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Journal articles on the topic 'Zonula Occludens Protein 1'

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Published: 4 June 2021
Last updated: 6 February 2022

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1

Németh, Zsuzsanna, Attila Marcell Szász, Áron Somorácz, et al. "Zonula Occludens-1, Occludin, and E-cadherin Protein Expression in Biliary Tract Cancers." Pathology & Oncology Research 15, no. 3 (2009): 533–39. http://dx.doi.org/10.1007/s12253-009-9150-4.

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2

DeMaio, Lucas, Mahsa Rouhanizadeh, Srinivasa Reddy, Alex Sevanian, Juliana Hwang, and Tzung K. Hsiai. "Oxidized phospholipids mediate occludin expression and phosphorylation in vascular endothelial cells." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 2 (2006): H674—H683. http://dx.doi.org/10.1152/ajpheart.00554.2005.

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Oxidized l-α-1-palmitoyl-2-arachidonoyl- sn-glycero-3-phosphorylcholine (OxPAPC), a component of minimally modified LDL, induces production of proinflammatory cytokines and development of atherosclerotic lesions. We tested the hypothesis that OxPAPC alters expression, phosphorylation, and localization of tight junction (TJ) proteins, particularly occludin, a transmembrane TJ protein. OxPAPC reduced total occludin protein and increased occludin phosphorylation dose dependently (10–50 μg/ml) and time dependently in bovine aortic endothelial cells. OxPAPC decreased occludin mRNA and reduced the i
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3

Basuroy, S., P. Sheth, C. M. Mansbach, and R. K. Rao. "Acetaldehyde disrupts tight junctions and adherens junctions in human colonic mucosa: protection by EGF and l-glutamine." American Journal of Physiology-Gastrointestinal and Liver Physiology 289, no. 2 (2005): G367—G375. http://dx.doi.org/10.1152/ajpgi.00464.2004.

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Acetaldehyde, a toxic metabolite of ethanol oxidation, is suggested to play a role in the increased risk for gastrointestinal cancers in alcoholics. In the present study, the effect of acetaldehyde on tyrosine phosphorylation, immmunofluorescence localization, and detergent-insoluble fractions of the tight junction and the adherens junction proteins was determined in the human colonic mucosa. The role of EGF and l-glutamine in prevention of acetaldehyde-induced effects was also evaluated. Acetaldehyde reduced the protein tyrosine phosphatase activity, thereby increasing the tyrosine phosphoryl
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4

Meyer, Tobias N., Catherine Schwesinger, and Bradley M. Denker. "Zonula Occludens-1 Is a Scaffolding Protein for Signaling Molecules." Journal of Biological Chemistry 277, no. 28 (2002): 24855–58. http://dx.doi.org/10.1074/jbc.c200240200.

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5

Ciolofan, C., X. B. Li, C. Olson, et al. "Association of connexin36 and zonula occludens-1 with zonula occludens-2 and the transcription factor zonula occludens-1-associated nucleic acid-binding protein at neuronal gap junctions in rodent retina." Neuroscience 140, no. 2 (2006): 433–51. http://dx.doi.org/10.1016/j.neuroscience.2006.02.032.

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6

Nestorovic, Aleksandra, Jovana Jasnic-Savovic, Georgine Faulkner, Dragica Radojkovic, and Snezana Kojic. "Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1." Archives of Biological Sciences 66, no. 3 (2014): 1233–42. http://dx.doi.org/10.2298/abs1403233n.

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The muscle ankyrin repeat protein Ankrd1 is localized in a mechanosensory complex of the sarcomeric I-band. It is involved in signaling pathways activated in response to mechanical stretch. It also acts as a transcriptional cofactor in the nucleus, playing an important role in cardiogenesis and skeletal muscle differentiation. To investigate its regulatory function in signaling we employed protein array methodology and identified 10 novel Ankrd1 binding partners among PDZ domain proteins known to act as platforms for multiprotein complex assembly. The zonula occludens protein-1 (ZO-1) was chos
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Nielsen, Peter A., Amos Baruch, Valery I. Shestopalov та ін. "Lens Connexins α3Cx46 and α8Cx50 Interact with Zonula Occludens Protein-1 (ZO-1)". Molecular Biology of the Cell 14, № 6 (2003): 2470–81. http://dx.doi.org/10.1091/mbc.e02-10-0637.

