsic (environmentally-induced) ageing. However, the role of TJs in the ageing process is still unknown. Therefore, in this study, using quantitative immunofluorescent staining TJ protein expression was investigated in intrinsically aged compared to young human skin. Since ultraviolet radiation (UVR) from sunlight is considered the major environmental insult to human skin, TJ proteins were also investigated in photoaged compared to photoprotected human skin, and in skin exposed to a single acute dose of UVR.In aged vs young skin, there was no significant difference either in the expression levels or localisation of TJ proteins.However, significant reduction in claudin-1 (cld-1) and increases in cld-7 and -12 expressions were demonstrated in chronically photoaged human skin suggesting differential regulation of clds in response to photoexposure. By contrast in acutely irradiated human skin, only a reduction in cld-1 expression was observed 24h after a single UVB dose. Moreover, in both chronic and acute UVR exposed human skin, cld-1 was most significantly reduced in the basal layer of the epidermis suggesting that the differentiation state of keratinocytes might be important in their response to UVR.To investigate these effects further, a normal human epidermal keratinocyte (NHEK) cell culture model was employed. A reduction in cld-1 expression and an increase in cld-4 were demonstrated in undifferentiated NHEK cells irradiated with sub lethal doses of UVR. Interestingly, no changes were observed in TJ protein expression in irradiated differentiated keratinocytes. However, when TJ function was measured in these cells using transepithelial electrical resistance (TEER) as a marker of TJ function, UVR induced a significant reduction in TEER. This coincided with an alteration in the organisation of cld-1 in irradiated differentiated keratinocytes.These data demonstrate that TJ protein expression is modulated by acute and chronic exposure to UVR. These observations may explain, at least in part, the decline in skin barrier function observed in response to UVR.
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Sonoda, Noriyuki. "Clostridium perfringens Enterotoxin Fragment Removes Specific Claudins from Tight Junction Strands : Evidence for Direct Involvement of Claudins in Tight Junction Barrier." Kyoto University, 2002. http://hdl.handle.net/2433/149669.

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McCabe, Mark James, and markmccabe02@hotmail com. "Hormonal regulation of the testicular Sertoli cell tight junction." RMIT University. Applied Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081212.100348.

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The Sertoli cell tight junction (TJ) of the seminiferous epithelium is important for the developmental process of spermatogenesis as it separates germ cells in the seminiferous tubules from the general circulation in the testicular interstitium. Absence of the TJ leads to spermatogenic arrest and infertility. TJs form at puberty as circulating gonadotrophins luteinising hormone/testosterone and follicle stimulating hormone increase. Several studies have demonstrated hormonal regulation of the two major TJ proteins, claudin-11 and occludin, and also of TJ function in vitro and in vivo. Men with low levels of circulating gonadotrophins exhibit an immature and dysfunctional TJ phenotype, which is reversed upon the exogenous application of gonadotrophins. This thesis hypothesises that claudin-11 and occludin are the major contributors to TJ function, and that gonadotrophins regulate TJ function and structure via these two proteins in several species including humans. This PhD was divided into four separate studies to address these hypotheses. The first study selectively silenced the genetic expression of claudin-11 and occludin with small interfering RNA (siRNA) in cultured immature rat Sertoli cells to determine their contribution to Sertoli cell TJ function in vitro. siRNA treatment against either protein significantly (p less than 0.01) reduced TJ function by ~50% as assessed by transepithelial electrical resistance. Immunocytochemistry displayed marked reductions in the localisation of these proteins to the TJ after siRNA treatment. It was concluded that both proteins significantly contributed to TJ function in vitro. The second and third studies then aimed to study hormonal regulation of the TJ in vivo. Weekly injections of the gonadotrophin releasing hormone antagonist acyline were used to suppress circulating gonadotrophins and spermatogenesis in adult rats. Acyline treatment disrupted i) the localisation of occludin to the TJ and ii) TJ function as shown by permeability to a biotin tracer, which was impermeable to TJs in controls. Short-term hormone replacement partially restored the effects of gonadotrophin suppression. It was concluded that gonadotrophins regulate the maintenance of the TJ in rats in vivo. The third study used the hypogonadal (hpg) mouse, which is a naturally occurring model of gonadotrophin deficiency with inactive spermatogenesis. Claudin-11 in hpg mice was not localised at the TJs, and these were dysfunctional as shown by permeability to biotin. Following hormone treatment, TJs were structurally and functionally competent, demonstrating that gonadotrophins also regulate the formation of TJs in vivo. The fourth study subsequently analysed TJs in gonadotrophin suppressed men, and it was found that claudin-11 staining was reduced from continuous bands in control men, to punctate staining in gonadotrophin-suppressed men, demonstrating that gonadotrophins also regulate the localisation of claudin-11 to the TJ in men in vivo. In summary, it is concluded that the Sertoli cell TJ is hormonally regulated, and that the major contributors to TJ function in vivo and in vitro are claudin-11 and occludin. It is hypothesised that the reduction of claudin-11 localisation to the TJ in men may also result in a loss of human Sertoli cell TJ function, suggesting that the TJ may be a potential target of hormonal contraception in men.
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Klein, Ryan Reaves Thakker Dhiren R. "Regulation of tight junction barrier function by phospholipase C." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2007. http://dc.lib.unc.edu/u?/etd,1380.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2007.
Title from electronic title page (viewed Apr. 25, 2008). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the School of Pharmacy." Discipline: Pharmacy; Department/School: Pharmacy.
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Bryant, Christopher. "Modulation of tight junction composition by the ERK pathway." Thesis, University of Bath, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.659138.

