| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.69334839 |
| Characterization of ZO 2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin . 0.69334839^^^ Consistently , occludin as well as alpha catenin directly bound to N ZO 2 as well as the NH 2 terminal dlg like portion of ZO 1 ( N ZO 1 ) in vitro . 0.57424574^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :1.0424975 |
| Exploration of other tight junction protein interactions demonstrated that ZO 2 binds directly to both ZO 1 and occludin . 1.0424975^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Immunoblot analysis revealed that overexpression of claudin 1 increased expression of ZO 1 but not of occludin or ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The effect on occludin was specific because other tight junction components , ZO 1 , ZO 2 , cingulin , and the adherens junction protein E cadherin , were unaltered by OCC 2 treatment . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Tight junctions are mediated by molecules such as occludin and its associated ZO 1 and ZO 2 , and adherens junctions are mediated by adhesion molecules such as cadherin and its associated catenins . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| In vitro affinity analyses demonstrated that recombinant 130 kD protein directly interacts with ZO 1 and the cytoplasmic domain of occludin , but not with ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The intercellular barrier is formed by rows of the transmembrane protein occludin , which is bound on the cytoplasmic surface to ZO 1 and ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Subcellular distribution of tight junction associated proteins ( occludin , ZO 1 , ZO 2 ) in rodent skin . ^^^ In this study , we investigated the expression and subcellular distribution of occludin , ZO 1 , and ZO 2 in rodent skin . ^^^ Immunoblotting detected all of these molecules in isolated epidermis , but the occludin / ZO 1 ( or occludin / ZO 2 ) ratio was significantly lower than that in cultured simple epithelial cells . ^^^ In the epidermis of adult skin , occludin was concentrated at cell cell borders only in the most superficial zone of the granular cell layer , whereas ZO 1 and ZO 2 were distributed in a much broader zone from the spinous to the granular layers . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| ZO 1 has been demonstrated to interact with the transmembrane protein occludin , a second tight junction specific MAGUK , ZO 2 , and F actin , although the nature and functional significance of these interactions is poorly understood . ^^^ To further elucidate the role of ZO 1 within the epithelial tight junction , we have introduced epitope tagged fragments of ZO 1 into cultured MDCK cells and identified domains critical for the interaction with ZO 2 , occludin , and F actin . ^^^ A combination of in vitro and in vivo binding assays indicate that both ZO 2 and occludin interact with specific domains within the N terminal ( MAGUK like ) half of ZO 1 , whereas the unique proline rich C terminal half of ZO 1 cosediments with F actin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Specifically , IFN gamma treatment resulted in an almost total loss of zonula occludens ( ZO ) 1 , whereas the levels of ZO 2 and occludin showed relatively modest decreases compared with untreated cells . ^^^ Loss of ZO 1 was associated with the altered localization of ZO 2 and occludin . ^^^ In IFN gamma treated cells , ZO 2 and occludin were diffusely distributed , whereas , in control cells , they , along with ZO 1 , were predominantly localized to the tight junctions . ^^^ In contrast to ZO 1 , ZO 2 and occludin did not show any major changes in these parameters . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| These changes reversed after ATP repletion , and the movement of insoluble occludin , ZO 1 , and ZO 2 back into the soluble pool was again via a genistein sensitive mechanism . ^^^ Furthermore , during the ATP repletion phase , tyrosine phosphorylation of Triton 10 100 insoluble occludin , which is localized at the junction , as well as ZO 2 , p130 / ZO 3 ( though not ZO 1 ) , and other proteins was evident ; this tyrosine phosphorylation was completely inhibited by genistein . ^^^ This indicates that tyrosine kinase activity is necessary for TJ reassembly during ATP repletion and suggests an important role for the tyrosine phosphorylation of occludin , ZO 2 , p130 / ZO 3 , and possibly other proteins in the processes involved in TJ ( re ) formation . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| These results suggest an important role for cytoplasmic proteins , presumably ZO 1 , ZO 2 , and ZO 3 , in localizing occludin in tight junction fibrils . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Immunofluorescence microscopy and immunoblot analysis showed that activated PMN adhesion to resting monolayers or PMN migration across interleukin 1 treated monolayers does not result in widespread proteolytic loss of TJ proteins ( ZO 1 , ZO 2 , and occludin ) from endothelial borders . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| TJ strands are mainly composed of two distinct types of four transmembrane proteins , occludin , and claudins , between which occludin was reported to directly bind to ZO 1 / ZO 2 / ZO 3 . ^^^ However , in occludin deficient intestinal epithelial cells , ZO 1 / ZO 2 / ZO 3 were still recruited to TJs . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Many ubiquitous molecular constituents of tight junctions have been identified and characterized including claudins , occludin , ZO 1 , ZO 2 , ZO 3 , cingulin , and 7H6 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Cocultures were analyzed for paracellular permeability by measurement of transepithelial electrical resistance ( TER ) and for the tight junction proteins ZO 1 , ZO 2 , occludin , and cingulin by immunocytochemistry and immunoprecipitation . ^^^ Immunoprecipitation of cocultures revealed dephosphorylation of ZO 2 , loss of ZO 1 from ZO 2 , and degradation of ZO 1 but less so of ZO 2 and none of occludin or E cadherin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Tight junction proteins ZO 1 , ZO 2 , and occludin along isolated renal tubules . ^^^ The differential expression of three tight junction proteins , ZO 1 , ZO 2 , and occludin , along isolated rabbit renal tubules is examined in this article . ^^^ METHODS : Microdissected rabbit renal tubules were processed for immunofluorescence detection of ZO 1 , ZO 2 , and occludin . ^^^ The quantity of ZO 2 and occludin present at the distal region was significantly higher compared with the proximal segment . ^^^ CONCLUSIONS : The distribution of ZO 1 , ZO 2 , and occludin follows the increase in junction complexity encountered in renal tubules . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Human gastric epithelial cells were isolated from samples of human gastric lining and immortalized with simian virus 40 ( SV 40 ) to generate the stable human gastric epithelial cell line `` JOK l . ' ' These cells express conventional epithelial markers ( vimentin , cytokeratin 18 , occludin , N and E cadherins , beta catenin , ZO 1 , ZO 2 , mucin , epithelial specific antigen ) as well as SV 40 large T antigen . ^^^ In contrast , the kidney epithelial cell line `` MDCK ' ' also expresses several epithelial markers ( vimentin , cytokeratin 18 , occludin , N and E cadherin , beta catenin , ZO 1 , ZO 2 , epithelial specific antigen ) , but does not express mucin , or large T antigen . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Using a yeast two hybrid system , immunocolocalization , immunoprecipitation , and in vitro binding studies , we found that two 4 . 1R isoforms of 135 and 150 kDa specifically interact with the protein ZO 2 ( zonula occludens 2 ) . 4 . 1R is colocalized with ZO 2 and occludin at Madin Darby canine kidney ( MDCK ) cell tight junctions . ^^^ Both isoforms of 4 . 1R coprecipitated with proteins that organize tight junctions such as ZO 2 , ZO 1 , and occludin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Removal of calcium from the culture media of the epithelial cells resulted in disruption of the TJs , characterised by a loss of membrane association of the TJ associated proteins occludin , ZO 1 and ZO 2 , by a loss of TJ strands , by a marked decrease in the transepithelial electrical resistance and by a dramatic increase in the transepithelial permeability to tracers . ^^^ The association of occludin , ZO 1 and ZO 2 with the actin cytoskeleton is not affected . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The tight junction components ZO 1 , ZO 2 , endogenous ZO 3 , and occludin were mislocalized during the early stages of tight junction assembly . ^^^ NZO 3 expression did not alter expression levels of ZO 1 , ZO 2 , endogenous ZO 3 , occludin , or E cadherin ; however , the amount of Triton 10 100 soluble , signaling active beta catenin was increased in NZO 3 expressing cells during junction assembly . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| PURPOSE : To investigate the expression and cellular distribution of putative tight junction ( TJ ) proteins occludin , ZO 1 , ZO 2 , and claudin 1 in rat corneal epithelium and alterations of TJs in cultured human corneal epithelial cells in response to lipopolysaccharide ( LPS ) challenge . ^^^ METHODS : Immunohistochemistry was used to determine tissue distribution of occludin , ZO 1 , ZO 2 , and claudin 1 in the rat cornea . ^^^ Immunocytochemistry and immunoblotting were used to assess alteration in the levels and localization of TJ associated proteins occludin , ZO 1 , and ZO 2 in LPS treated THCE cells . ^^^ RESULTS : Occludin , ZO 1 , and ZO 2 were found at the cell borders of the superficial layer , whereas claudin 1 was localized mainly in the basal and wing cell layers of rat corneal epithelium . ^^^ CONCLUSIONS : Occludin , ZO 1 , and ZO 2 , but not claudin 1 , are components of corneal epithelial TJs . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| IL 15 mediated up regulation of ZO 1 and ZO 2 expression was independent of the IL 2Rbeta subunit , whereas the phosphorylation of occludin and enhanced membrane association of claudin 1 and claudin 2 by IL 15 required the presence of the IL 2Rbeta subunit . ^^^ Recruitment of claudins and hyperphosphorylated occludin into tight junctions resulted in a more marked induction of tight junction formation in intestinal epithelial cells than the up regulation of ZO 1 and ZO 2 by itself . ^^^ The regulation of the intestinal epithelial barrier function by IL 15 involves IL 2Rbeta dependent and independent signaling pathways leading to the recruitment of claudins , hyperphosphorylated occludin , ZO 1 , and ZO 2 into the tight junctional protein complex . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| We show that these compounds promote the differentiation of human colon carcinoma SW 480 cells expressing vitamin D receptors ( VDRs ) ( SW 480 ADH ) but not that of a malignant subline ( SW 480 R ) or metastasic derivative ( SW 620 ) cells lacking VDR . 1alpha , 25 ( OH ) 2D ( 3 ) induced the expression of E cadherin and other adhesion proteins ( occludin , Zonula occludens [ ZO ] 1 , ZO 2 , vinculin ) and promoted the translocation of beta catenin , plakoglobin , and ZO 1 from the nucleus to the plasma membrane . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| During this time period , toxin exposure did not induce translocation of ZO 2 , dephosphorylation or translocation of occludin , or cell rounding . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Both integral ( claudin 1 and occludin ) and membrane associated zonula occluden 1 and 2 ( ZO 1 and ZO 2 ) proteins combine to form these TJ complexes that are anchored to the cytoskeletal architecture ( actin ) . ^^^ Furthermore , immunofluorescence studies showed alterations in occludin , ZO 1 , and ZO 2 protein localization during hypoxia and posthypoxic reoxygenation that correlate with the observed changes in BBMEC permeability . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| S . flexneri serotype 2a and 5 , but not the non invasive Escherichia coli strain F 18 , share the ability to regulate expression of ZO 1 , ZO 2 , E cadherin and to dephosphorylate occludin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The PLC gamma inhibitor , 3 NC , but not the inactive analog , 7 OH 3 NC , caused hyperphosphorylation of the tight junction proteins , occludin , ZO 1 , and ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| In the present work we demonstrate that heterotypic TJs in mixed monolayers of MDCK cells with a different cell type ( LLC PK 1 ) are true TJs through several criteria , such as TER , the ability to stop the membrane diffusion of fluorescent sphingomyelin from the apical to the lateral domain , the presence of ZO 1 , ZO 2 , occludin , claudin 1 and claudin 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| This process is accompanied by increased junctional localization and cytoskeletal association of the adherens junctional plakoglobin and the tight junction associated proteins ZO 1 , ZO 2 , and occludin . ^^^ Plakoglobin , ZO 1 , ZO 2 , and occludin showed increased junctional localization when 10T1 / 2 cells were present . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Dynamic assembly of tight junction associated proteins ZO 1 , ZO 2 , ZO 3 and occludin during mouse tooth development . ^^^ In order to address these questions , we have studied the distribution pattern of the tight junction associated proteins ZO 1 , ZO 2 , ZO 3 and occludin in the developing mouse tooth as a model . ^^^ The occurrence and relation during tooth development of tight junction proteins ZO 1 , ZO 2 and occludin , but not ZO 3 , suggests a combinatory assembly in tooth morphogenesis and cell differentiation . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Many ubiquitous molecular tight junction components have been identified and characterized including claudins , occludin , ZO 1 , ZO 2 , ZO 3 , cingulin and 7H6 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation of occludin attenuates its interactions with ZO 1 , ZO 2 , and ZO 3 . ^^^ While the homotypic interaction of extracellular loops of occludin appears to determine the barrier function of tight junction , the intracellular C terminal tail , C occludin , interacts with other tight junction proteins such as ZO 1 , ZO 2 , and ZO 3 and with the actin filaments of cytoskeleton . ^^^ The effect of tyrosine phosphorylation of C occludin on its ability to bind ZO 1 , ZO 2 , ZO 3 , and F actin was evaluated . ^^^ Results show that the amounts of ZO 1 , ZO 2 , and ZO 3 bound to tyrosine phosphorylated C occludin were several fold less than the amounts bound to non phosphorylated C occludin . ^^^ These results demonstrate that tyrosine phosphorylation of occludin reduces its ability to bind ZO 1 , ZO 2 , and ZO 3 , but not F actin . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The results suggest that enhanced epithelial barrier function induced by bryostatin 1 involves a PKC epsilon dependent signaling pathway leading to recruitment of claudin 1 and ZO 2 , and phosphorylation of occludin , into the tight junctional complex . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Expression of the various genes throughout human preimplantation development showed differing levels of sensitivity of detection ; these genes included claudin 1 , occludin ( TM4+ and TM 4 isoforms ) , ZO 1 ( ZO 1alpha+ and ZO 1alpha isoforms ) , ZO 2 and JAM ( junction adhesion molecule ) , and the desmosome junction gene , DSC 2 ( desmocollin 2 ) . ^^^ Some transcripts appeared to be expressed throughout preimplantation development ( claudin 1 , JAM , occludin TM4+ and TM 4 , ZO 1alpha isoform ) while others tended to be expressed preferentially in later cleavage and associated with blastocyst formation ( ZO 2 , ZO 1alpha+ isoform , DSC 2 ) , illustrating an expression pattern broadly similar to mouse cleavage stages . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Calpeptin treatment of MDCK cells resulted in a displacement of zonula occludens 1 ( ZO 1 ) and occludin from cell cell junctions and a loss of phosphotyrosine on ZO 1 and ZO 2 , without any detectable effect on tight junction permeability . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Expression of the TJ proteins , zonula occludens ( ZO ) 1 , ZO 2 , ZO 3 , and occludin , as assessed by immunoblotting and / or immunofluorescence , decreased in lung after the injection of mice with LPS . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Immunoblotting revealed decreased expression of zonula occludens ( ZO ) 1 , ZO 2 , ZO 3 , and occludin in liver after injection of C57Bl / 6J mice with 2 mg / kg Escherichia coli 0111 : B 4 LPS . ^^^ |
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| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| We showed here that cAMP increased gene expression of claudin 5 and decreased that of claudin 1 in porcine blood brain barrier endothelial cells via protein kinase A ( PKA ) independent and dependent pathways , respectively . cAMP also enhanced immunoreactivity of claudin 5 along cell borders and in the cytoplasm , reorganized actin filaments , and altered signals of claudin 5 , occludin , ZO 1 , and ZO 2 along cell boundaries from zipperlike to linear patterns . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| MCP 1 induces reorganization of actin cytoskeleton ( stress fiber formation ) and redistribution of tight junction proteins , ZO 1 , ZO 2 occludin and claudin 5 , from the Triton 10 100 soluble to the Triton 10 100 insoluble fractions . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Strikingly , opening of the endothelial TJs was not accompanied by any visible change in the molecular composition of endothelial TJs as junctional localization of the TJ associated proteins claudin 3 , claudin 5 , occludin , ZO 1 or ZO 2 or the adherens junction associated proteins beta catenin or p120cas did not change . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Paralleling hypoxia and VEGF induced permeability changes , localization of the tight junction proteins occludin , zonula occludens 1 ( ZO 1 ) , and ZO 2 along the cell membrane changed from a continuous to a more discontinuous expression pattern during hypoxia . ^^^ In particular , localization of ZO 1 and ZO 2 expression moved from the cell membrane to the cytoplasm and nucleus whereas occludin expression remained at the cell membrane . ^^^ |