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Connexin α1Cx43 has previously been shown to bind to the PDZ domain–containing protein ZO-1. The similarity of the carboxyl termini of this connexin and the lens fiber connexins α3Cx46 and α8Cx50 suggested that these connexins may also interact with ZO-1. ZO-1 was shown to be highly expressed in mouse lenses. Colocalization of ZO-1 with α3Cx46 and α8Cx50 connexins in fiber cells was demonstrated by immunofluorescence and by fracture-labeling electron microscopy but showed regional variations throughout the lens. ZO-1 was found to coimmunoprecipitate with α3Cx46 and α8Cx50, and pull-down experi
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8

Siti Sarah, Che Othman, Norasnieda Md Shukri, Noor Suryani Mohd Ashari, and Kah Keng Wong. "Zonula occludens and nasal epithelial barrier integrity in allergic rhinitis." PeerJ 8 (September 4, 2020): e9834. http://dx.doi.org/10.7717/peerj.9834.

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Allergic rhinitis (AR) is a common disease affecting 400 million of the population worldwide. Nasal epithelial cells form a barrier against the invasion of environmental pathogens. These nasal epithelial cells are connected together by tight junction (TJ) proteins including zonula occludens-1 (ZO-1), ZO-2 and ZO-3. Impairment of ZO proteins are observed in AR patients whereby dysfunction of ZOs allows allergens to pass the nasal passage into the subepithelium causing AR development. In this review, we discuss ZO proteins and their impairment leading to AR, regulation of their expression by Th1
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9

Kurtman, Cengiz, Esra Gümüştepe, Serdağ Demirören, Fatma Firat, Şaban Çakır Gökçe, and Kemal Özbilgin. "INVESTİGATİON OF ZONULA OCCLUDENS-1 PROTEİN LEVEL İN RECTUM TİSSUE AFTER RADİOTHERAPY." International Journal of Research -GRANTHAALAYAH 8, no. 10 (2020): 271–77. http://dx.doi.org/10.29121/granthaalayah.v8.i10.2020.1619.

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The transmembrane protein zonula occludens of rectal tissue has function to prevents the spread of bacterial toxins into the intestinal mucosa and to systemic circulation. But radiotherapy causes ablation of crypt cell proliferation, mitotic catastrophe, and apoptosis leading to gastrointestinal mucositis. We investigated the acute radiation effect on gastrointestinal mucosa of rectum tissue thickness with immunohistochemistry method for zonula occludens-1 (ZO-1) protein in animal model.
 A total of 24 healthy Swiss Albino mice were divided into 4 groups, and except control group the grou
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10

Chen, Bangbin, Renge Bu, and Xuewen Xu. "Expression of Tight Junction Proteins Is Altered in Bladder Cancer." Analytical Cellular Pathology 2020 (November 16, 2020): 1–8. http://dx.doi.org/10.1155/2020/6341256.

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Bladder cancer (BC) is one of the tumors which occur most frequently in urological system, but less is known about the expression of tight junction proteins and its clinical significance in BC. In this study, expression of claudin-4, zonula occludens-1 (ZO-1) and zonula occludens-1 nucleic acid-binding protein (ZONAB), in BC tissues, adjacent nontumor tissue (ANTT), and BC cell lines was examined by Western blotting, semiquantitative RT-PCR, and immunohistochemistry, and then, the clinical significance of these proteins was investigated. The mRNA and protein expression of ZONAB were significan
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11

McNeil, Elizabeth, Christopher T. Capaldo, and Ian G. Macara. "Zonula Occludens-1 Function in the Assembly of Tight Junctions in Madin-Darby Canine Kidney Epithelial Cells." Molecular Biology of the Cell 17, no. 4 (2006): 1922–32. http://dx.doi.org/10.1091/mbc.e05-07-0650.

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Zonula occludens (ZO)-1 was the first tight junction protein to be cloned and has been implicated as an important scaffold protein. It contains multiple domains that bind a diverse set of junction proteins. However, the molecular functions of ZO-1 and related proteins such as ZO-2 and ZO-3 have remained unclear. We now show that gene silencing of ZO-1 causes a delay of ∼3 h in tight junction formation in Madin-Darby canine kidney (MDCK) epithelial cells, but mature junctions seem functionally normal even in the continuing absence of ZO-1. Depletion of ZO-2, cingulin, or occludin, proteins that
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12

Zhang, Bingkun, and Yuming Guo. "Supplemental zinc reduced intestinal permeability by enhancing occludin and zonula occludens protein-1 (ZO-1) expression in weaning piglets." British Journal of Nutrition 102, no. 5 (2009): 687–93. http://dx.doi.org/10.1017/s0007114509289033.

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The present study was carried out to evaluate the pharmacological effect of Zn in diarrhoea in relation to intestinal permeability. Seventy-two weaning piglets, aged 24 d, were allocated to three dietary treatments: (1) control diet without supplemental Zn; (2) control diet supplemented with 2000 mg Zn/kg from ZnO; (3) control diet supplemented with 2000 mg Zn/kg from tetrabasic zinc chloride (TBZC). At the end of a 14 d experiment period, piglets were weighed, feed consumption was measured, and mucosal barrier function was determined using the lactulose/mannitol test. Expression of mucosal ti
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13

Rhett, J. Matthew, Jane Jourdan, and Robert G. Gourdie. "Connexin 43 connexon to gap junction transition is regulated by zonula occludens-1." Molecular Biology of the Cell 22, no. 9 (2011): 1516–28. http://dx.doi.org/10.1091/mbc.e10-06-0548.