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Epithelia are an essential organising feature of multicellular organisms and the selective permeability of these barriers is regulated by the junctional repertoire of tight junction proteins. The regulation of epithelial permeability is essential for the physiological function of various organs and is often pathologically deregulated, for example in inflammatory disease and cancer. Tight junctions are dynamically regulated in response to diverse stimuli through multiple signalling pathways. The RAF/MEK/ERK pathway has been reported to mediate junctional remodelling in response to various growth factors and hormones, although the unique contribution of this pathway and the mechanisms of reorganisation remain unclear. To address this, specific activation of the RAF/MEK/ERK pathway was achieved through the expression of BRAFWT or oncogenic BRAFV600E in Madin-Darby Canine Kidney (MDCK) II cells, a model epithelial cell line used to study tight junctions. Specific activation of the RAF/MEK/ERK pathway generated a transient increase in transepithelial resistance, which occurred concurrently with the differential regulation of tight junction protein expression levels and subcellular distribution. Claudin-2 protein levels were decreased, while junctional levels of claudin-4 were increased. Total levels of claudin-1, occludin and ZO-1 were unchanged and were retained at areas of cell contact although showing varying degrees of cytoplasmic accumulation. Conditionally active CRAF:ER fusion proteins were expressed to provide increased control of RAF/MEK/ERK signal duration and to study the rates of TJ protein synthesis, degradation and localisation. RAF-mediated downregulation of CLDN2 mRNA caused subsequent claudin-2 protein depletion without influencing rates of internalisation or degradation. In contrast, RAF activation caused the redistribution of claudin-1 and -4 from the lateral membrane to the apical junction. This junctional accumulation could not be attributed to changes in claudin protein levels, stability or endocytic trafficking. Taken together, these data reveal surprising diversity in RAF/MEK/ERK-mediated TJ control, where distinct combinations of claudin-specific regulatory mechanisms act in concert to regulate epithelial permeability.
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Tavalali, Shida. "Analyse der Genexpression von Tight-junction-Proteinen der Claudin-Genfamilie." [S.l.] : [s.n.], 2005. http://www.diss.fu-berlin.de/2005/23/index.html.

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Books on the topic "Tight junction"

1

Marcelino, Cereijido, and Anderson James 1908-, eds. Tight junctions. 2nd ed. Boca Raton: CRC Press, 2001.

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Michael, Fromm. Molecular structure and function of the tight junction: From basic mechanisms to clinical manifestations. Boston, Mass: Published by Blackwell Pub. on behalf of the New York Academy of Sciences, 2009.