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| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Immunoblotting of total protein and NP 40 insoluble proteins revealed decreased expression and decreased TJ localization , respectively , of the TJ proteins , zonula occludens ( ZO ) 1 , ZO 2 , ZO 3 , and / or occludin in ileal mucosa and colonic mucosa ( total protein only ) after injection of C57B1 / 6J mice with LPS . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| In good agreement , by immunofluorescence microscopy , most TJ proteins including claudins and occludin appeared to be normally concentrated at TJs of ZO 1 / cells with the exception that a ZO 1 deficiency significantly up or down regulated the recruitment of ZO 2 and cingulin , another TJ scaffold protein , respectively , to TJs . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| In contrast to claudins , localization of other tight junction proteins , zonula occludens ( ZO ) 1 , ZO 2 , and occludin , was not sensitive to HFL cell phenotype . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| In hetero and homozygous ( + / and / ) embryoid bodies , immunoblotting revealed a Triton soluble , truncated form of cingulin , increased levels of the tight junction proteins ZO 2 , occludin , claudin 6 and Lfc , and decreased levels of ZO 1 . ^^^ |
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| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| We find that the HDAC inhibitor sodium butyrate significantly up regulates the protein levels of cingulin , ZO 1 , and ZO 2 in Rat 1 fibroblasts , cingulin in COS 7 cells , and cingulin and occludin in HeLa cells . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| At the cellular level , MCP 1 causes alteration of tight junction ( TJ ) proteins in endothelial cells ( redistribution of TJ proteins determined by Western blotting and loss of immunostaining for occludin , claudin 5 , ZO 1 , ZO 2 ) . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Also , gp 120 proteins caused disruption and downregulation of the tight junction proteins ZO 1 , ZO 2 , and occludin in these cells . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Paracellular permeability changes by H2O2 correlated to changes of the localization of the tight junction ( TJ ) proteins occludin , zonula occludens 1 ( ZO 1 ) , and zonula occludens 2 ( ZO 2 ) which were prevented by blocking the p44 / p42 MAP kinase activation . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The colonic epithelial barrier was morphologically altered and expression of mRNA encoding tight junction proteins ZO 2 and occludin was decreased . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| Depletion of ZO 2 , cingulin , or occludin , proteins that can interact with ZO 1 , had no discernible effects on tight junctions . ^^^ These data reveal an unexpected function for the SH 3 domain of ZO 1 in regulating tight junction assembly in epithelial cells and show that cingulin , occludin , or ZO 2 are not limiting for junction assembly in MDCK monolayers . . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The present study used cultured brain endothelial cells to examine the signaling networks involved in the redistribution of TJ proteins ( occludin , ZO 1 , ZO 2 , claudin 5 ) by CCL 2 . ^^^ The CCL 2 induced alterations in the brain endothelial barrier were associated with de novo Ser / Thr phosphorylation of occludin , ZO 1 , ZO 2 , and claudin 5 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| This domain , as expressed in a bacterial system or isolated from native cellular occludin , maintains its ability to bind ZO 1 and ZO 2 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| TJ proteins identified include transmembrane proteins ; occludin and claudin , and cytoplasmic plaque proteins ; ZO 1 , ZO 2 , ZO 3 , cingulin , and 7H6 . ^^^ |
|
| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| The transmembrane tight junction proteins occludin , claudin 1 and claudin 5 , as well as the cytoplasmic accessory proteins ZO 1 and ZO 2 displayed a continuous distribution at cell boundaries . ^^^ Abeta 1 42 treatment altered also protein expression : occludin was lower at 1st day , claudin 1 increased at all times , and ZO 2 increased after 1 day and then decreased . ^^^ |
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| Interacting proteins: Q9UDY2 and Q16625 |
Pubmed |
SVM Score :0.0 |
| While molecular expression of junctional adhesion molecule ( JAM ) , ZO 2 , ZO 3 , claudin 2 and claudin 3 were unaltered , ZO 1 , occludin , and claudin 4 were all up regulated ( 1 . 6 , 1 . 6 , 2 . 4 fold , respectively ; P < 0 . 001 0 . 01 ) and claudin 1 down regulated ( 2 . 5 fold ; P < 0 . 05 ) by trans 10 , cis 12 CLA , which may underpin its effects on tight junction function and paracellular Ca transport . ^^^ |
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