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Connexin 43 (Cx43) is a gap junction (GJ) protein widely expressed in mammalian tissues that mediates cell-to-cell coupling. Intercellular channels comprising GJ aggregates form from docking of paired connexons, with one each contributed by apposing cells. Zonula occludens-1 (ZO-1) binds the carboxy terminus of Cx43, and we have previously shown that inhibition of the Cx43/ZO-1 interaction increases GJ size by 48 h. Here we demonstrated that increases in GJ aggregation occur within 2 h (∼Cx43 half-life) following disruption of Cx43/ZO-1. Immunoprecipitation and Duolink protein–protein interact
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14

Yang, Dan-Hong. "Effect of salvianolate on intestinal epithelium tight junction protein zonula occludens protein 1 in cirrhotic rats." World Journal of Gastroenterology 18, no. 47 (2012): 7040. http://dx.doi.org/10.3748/wjg.v18.i47.7040.

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15

Fanning, Alan S., Christina M. Van Itallie, and James M. Anderson. "Zonula occludens-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia." Molecular Biology of the Cell 23, no. 4 (2012): 577–90. http://dx.doi.org/10.1091/mbc.e11-09-0791.

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The structure and function of both adherens (AJ) and tight (TJ) junctions are dependent on the cortical actin cytoskeleton. The zonula occludens (ZO)-1 and -2 proteins have context-dependent interactions with both junction types and bind directly to F-actin and other cytoskeletal proteins, suggesting ZO-1 and -2 might regulate cytoskeletal activity at cell junctions. To address this hypothesis, we generated stable Madin-Darby canine kidney cell lines depleted of both ZO-1 and -2. Both paracellular permeability and the localization of TJ proteins are disrupted in ZO-1/-2–depleted cells. In addi
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16

Wu, Jingshing, Pascal Rowart, Francois Jouret, et al. "Mechanisms involved in AMPK-mediated deposition of tight junction components to the plasma membrane." American Journal of Physiology-Cell Physiology 318, no. 3 (2020): C486—C501. http://dx.doi.org/10.1152/ajpcell.00422.2019.

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AMP-activated protein kinase (AMPK) activation promotes early stages of epithelial junction assembly. AMPK activation in MDCK renal epithelial cells facilitates localization of the junction-associated proteins aPKCζ and Par3 to the plasma membrane and promotes conversion of Cdc42, a key regulator of epithelial polarization and junction assembly, to its active GTP bound state. Furthermore, Par3 is an important regulator of AMPK-mediated aPKCζ localization. Both aPKCζ and Par3 serve as intermediates in AMPK-mediated junction assembly, with inhibition of aPKCζ activity or Par3 knockdown disruptin
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17

Li, Danxi, and Randall J. Mrsny. "Oncogenic Raf-1 Disrupts Epithelial Tight Junctions via Downregulation of Occludin." Journal of Cell Biology 148, no. 4 (2000): 791–800. http://dx.doi.org/10.1083/jcb.148.4.791.

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Occludin is an integral membrane protein of the epithelial cell tight junction (TJ). Its potential role in coordinating structural and functional events of TJ formation has been suggested recently. Using a rat salivary gland epithelial cell line (Pa-4) as a model system, we have demonstrated that occludin not only is a critical component of functional TJs but also controls the phenotypic changes associated with epithelium oncogenesis. Transfection of an oncogenic Raf-1 into Pa-4 cells resulted in a complete loss of TJ function and the acquisition of a stratified phenotype that lacked cell–cell
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18

Kang, Lichun, Long Shen, Liqing Lu, et al. "Asparaginyl endopeptidase induces endothelial permeability and tumor metastasis via downregulating zonula occludens protein ZO-1." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1865, no. 9 (2019): 2267–75. http://dx.doi.org/10.1016/j.bbadis.2019.05.003.

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19

Schmidt, A., D. I. Utepbergenov, S. L. Mueller, et al. "Occludin binds to the SH3-hinge-GuK unit of zonula occludens protein 1: potential mechanism of tight junction regulation." Cellular and Molecular Life Sciences (CMLS) 61, no. 11 (2004): 1354–65. http://dx.doi.org/10.1007/s00018-004-4010-6.

