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Titolo:
ALTERATIONS IN BETA-CATENIN PHOSPHORYLATION AND PLAKOGLOBIN EXPRESSION IN HUMAN BREAST-CANCER CELLS
Autore:
SOMMERS CL; GELMANN EP; KEMLER R; COWIN P; BYERS SW;
Indirizzi:
GEORGETOWN UNIV,SCH MED,DEPT CELL BIOL,3900 RESERVOIR RD NW WASHINGTON DC 20007 GEORGETOWN UNIV,SCH MED,DEPT CELL BIOL WASHINGTON DC 20007 GEORGETOWN UNIV,SCH MED,DEPT MED WASHINGTON DC 20007 MAX PLANCK INST IMMUNBIOL W-7800 FREIBURG GERMANY NYU,DEPT CELL BIOL NEW YORK NY 10016 LOMBARDI CANC RES CTR WASHINGTON DC 20007
Titolo Testata:
Cancer research
fascicolo: 13, volume: 54, anno: 1994,
pagine: 3544 - 3552
SICI:
0008-5472(1994)54:13<3544:AIBPAP>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADHESION MOLECULE UVOMORULIN; E-CADHERIN EXPRESSION; EPITHELIAL-CELLS; CYTOPLASMIC DOMAIN; TYROSINE PHOSPHORYLATION; CARCINOMA-CELLS; ALPHA-CATENIN; P-CADHERIN; JUNCTIONS; INVASION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
C.L. Sommers et al., "ALTERATIONS IN BETA-CATENIN PHOSPHORYLATION AND PLAKOGLOBIN EXPRESSION IN HUMAN BREAST-CANCER CELLS", Cancer research, 54(13), 1994, pp. 3544-3552

Abstract

Because the cell adhesion molecule epithelial cadherin (E-cadherin) is absent in many invasive carcinomas, we transfected the E-cadherin gene into E-cadherin-negative, invasive breast cancer cell lines BT549 and HS578t to investigate the role of E-cadherin in invasive behavior. Although the transfected E-cadherin could mediate calcium-dependent aggregation to E-cadherin-transfected L-cells, morphology and invasiveness of the breast cancer cells were not altered. We investigated the strength of the linkage of the transfected E-cadherin to the actin cytoskeleton by examining the Triton X-100 solubility of the transfected E cadherin. In BT549 and HS578t cells, a large proportion of the transfected E-cadherin was Triton soluble, whereas in E-cadherin-positive MCF-7 cells, Triton-insoluble E-cadherin was apparent at cell-cell borders. Interaction of E-cadherin with the actin cytoskeleton is thought tobe mediated by the E-cadherin-binding proteins alpha-catenin, beta-catenin, and plakoglobin. We found normal levels of alpha-catenin and beta-catenin in BT549 and HS578t cells; however, low levels of plakoglobin were expressed in these cells compared to those found in weakly invasive MCF-7 cells. Furthermore, levels of tyrosine phosphorylation of beta-catenin were elevated in E-cadherin-transfected BT549 and HS578t cells compared to MCF-7 cells. We conclude that other factors such as the expression and appropriate posttranslational modification of cadherin-associated proteins must be in place for E-cadherin to be fully functional, i.e., to alter invasiveness. During cancer progression, lossof E-cadherin expression itself or multiple other mechanisms that lead to loss of cell-cell adhesion (mutation, loss of catenin expression,alterations in phosphorylation) may contribute to a more metastatic phenotype.

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Documento generato il 21/09/20 alle ore 02:13:05