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Michael, Fromm, and Jörg-Dieter Schulzke. Barriers and channels formed by tight junction proteins. Edited by New York Academy of Sciences. Boston, Mass: Published by Wiley-Blackwell Pub. on behalf of the New York Academy of Sciences, 2012.

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Michael, Fromm. Molecular structure and function of the tight junction: From basic mechanisms to clinical manifestations. Boston, Mass: Published by Blackwell Pub. on behalf of the New York Academy of Sciences, 2009.

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González-Mariscal, Lorenza, ed. Tight Junctions. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97204-2.

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Gonzalez-Mariscal, Lorenza. Tight Junctions. Boston, MA: Springer US, 2006. http://dx.doi.org/10.1007/0-387-36673-3.

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Marcelino, Cereijido, ed. Tight junctions. Boca Raton: CRC Press, 1992.

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Claudins: Methods and protocols. New York: Humana, 2011.

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Martin, Tracey A., and Wen G. Jiang, eds. Tight Junctions in Cancer Metastasis. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6028-8.

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Tight junctions in cancer metastasis. Dordrecht: Springer, 2013.

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Book chapters on the topic "Tight junction"

1

Osanai, Makoto. "Tight Junction." In Encyclopedia of Cancer, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_5814-3.

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Mehlhorn, Heinz. "Tight Junction." In Encyclopedia of Parasitology, 2740. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_4407.

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Mehlhorn, Heinz. "Tight Junction." In Encyclopedia of Parasitology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27769-6_4407-1.

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Osanai, Makoto. "Tight Junction." In Encyclopedia of Cancer, 4544–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_5814.

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Arampatzis, Adamantios, Lida Mademli, Thomas Reilly, Mike I. Lambert, Laurent Bosquet, Jean-Paul Richalet, Thierry Busso, et al. "Tight Junction." In Encyclopedia of Exercise Medicine in Health and Disease, 852. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_3124.

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Osanai, Makoto. "Tight Junction." In Encyclopedia of Cancer, 3694–98. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5814.

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Anderson, James Melvin, and Christina M. Van Itallie. "Tight Junction Channels." In Tight Junctions, 33–42. Boston, MA: Springer US, 2006. http://dx.doi.org/10.1007/0-387-36673-3_3.

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Stamatovic, Svetlana M., Ingolf E. Blasig, Richard F. Keep, and Anuska V. Andjelkovic. "Endocytosis of Tight Junction Proteins: A Pathway for Barrier Remodeling." In Tight Junctions, 299–321. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97204-2_13.

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Naser, Amna N., Tiaosi Xing, Qun Lu, and Yan-Hua Chen. "Non-tight Junction Functions of Claudin Proteins: Roles in Cell-Matrix Interactions and Stem Cell Regulations." In Tight Junctions, 199–215. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97204-2_9.

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Chanez-Paredes, Sandra D., Shabnam Abtahi, Wei-Ting Kuo, and Jerrold R. Turner. "Differentiating Between Tight Junction-Dependent and Tight Junction-Independent Intestinal Barrier Loss In Vivo." In Methods in Molecular Biology, 249–71. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/7651_2021_389.

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Conference papers on the topic "Tight junction"

1

Karakaya, M., R. A. Kerekes, J. L. Morrell-Falvey, C. M. Foster, and S. T. Retterer. "Analysis of tight junction formation and integrity." In 2012 34th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2012. http://dx.doi.org/10.1109/embc.2012.6346776.

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Ding, Gui-Rong, Lian-Bo Qiu, Kang-Chu Li, Xiao-Wu Wang, Yong-Chun Zhou, Yan Zhou, Jun-ye Liu, Yu-Rong Li, and Guo-Zhen Guo. "Alteration of BBB tight junction protein expression induced by EMP exposure." In 2010 Asia-Pacific International Symposium on Electromagnetic Compatibility. IEEE, 2010. http://dx.doi.org/10.1109/apemc.2010.5475732.