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20

Eadon, Michael T., Bradley K. Hack, Chang Xu, Benjamin Ko, F. Gary Toback, and Patrick N. Cunningham. "Endotoxemia alters tight junction gene and protein expression in the kidney." American Journal of Physiology-Renal Physiology 303, no. 6 (2012): F821—F830. http://dx.doi.org/10.1152/ajprenal.00023.2012.

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Intact tight junctional (TJ) proteins are required for tubular ion transport and waste excretion. Disruption of TJs may contribute to a decreased glomerular filtration rate in acute kidney injury (AKI) via tubular backleak. The effect of LPS-mediated AKI on murine TJs has not been studied extensively. We hypothesized LPS endotoxin administration to mice would disrupt tubular TJ proteins including zonula occludens-1 (ZO-1), occludin, and claudins. ZO-1 and occludin immunofluorescence 24 h post-LPS revealed a marked change in localization from the usual circumferential fencework pattern to one w
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21

Chen, Jie, Lan Xiao, Jaladanki N. Rao, et al. "JunD Represses Transcription and Translation of the Tight Junction Protein Zona Occludens-1 Modulating Intestinal Epithelial Barrier Function." Molecular Biology of the Cell 19, no. 9 (2008): 3701–12. http://dx.doi.org/10.1091/mbc.e08-02-0175.

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The AP-1 transcription factor JunD is highly expressed in intestinal epithelial cells, but its exact role in maintaining the integrity of intestinal epithelial barrier remains unknown. The tight junction (TJ) protein zonula occludens (ZO)-1 links the intracellular domain of TJ-transmembrane proteins occludin, claudins, and junctional adhesion molecules to many cytoplasmic proteins and the actin cytoskeleton and is crucial for assembly of the TJ complex. Here, we show that JunD negatively regulates expression of ZO-1 and is implicated in the regulation of intestinal epithelial barrier function.
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Bal, Manjot Singh, Victor Castro, Jörg Piontek, et al. "The hinge region of the scaffolding protein of cell contacts, zonula occludens protein 1, regulates interacting with various signaling proteins." Journal of Cellular Biochemistry 113, no. 3 (2012): 934–45. http://dx.doi.org/10.1002/jcb.23422.

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23

Song, Li, Shujun Ge, and Joel S. Pachter. "Caveolin-1 regulates expression of junction-associated proteins in brain microvascular endothelial cells." Blood 109, no. 4 (2006): 1515–23. http://dx.doi.org/10.1182/blood-2006-07-034009.

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Abstract Recent evidence from this laboratory indicated that reduced expression of caveolin-1 accompanied the diminished expression of tight junction (TJ)–associated proteins occludin and zonula occludens-1 (ZO-1) following stimulation of brain microvascular endothelial cells (BMECs) with the chemokine CCL2 (formerly called MCP-1). Because attenuated caveolin-1 levels have also been correlated with heightened permeability of other endothelia, the objective of this study was to test the hypothesis that reduced caveolin-1 expression is causally linked to the action of CCL2 on BMEC junctional pro
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Lu, Xiao-Yu, Bing-Chen Liu, Yu-Ze Cao, et al. "High glucose reduces expression of podocin in cultured human podocytes by stimulating TRPC6." American Journal of Physiology-Renal Physiology 317, no. 6 (2019): F1605—F1611. http://dx.doi.org/10.1152/ajprenal.00215.2019.

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The transient receptor potential canonical 6 (TRPC6) channel and podocin are colocalized in the glomerular slit diaphragm as an important complex to maintain podocyte function. Gain of TRPC6 function and loss of podocin function induce podocyte injury. We have previously shown that high glucose induces apoptosis of podocytes by activating TRPC6; however, whether the activated TRPC6 can alter podocin expression remains unknown. Western blot analysis and confocal microscopy were used to examine both expression levels of TRPC6, podocin, and nephrin and morphological changes of podocytes in respon
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Shen, Le, Christopher R. Weber, and Jerrold R. Turner. "The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state." Journal of Cell Biology 181, no. 4 (2008): 683–95. http://dx.doi.org/10.1083/jcb.200711165.

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The tight junction defines epithelial organization. Structurally, the tight junction is comprised of transmembrane and membrane-associated proteins that are thought to assemble into stable complexes to determine function. In this study, we measure tight junction protein dynamics in live confluent Madin–Darby canine kidney monolayers using fluorescence recovery after photobleaching and related methods. Mathematical modeling shows that the majority of claudin-1 (76 ± 5%) is stably localized at the tight junction. In contrast, the majority of occludin (71 ± 3%) diffuses rapidly within the tight j
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Xu, Jianliang, Farhana Anuar, Safiah Mohamed Ali, Mei Yong Ng, Dominic C. Y. Phua, and Walter Hunziker. "Zona Occludens-2 Is Critical for Blood–Testis Barrier Integrity and Male Fertility." Molecular Biology of the Cell 20, no. 20 (2009): 4268–77. http://dx.doi.org/10.1091/mbc.e08-12-1236.

