Increased tyrosine phosphorylation causes redistribution of adherens junction and tight junction proteins and perturbs paracellular barrier function in MDCK epithelia

dc.creatorCollares-Buzato, CB
dc.creatorJepson, MA
dc.creatorSimmons, NL
dc.creatorHirst, BH
dc.date1998
dc.dateJUN
dc.date2014-12-02T16:26:39Z
dc.date2015-11-26T17:28:31Z
dc.date2014-12-02T16:26:39Z
dc.date2015-11-26T17:28:31Z
dc.date.accessioned2018-03-29T00:15:39Z
dc.date.available2018-03-29T00:15:39Z
dc.identifierEuropean Journal Of Cell Biology. Gustav Fischer Verlag, v. 76, n. 2, n. 85, n. 92, 1998.
dc.identifier0171-9335
dc.identifierWOS:000074550800001
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60041
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/60041
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60041
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1285075
dc.descriptionPolarized monolayers of strain IT Madin-Darby canine kidney cells (MDCK II) were treated with vanadate/H2O2, known inhibitors of protein tyrosine phosphatase activity. Vanadate/H2O2 treatment resulted in a rapid increase in paracellular permeability as revealed by decreased transepithelial resistance and increased permeability to inulin. These alterations in epithelial barrier function coincided with increased phosphotyrosine immunoflourescence in the vicinity of intercellular junctions and with redistribution of F-actin, the adherens junction protein E-cadherin and the tight junction protein ZO-1. The effects of vanadate/H2O2 on intercellular junction permeability and protein distribution were completely blocked by the specific protein tyrosine kinase (PTK) inhibitor tyrphostin 25 and partially inhibited by the alternative PTK inhibitor genistein. The relative potency of these two inhibitors in blocking the effects of vanadate/H2O2 on intercellular junctions correlated with their abilities to inhibit tyrosine phosphorylation. The patent ser/thr protein kinase inhibitor staurosporine had only a small influence on the vanadate/H2O2-induced increase in paracellular permeability and did not affect the observed redistribution of intercellular junction proteins or phosphotyrosine immunoflourescence. The relative potencies of these distinct protein kinase inhibitors in reversing the effects of vanadate/H2O2 indicate that these effects are directly related to tyrosine phosphorylation. In conclusion, our data provide evidence that enhanced tyrosine phosphorylation of intercellular junction proteins in MDCK epithelia increases paracellular permeability and can also induce prominent reorganization of the junctional complex.
dc.description76
dc.description2
dc.description85
dc.description92
dc.languageen
dc.publisherGustav Fischer Verlag
dc.publisherJena
dc.publisherAlemanha
dc.relationEuropean Journal Of Cell Biology
dc.relationEur. J. Cell Biol.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectadherens junction
dc.subjectepithelial barrier
dc.subjectparacellular permeability
dc.subjectprotein tyrosine phosphorylation
dc.subjecttight junction
dc.subjectEpidermal Growth-factor
dc.subjectCadherin-catenin Complex
dc.subjectKinase Inhibitors
dc.subjectBeta-catenin
dc.subjectCell-adhesion
dc.subjectIntercellular-junctions
dc.subjectOccluding Junctions
dc.subjectCarcinoma-cells
dc.subjectTumor Promoters
dc.subjectFactor Receptor
dc.titleIncreased tyrosine phosphorylation causes redistribution of adherens junction and tight junction proteins and perturbs paracellular barrier function in MDCK epithelia
dc.typeArtículos de revistas


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