Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194206
Type: Artigo de periódico
Title: Increased Tyrosine Phosphorylation Causes Redistribution Of Adherens Junction And Tight Junction Proteins And Perturbs Paracellular Barrier Function In Mdck Epithelia.
Author: Collares-Buzato, C B
Jepson, M A
Simmons, N L
Hirst, B H
Abstract: Polarized 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.
Subject: Actins
Animals
Cadherins
Cell Line
Cell Membrane Permeability
Dogs
Genistein
Immunohistochemistry
Inulin
Kidney
Membrane Proteins
Nitriles
Peroxides
Phalloidine
Phosphoproteins
Phosphorylation
Phosphotyrosine
Protein Tyrosine Phosphatases
Protein-tyrosine Kinases
Rhodamines
Staurosporine
Tight Junctions
Tyrphostins
Vanadates
Zonula Occludens-1 Protein
Rights: fechado
Identifier DOI: 10.1016/S0171-9335(98)80020-4
Address: http://www.ncbi.nlm.nih.gov/pubmed/9696347
Date Issue: 1998
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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