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Tight junction integral membrane proteins such as claudins and occludin are tethered to the actin cytoskeleton by adaptor proteins, notably the closely related zonula occludens (ZO) proteins ZO-1, ZO-2, and ZO-3. All three ZO proteins have recently been inactivated in mice. Although ZO-3 knockout mice lack an obvious phenotype, animals deficient in ZO-1 or ZO-2 show early embryonic lethality. Here, we rescue the embryonic lethality of ZO-2 knockout mice by injecting ZO-2(−/−) embryonic stem (ES) cells into wild-type blastocysts to generate viable ZO-2 chimera. ZO-2(−/−) ES cells contribute ext
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Shimada, Tadayuki, Shin Yasuda, Hiroko Sugiura, and Kanato Yamagata. "Syntenin: PDZ Protein Regulating Signaling Pathways and Cellular Functions." International Journal of Molecular Sciences 20, no. 17 (2019): 4171. http://dx.doi.org/10.3390/ijms20174171.

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Syntenin is an adaptor-like molecule that has two adjacent tandem postsynaptic density protein 95/Discs large protein/Zonula occludens 1 (PDZ) domains. The PDZ domains of syntenin recognize multiple peptide motifs with low to moderate affinity. Many reports have indicated interactions between syntenin and a plethora of proteins. Through interactions with various proteins, syntenin regulates the architecture of the cell membrane. As a result, increases in syntenin levels induce the metastasis of tumor cells, protrusion along the neurite in neuronal cells, and exosome biogenesis in various cell
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Grisendi, Silvia, Monique Arpin, and Tiziana Crepaldi. "Effect of hepatocyte growth factor on assembly of zonula occludens-1 protein at the plasma membrane." Journal of Cellular Physiology 176, no. 3 (1998): 465–71. http://dx.doi.org/10.1002/(sici)1097-4652(199809)176:3<465::aid-jcp3>3.0.co;2-m.

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Huber, Tobias B., Miriam Schmidts, Peter Gerke, et al. "The Carboxyl Terminus of Neph Family Members Binds to the PDZ Domain Protein Zonula Occludens-1." Journal of Biological Chemistry 278, no. 15 (2003): 13417–21. http://dx.doi.org/10.1074/jbc.c200678200.

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Xu, X., K. You, and B. Wu. "Zonula occludens-1 associated nucleic acid binding protein plays an invasion-promoting role in bladder cancer." Neoplasma 66, no. 03 (2019): 405–19. http://dx.doi.org/10.4149/neo_2018_180725n530.

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Remue, Eline, Kris Meerschaert, Tsutomu Oka, et al. "TAZ interacts with zonula occludens-1 and -2 proteins in a PDZ-1 dependent manner." FEBS Letters 584, no. 19 (2010): 4175–80. http://dx.doi.org/10.1016/j.febslet.2010.09.020.

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Hunter, Andrew W., Ralph J. Barker, Ching Zhu, and Robert G. Gourdie. "Zonula Occludens-1 Alters Connexin43 Gap Junction Size and Organization by Influencing Channel Accretion." Molecular Biology of the Cell 16, no. 12 (2005): 5686–98. http://dx.doi.org/10.1091/mbc.e05-08-0737.

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Regulation of gap junction (GJ) organization is critical for proper function of excitable tissues such as heart and brain, yet mechanisms that govern the dynamic patterning of GJs remain poorly defined. Here, we show that zonula occludens (ZO)-1 localizes preferentially to the periphery of connexin43 (Cx43) GJ plaques. Blockade of the PDS95/dlg/ZO-1 (PDZ)-mediated interaction between ZO-1 and Cx43, by genetic tagging of Cx43 or by a membrane-permeable peptide inhibitor that contains the Cx43 PDZ-binding domain, led to a reduction of peripherally associated ZO-1 accompanied by a significant inc
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Tan, Yang, Wei Zhang, Hai-ying Wu, et al. "Effects of emodin on intestinal mucosal barrier by the upregulation of miR-218a-5p expression in rats with acute necrotizing pancreatitis." International Journal of Immunopathology and Pharmacology 34 (January 2020): 205873842094176. http://dx.doi.org/10.1177/2058738420941765.

