Cytoplasmic Control of Cell Adhesion

Geiger, Benjamin; Ayalon, Oran; Ginsberg, D.; Volberg, Tova; Fernández, J.L. Rodrúguez; Yarden, Yosef; Ben-Ze’ev, Avri

doi:10.1101/sqb.1992.057.01.069

Cited by 58 publications

(27 citation statements)

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“…the polyclonal anti-ErbB2 from DakoCytomation and a monoclonal antibody against cadherin from Transduction Laboratories (data not shown). These observations are consistent with previous studies showing localization of ErbB2 at intercellular junctions of epithelial cells (23). (Fig.…”

Section: Methodssupporting

confidence: 83%

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

Palau

Carraway

Salas

et al. 2003

Journal of Biological Chemistry

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Section: Methodssupporting

confidence: 83%

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

Palau

Carraway

Salas

et al. 2003

Journal of Biological Chemistry

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“…However, in malignant cells EphA2 is not tyrosine-phosphorylated (17,28,34). Because of unstable cell-cell contacts in malignant cells (37)(38)(39), EphA2 cannot bind to its membrane-anchored ligand ephrinA1 (28). Notably, the E-cadherin adhesion protein is a powerful suppressor of metastasis, and E-cadherin has been shown to regulate the ability of EphA2 to bind its ligand (40).…”

Section: Discussionmentioning

confidence: 99%

EphA2 Expression Is Associated with Aggressive Features in Ovarian Carcinoma

Thaker

Deavers

Celestino

et al. 2004

Clinical Cancer Research

194

170

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Purpose: EphA2 (epithelial cell kinase) is a transmembrane receptor tyrosine kinase that has been implicated in oncogenesis. There are no published data regarding the role of EphA2 in ovarian carcinoma, which is the focus of the present study.Experimental Design: Nontransformed (HIO-180) and ovarian cancer (EG, 222, SKOV3, and A2780-PAR) cell lines were evaluated for EphA2 by Western blot analysis. Five benign ovarian masses, 10 ovarian tumors of low malignant potential, and 79 invasive ovarian carcinomas were also evaluated for EphA2 expression by immunohistochemistry. All samples were scored in a blinded fashion. Univariate and multivariate analyses were used to determine significant associations between EphA2 expression and clinicopathological variables.Results: By Western blot analysis, EG, 222, and SKOV3 cell lines overexpressed EphA2, whereas A2780-PAR and HIO-180 had low to absent EphA2 expression. All of the benign tumors had low or absent EphA2 expression. Among the invasive ovarian carcinomas examined (mean age of patients was 59.2 years), 60 (75.9%) tumors overexpressed EphA2 and the other 19 tumors had negative or minimal EphA2 expression. There was no association of EphA2 overexpression with ascites, likelihood of nodal positivity, pathological subtype, and optimum surgical cytoreduction (residual tumor <1 cm). However, EphA2 overexpression was significantly associated with higher tumor grade (P ‫؍‬ 0.02) and advanced stage of disease (P ‫؍‬ 0.001). The median survival for patients with tumor EphA2 overexpression was significantly shorter (median, 3.1 years; P ‫؍‬ 0.004); the median survival for patients with low or absent EphA2 tumor expression was at least 12 years and has not yet been reached. In multivariate analysis using the Cox proportional hazards model, only volume of residual disease (P < 0.04) and EphA2 overexpression (P < 0.01) were significant and independent predictors of survival.Conclusions: EphA2 overexpression is predictive of aggressive ovarian cancer behavior and may be an important therapeutic target.

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“…The cooperative model for the assembly of the junctional plaque from soluble cytoplasmic components (Kreis et al, 1984;Geiger et al, 1990Geiger et al, , 1992a would predict that a decrease in vinculin expression may result in an inefficient assembly of adhesion plaque molecules, leading to decreased adhesion, and this in turn will result in increased motility. In contrast, overexpression of vinculin may facilitate a cooperative and more efficient recruitment and assembly of AJs, and will lead to increased adhesion and decreased motility.…”

Section: Discussionmentioning

confidence: 99%

Suppression of vinculin expression by antisense transfection confers changes in cell morphology, motility, and anchorage-dependent growth of 3T3 cells

Fernández

Geiger

Salomon

et al. 1993

The Journal of Cell Biology

180

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Abstract. The expression of vinculin, a major component of adhesion plaques and cell-cell junctions, is markedly modulated in cells during growth activation, differentiation, motility and cell transformation. The stimulation of quiescent cells by serum factors and the culturing of cells on highly adhesive matrices induce vinculin gene expression, whereas the transformation of fibroblast and epithelial cells often results in decreased vinculin expression (reviewed in Rodrfguez Fermindez, J. L., B. Geiger, D. Salomon, I. Sabanay, M. Z611er, and A. Ben-Ze'ev. 1992. J. Cell Biol. 119:427). To study the effect of reduced vinculin expression on cell behavior, 3T3 cells were transfected with an antisense vinculin cDNA construct, and clones displaying decreased vinculin levels down to 10-30% of control levels were isolated. These cells showed a round phenotype with smaller and fewer vinculin-positive plaques localized mostly at the cell periphery. In addition, they displayed an increased motility compared to controls, manifested by a faster closure of "wounds" introduced into the monolayer, and by the formation of longer phagokinetic tracks. Moreover, the antisense transfectants acquired a higher cloning efficiency and produced larger colonies in soft agar than the parental counterparts. The results demonstrate that the regulation of vinculin expression in cells can affect, in a major way, cell shape and motility, and that decreased vinculin expression can induce cellular changes reminiscent of those found in transformed cells.

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Cytoplasmic Control of Cell Adhesion

Cited by 58 publications

References 0 publications

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

Muc4/Sialomucin Complex, the Intramembrane ErbB2 Ligand, Translocates ErbB2 to the Apical Surface in Polarized Epithelial Cells

EphA2 Expression Is Associated with Aggressive Features in Ovarian Carcinoma

Suppression of vinculin expression by antisense transfection confers changes in cell morphology, motility, and anchorage-dependent growth of 3T3 cells

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