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Titolo:
HYPERPHOSPHORYLATION OF BETA-CATENIN ON SERINE-THREONINE RESIDUES ANDLOSS OF CELL-CELL CONTACTS INDUCED BY CALYCULIN-A AND OKADAIC ACID INHUMAN EPIDERMAL-CELLS
Autore:
SERRES M; GRANGEASSE C; HAFTEK M; DUROCHER Y; DUCLOS B; SCHMITT D;
Indirizzi:
HOP EDOUARD HERRIOT,INSERM UNITE 346,PAVILLON R F-69437 LYON 03 FRANCE INST BIOL & CHIM PROT,UPR 412 CNRS F-69007 LYON FRANCE ECOLE NORMALE SUPER,UMR 49 CNRS F-69007 LYON FRANCE
Titolo Testata:
Experimental cell research
fascicolo: 1, volume: 231, anno: 1997,
pagine: 163 - 172
SICI:
0014-4827(1997)231:1<163:HOBOSR>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
SEGMENT POLARITY GENE; KERATIN INTERMEDIATE FILAMENTS; E-CADHERIN; TYROSINE PHOSPHORYLATION; DESMOSOMAL PROTEINS; CYTOPLASMIC DOMAIN; SIGNAL-TRANSDUCTION; EPITHELIAL-CELLS; ADHESION; PLAKOGLOBIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
69
Recensione:
Indirizzi per estratti:
Citazione:
M. Serres et al., "HYPERPHOSPHORYLATION OF BETA-CATENIN ON SERINE-THREONINE RESIDUES ANDLOSS OF CELL-CELL CONTACTS INDUCED BY CALYCULIN-A AND OKADAIC ACID INHUMAN EPIDERMAL-CELLS", Experimental cell research, 231(1), 1997, pp. 163-172

Abstract

Phosphorylation and dephosphorylation events may critically control junction assembly and stability, as well as regulate the formation of the cadherin-cytoskeleton complex, thus influencing the adhesive function of cells. In the present study, we have used specific activators and inhibitors of protein kinases and phosphatases to analyze the role of protein phosphorylation in the maintenance of epithelial architecture, Okadaic acid and calyculin A cell treatments induced two major effects: a dramatic alteration of the keratin network of epidermal cells and a complete disruption of cell-cell contacts. This loss in cell-cellcontacts was not tissue and species restricted and the interactions of keratinocytes with the matrix were not involved, The observed changes were highly specific for these drugs and were obtained in the range of concentrations corresponding to the inhibition of protein phosphatase 1 (PP1), They were time- and dose-dependent, and reversible, excluding a cytotoxic effect of the drugs. A decrease in electrophoretic mobility of beta-catenin, a major protein involved in the regulation of intercellular adherens junctions, was observed in keratinocytes and fibroblasts treated with okadaic acid and calyculin A, suggesting a change in the protein phosphorylation level and/or protein conformation. Data from beta-catenin immunocomplex autoradiography performed after P-32 in vivo incorporation in untreated and okadaic acid or calyculin A-treated Ha-CaT cells, demonstrated a higher level of phosphorylation ofbeta-catenin in treated cells compared to untreated ones. Analysis ofP-32-labeled phosphoaminoacids demonstrated that beta-catenin was exclusively phosphorylated on serine-threonine residues but not on tyrosine residues. Immunoprecipitations and Western blotting using anti-phosphoserine and anti-phosphotyrosine antibodies confirmed these data, The change in beta-catenin phosphorylation on serine-threonine residues may play a role in the control of the cohesion between epithelial cells and may be involved in the regulation of the transduction signal. (C) 1997 Academic Press.

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Documento generato il 24/09/20 alle ore 23:58:37