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Emodin is an effective component in rhubarb to cure intestinal dysfunction, but the specific mechanism remains unknown. This study aimed to evaluate the protective effects of emodin on intestinal dysfunction caused by acute severe pancreatitis and reveal the functional mechanism of emodin in the treatment of this condition. An acute severe pancreatitis model was prepared using taurocholate. In the treatment group, 50 mg/kg emodin was injected intravenously 2 h before the induction of acute severe pancreatitis at an interval of 8 h. After 24 h, the gene expression and protein levels of miR-218a
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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 (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
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Guo, Xin, Jaladanki N. Rao, Lan Liu, et al. "Polyamines are necessary for synthesis and stability of occludin protein in intestinal epithelial cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 6 (2005): G1159—G1169. http://dx.doi.org/10.1152/ajpgi.00407.2004.

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Occludin is an integral membrane protein that forms the sealing element of tight junctions and is critical for epithelial barrier function. Polyamines are implicated in multiple signaling pathways driving different biological functions of intestinal epithelial cells (IEC). The present study determined whether polyamines are involved in expression of occludin and play a role in intestinal epithelial barrier function. Studies were conducted in stable Cdx2-transfected IEC-6 cells (IEC-Cdx2L1) associated with a highly differentiated phenotype. Polyamine depletion by α-difluoromethylornithine (DFMO
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Benedicto, Ignacio, Francisca Molina-Jiménez, Birke Bartosch, et al. "The Tight Junction-Associated Protein Occludin Is Required for a Postbinding Step in Hepatitis C Virus Entry and Infection." Journal of Virology 83, no. 16 (2009): 8012–20. http://dx.doi.org/10.1128/jvi.00038-09.

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ABSTRACT The precise mechanisms regulating hepatitis C virus (HCV) entry into hepatic cells remain unknown. However, several cell surface proteins have been identified as entry factors for this virus. Of these molecules, claudin-1, a tight junction (TJ) component, is considered a coreceptor required for HCV entry. Recently, we have demonstrated that HCV envelope glycoproteins (HCVgp) promote structural and functional TJ alterations. Additionally, we have shown that the intracellular interaction between viral E2 glycoprotein and occludin, another TJ-associated protein, could be the cause of the
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Chen, Min, Huan Cai, Jun-Ling Yang, et al. "Effect of Heat Stress on Expression of Junction-Associated Molecules and Upstream Factors Androgen Receptor and Wilms’ Tumor 1 in Monkey Sertoli Cells." Endocrinology 149, no. 10 (2008): 4871–82. http://dx.doi.org/10.1210/en.2007-1093.

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Sertoli cells are important in determining the fate of spermatogenic cells by providing nutrition and structural support via cell junctions. In this study, we sought to examine the effect of 43 C warming on cell junctions in seminiferous epithelium and the expression of junction-associated molecules in Sertoli cells. Electron microscopy showed the appearance of large vacuoles between Sertoli and germ cells and adjacent Sertoli cells, leading to disruption of corresponding cell junctions 24 h after terminating the heat treatment. Using primary Sertoli cells isolated from pubertal monkey testes,
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Hiroaki, Hidekazu, Kaori Satomura, Natsuko Goda, et al. "Spatial Overlap of Claudin- and Phosphatidylinositol Phosphate-Binding Sites on the First PDZ Domain of Zonula Occludens 1 Studied by NMR." Molecules 23, no. 10 (2018): 2465. http://dx.doi.org/10.3390/molecules23102465.

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Background: The tight junction is an intercellular adhesion complex composed of claudins (CLDs), occludin, and the scaffolding proteins zonula occludens 1 (ZO-1) and its two paralogs ZO-2 and ZO-3. ZO-1 is a multifunctional protein that contains three PSD95/Discs large/ZO-1(PDZ) domains. A key functional domain of ZO-1 is the first PDZ domain (ZO-1(PDZ1)) that recognizes the conserved C-termini of CLDs. Methods: In this study, we confirmed that phosphoinositides bound directly to ZO-1(PDZ1) by biochemical and solution NMR experiments. We further determined the solution structure of mouse ZO-1(
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Qin, Lan-hui, Wen Huang, Xue-an Mo, Yan-lan Chen, and Xiang-hong Wu. "LPS Induces Occludin Dysregulation in Cerebral Microvascular Endothelial Cells via MAPK Signaling and Augmenting MMP-2 Levels." Oxidative Medicine and Cellular Longevity 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/120641.

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Disrupted blood-brain barrier (BBB) integrity contributes to cerebral edema during central nervous system infection. The current study explored the mechanism of lipopolysaccharide- (LPS-) induced dysregulation of tight junction (TJ) proteins. Human cerebral microvascular endothelial cells (hCMEC/D3) were exposed to LPS, SB203580 (p38MAPK inhibitor), or SP600125 (JNK inhibitor), and cell vitality was determined by MTT assay. The proteins expressions of p38MAPK, JNK, and TJs (occludin and zonula occludens- (ZO-) 1) were determined by western blot. The mRNA levels of TJ components and MMP-2 were
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Gumbiner, B. "Structure, biochemistry, and assembly of epithelial tight junctions." American Journal of Physiology-Cell Physiology 253, no. 6 (1987): C749—C758. http://dx.doi.org/10.1152/ajpcell.1987.253.6.c749.