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Carson, Johnny L., Albert M. Collier, and Milan J. Hazucha. "Inflammation And Tight Junction Fragmentation In The Nasal Mucosa Of Active Smokers." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1743.

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Cherradi, Sara, Adeline Ayrolles-Torro, Nadia Vezzo-Vié, Eve Combes, Lucile Canterel-Thouennon, Fabien Gava, Valérie Lobjois, Bernard Ducommun, Celine Gongora, and Maguy Del Rio. "Abstract 2902: Targeting the tight junction protein claudin-1 in colorectal cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2902.

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Wang Xiao-Wu, Ding Gui-Rong, Zeng Li-Hua, Liu Xiao-Wei, Miao Xia, Zhao Tao, Zhang Jie, Xie Xue-Jun, Su Xiao-Ming, and Guo Guo-Zhen. "Effects of electromagnetic pulse on the tight junction of mice blood-testis-barrier." In 2008 8th International Symposium on Antennas, Propagation & EM Theory (ISAPE - 2008). IEEE, 2008. http://dx.doi.org/10.1109/isape.2008.4735438.

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Royse, Kathryn E., Liang Chen, Jocelyn Uriostegui, Michael Ittmann, David Y. Graham, Hashem El-Serag, and Li Jiao. "Abstract 4591: Differential expression of tight junction polarity genes in human colon cancer." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4591.

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Ohta, Hiromitsu, Shigeki Chiba, Shu Hisata, Masahito Ebina, and Toshihiro Nukiwa. "Bleomycin - Induced Lung Injury Causes Disturbance Of Tight Junction Of Alveolar Epithelial Cells." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5983.

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Itoh, H., and J. Inoue. "Full tight-binding calculation of TMR for Fe/MgO/Fe junction with randomness." In INTERMAG Asia 2005: Digest of the IEEE International Magnetics Conference. IEEE, 2005. http://dx.doi.org/10.1109/intmag.2005.1463733.

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Bachinger, D., E. Mayer, and K. Teichmann. "Phytogenic Substances in a Model for Intestinal Barrier Function after Tight Junction Disruption." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608297.

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Mosley, Michael, James Knight, Albrecht Neesse, Patrick Michl, Veerle Kersemans, and Bart Cornelissen. "Abstract 4929: Radiolabeled cCPE for molecular imaging of tight junction changes during breast oncogenesis." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4929.

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Reports on the topic "Tight junction"

1

Beeman, Neal E., and Margaret Neville. Role of the Adherens Junction Protein Fascin in the Regulation of Tight Junction Permeability in the Mouse Mammary Gland. Fort Belvoir, VA: Defense Technical Information Center, August 2004. http://dx.doi.org/10.21236/ada436567.

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Beeman, Neal E., and Margaret Neville. Role of the Adherens Junction Protein Fascin in the Regulation of Tight Junction Permeability in the Mouse Mammary Gland. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada397802.

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Beeman, Neal E., and Margaret C. Neville. Role of the Adherens Junction Protein Fascin in the Regulation of Tight Junction Permeability in the Mouse Mammary Gland. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada423862.

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Sukumar, Saraswati. Imaging the Vascular and Metabolic Impact of Claudin-7, a Tight Junction Protein in Transgenic Human Breast Cancer Models. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada410196.

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Katsarou, Spyridoula, Michael Makris, Efstratios Vakirlis, and Stamatios Gregoriou. The role of tight junctions in atopic dermatitis: A systematic review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, January 2023. http://dx.doi.org/10.37766/inplasy2023.1.0012.

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Abstract:
Review question / Objective: The role of tight junctions in atopic dermatitis. Eligibility criteria: Inclusion criteria: Literature from 2009 to 2022, studies written in english. Exclusion criteria: articles focused in diseases other that atopic dermatitis, articles whose full-text version was not available, articles written in language other than English. Main outcome(s): Exploring the crosstalk between TJs and the immune system, in order to develop topical agents that improve TJs functionality. Publication of new data is possible to change our current knowledge as presented in this review in the future, as this is an emerging field.
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