Increased Tyrosine Phosphorylation Causes Redistribution Of Adherens Junction And Tight Junction Proteins And Perturbs Paracellular Barrier Function In Mdck Epithelia.

dc.creatorCollares-Buzato, C B
dc.creatorJepson, M A
dc.creatorSimmons, N L
dc.creatorHirst, B H
dc.date1998-Jun
dc.date2015-11-27T12:19:18Z
dc.date2015-11-27T12:19:18Z
dc.date.accessioned2018-03-29T00:52:54Z
dc.date.available2018-03-29T00:52:54Z
dc.identifierEuropean Journal Of Cell Biology. v. 76, n. 2, p. 85-92, 1998-Jun.
dc.identifier0171-9335
dc.identifier10.1016/S0171-9335(98)80020-4
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9696347
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194206
dc.identifier9696347
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294439
dc.descriptionPolarized monolayers of strain II 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 immunofluorescence 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 potent 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 immunofluorescence. 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.description85-92
dc.languageeng
dc.relationEuropean Journal Of Cell Biology
dc.relationEur. J. Cell Biol.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectActins
dc.subjectAnimals
dc.subjectCadherins
dc.subjectCell Line
dc.subjectCell Membrane Permeability
dc.subjectDogs
dc.subjectGenistein
dc.subjectImmunohistochemistry
dc.subjectInulin
dc.subjectKidney
dc.subjectMembrane Proteins
dc.subjectNitriles
dc.subjectPeroxides
dc.subjectPhalloidine
dc.subjectPhosphoproteins
dc.subjectPhosphorylation
dc.subjectPhosphotyrosine
dc.subjectProtein Tyrosine Phosphatases
dc.subjectProtein-tyrosine Kinases
dc.subjectRhodamines
dc.subjectStaurosporine
dc.subjectTight Junctions
dc.subjectTyrphostins
dc.subjectVanadates
dc.subjectZonula Occludens-1 Protein
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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