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The zonula occludens (ZO), also referred to as the tight junction, forms the barrier to the diffusion of molecules and ions across the epithelial cell layer through the paracellular space. The level of electrical resistance of the paracellular pathway seems to depend on the number of strands in the ZO observed by freeze-fracture electron microscopy (EM). The ZO also forms the boundary between the compositionally distinct apical and basolateral plasma membrane domains because it is a barrier to the lateral diffusion of lipids and membrane proteins that reside in the extracytoplasmic leaflet of
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Decaens, C., and D. Cassio. "Spatiotemporal expression of catenins, ZO-1, and occludin during early polarization of hepatic WIF-B9 cells." American Journal of Physiology-Cell Physiology 280, no. 3 (2001): C527—C539. http://dx.doi.org/10.1152/ajpcell.2001.280.3.c527.

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WIF-B9 is a suitable model for in vitro studies of hepatocyte polarity. To better understand polarity establishment, we have localized key proteins of the adhesion system, cytoskeleton, and tight junctions soon after plating, when most cells are isolated or in doublets. In isolated attached cells, only cytoskeletal proteins (tubulin, cytokeratins) displayed a precise localization. As soon as two cells formed a doublet, E-cadherin, α-, β-, and γ-catenins, and p120 protein were present at the doublet contiguous membrane. Actin, ezrin, and zonula occludens-1 (ZO-1) colocalized at this membrane, b
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Bilal, Sahar, Shirin Jaggi, Danielle Janosevic, et al. "ZO-1 protein is required for hydrogen peroxide to increase MDCK cell paracellular permeability in an ERK 1/2-dependent manner." American Journal of Physiology-Cell Physiology 315, no. 3 (2018): C422—C431. http://dx.doi.org/10.1152/ajpcell.00185.2017.

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Hydrogen peroxide (H2O2) increases paracellular permeability of Madin-Darby canine kidney (MDCK) cells, but the mechanism mediating this effect remains unclear. Treatment of MDCK cells with H2O2 activated ERK 1/2. Inhibition of ERK 1/2 activation blocked the ability of H2O2 to increase paracellular permeability. Knockdown of zonula occludens-1 (ZO-1) protein but not occludin eliminated the ability of H2O2 to increase paracellular permeability. H2O2 treatment did not, however, affect the total cell content or contents of the Triton X-100-soluble and -insoluble fractions for occludin, ZO-1, or Z
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Strauss, Randy E., Louisa Mezache, Rengasayee Veeraraghavan та Robert G. Gourdie. "The Cx43 Carboxyl-Terminal Mimetic Peptide αCT1 Protects Endothelial Barrier Function in a ZO1 Binding-Competent Manner". Biomolecules 11, № 8 (2021): 1192. http://dx.doi.org/10.3390/biom11081192.

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The Cx43 carboxyl-terminus (CT) mimetic peptide, αCT1, originally designed to bind to Zonula Occludens 1 (ZO1) and thereby inhibit Cx43/ZO1 interaction, was used as a tool to probe the role of Cx43/ZO1 association in regulation of epithelial/endothelial barrier function. Using both in vitro and ex vivo methods of barrier function measurement, including Electric Cell-Substrate Impedance Sensing (ECIS), a TRITC-dextran Transwell permeability assay, and a FITC-dextran cardiovascular leakage protocol involving Langendorff-perfused mouse hearts, αCT1 was found to protect the endothelium from thromb
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Lee, Min Joung, Yunseon Jang, Jiebo Zhu, et al. "Auraptene Enhances Junction Assembly in Cerebrovascular Endothelial Cells by Promoting Resilience to Mitochondrial Stress through Activation of Antioxidant Enzymes and mtUPR." Antioxidants 10, no. 3 (2021): 475. http://dx.doi.org/10.3390/antiox10030475.

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Junctional proteins in cerebrovascular endothelial cells are essential for maintaining the barrier function of the blood-brain barrier (BBB), thus protecting the brain from the infiltration of pathogens. The present study showed that the potential therapeutic natural compound auraptene (AUR) enhances junction assembly in cerebrovascular endothelial cells by inducing antioxidant enzymes and the mitochondrial unfolded protein response (mtUPR). Treatment of mouse cerebrovascular endothelial cells with AUR enhanced the expression of junctional proteins, such as occludin, zonula occludens-1 (ZO-1)
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Saitou, Mitinori, Kazushi Fujimoto, Yoshinori Doi, et al. "Occludin-deficient Embryonic Stem Cells Can Differentiate into Polarized Epithelial Cells Bearing Tight Junctions." Journal of Cell Biology 141, no. 2 (1998): 397–408. http://dx.doi.org/10.1083/jcb.141.2.397.

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Occludin is the only known integral membrane protein of tight junctions (TJs), and is now believed to be directly involved in the barrier and fence functions of TJs. Occludin-deficient embryonic stem (ES) cells were generated by targeted disruption of both alleles of the occludin gene. When these cells were subjected to suspension culture, they aggregated to form simple, and then cystic embryoid bodies (EBs) with the same time course as EB formation from wild-type ES cells. Immunofluorescence microscopy and ultrathin section electron microscopy revealed that polarized epithelial (visceral endo
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Khan-Dawood, F. S., J. Yang, and M. Y. Dawood. "Localization and expression of zonula occludens-1 tight junction-associated protein in baboon (Papio anubis) corpora lutea." Human Reproduction 11, no. 6 (1996): 1262–67. http://dx.doi.org/10.1093/oxfordjournals.humrep.a019369.

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Siu, Erica R., Elissa W. P. Wong, Dolores D. Mruk, K. L. Sze, Catarina S. Porto, and C. Yan Cheng. "An Occludin-Focal Adhesion Kinase Protein Complex at the Blood-Testis Barrier: A Study Using the Cadmium Model." Endocrinology 150, no. 7 (2009): 3336–44. http://dx.doi.org/10.1210/en.2008-1741.

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Several integral membrane proteins that constitute the blood-testis barrier (BTB) in mammalian testes, in particular rodents, are known to date. These include tight junction (TJ) proteins (e.g. occludin, junctional adhesion molecule-A, claudins), basal ectoplasmic specialization proteins (e.g. N-cadherin), and gap junction proteins (e.g. connexin43). However, the regulators (e.g. protein kinases and phosphatases) that affect these proteins, such as their interaction with the cytoskeletal actin, which in turn confer cell adhesion at the TJ, remain largely unknown. We report herein that focal ad
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Capaldo, Christopher T., Stefan Koch, Michael Kwon, Oskar Laur, Charles A. Parkos, and Asma Nusrat. "Tight function zonula occludens-3 regulates cyclin D1–dependent cell proliferation." Molecular Biology of the Cell 22, no. 10 (2011): 1677–85. http://dx.doi.org/10.1091/mbc.e10-08-0677.

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Coordinated regulation of cell proliferation is vital for epithelial tissue homeostasis, and uncontrolled proliferation is a hallmark of carcinogenesis. A growing body of evidence indicates that epithelial tight junctions (TJs) play a role in these processes, although the mechanisms involved are poorly understood. In this study, we identify and characterize a novel plasma membrane pool of cyclin D1 with cell-cycle regulatory functions. We have determined that the zonula occludens (ZO) family of TJ plaque proteins sequesters cyclin D1 at TJs during mitosis, through an evolutionarily conserved c
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Choi, Wangsun, Bipul R. Acharya, Grégoire Peyret, et al. "Remodeling the zonula adherens in response to tension and the role of afadin in this response." Journal of Cell Biology 213, no. 2 (2016): 243–60. http://dx.doi.org/10.1083/jcb.201506115.

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Morphogenesis requires dynamic coordination between cell–cell adhesion and the cytoskeleton to allow cells to change shape and move without losing tissue integrity. We used genetic tools and superresolution microscopy in a simple model epithelial cell line to define how the molecular architecture of cell–cell zonula adherens (ZA) is modified in response to elevated contractility, and how these cells maintain tissue integrity. We previously found that depleting zonula occludens 1 (ZO-1) family proteins in MDCK cells induces a highly organized contractile actomyosin array at the ZA. We find that
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Muthusamy, Arivalagan, Cheng-Mao Lin, Sumathi Shanmugam, Heather M. Lindner, Steven F. Abcouwer, and David A. Antonetti. "Ischemia–Reperfusion Injury Induces Occludin Phosphorylation/Ubiquitination and Retinal Vascular Permeability in a VEGFR-2-Dependent Manner." Journal of Cerebral Blood Flow & Metabolism 34, no. 3 (2014): 522–31. http://dx.doi.org/10.1038/jcbfm.2013.230.

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Retinal ischemia–reperfusion (IR) induces neurodegenaration as well as blood–retinal barrier (BRB) breakdown causing vascular permeability. Whereas the neuronal death has been extensively studied, the molecular mechanisms related to BRB breakdown in IR injury remain poorly understood. In this study, we investigated the early changes in tight junctional (TJ) proteins in response to IR injury. Ischemia–reperfusion injury was induced in male rat retinas by increasing the intraocular pressure for 45 minutes followed by natural reperfusion. The results demonstrate that IR injury induced occludin Se
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