Insulin-like growth factor I activates the invasion suppressor function of E-cadherin in MCF-7 human mammary carcinoma cells in vitro

Bracke, Marc; Vyncke, Barbara M.; Bruyneel, Erik; Vermeulen, Stefan; Bruyne, Georges K. De; Larebeke, N. Van; Vleminckx, Kris; Roy, Frans van; Mareel, Marc

doi:10.1038/bjc.1993.329

Cited by 89 publications

(62 citation statements)

References 26 publications

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“…The mouse monoclonal antibody MB2 was raised against MCF7/AZ cells and selected for functional inactivation of E-cadherin. 26 Mouse monoclonal anti-MUC1 (214D4 27 ) and anti-MUC5AC (21M1 22 ) antibodies, and rabbit polyclonal anti-E-cadherin antibody (␣-UMT) were a gift, respectively, from Dr. J. Hilkens (The Netherlands Cancer Institute, Amsterdam), Dr. J. Bara (INSERM U-482, Saint-Antoine Hospital, Paris, France) and Dr. J. Behrens (Friedrich-Miescher Laboratory der Max Planck society in Tübingen). The polyclonal anti-MUC5AC antibody (LUM5-1 28 ) was a gift from Dr. Carlstedt (Lund University, Sweden).…”

Section: Antibodiesmentioning

confidence: 99%

Requirement of both mucins and proteoglycans in cell‐cell dissociation and invasiveness of colon carcinoma HT‐29 cells

Truant

Bruyneel

Gouyer

et al. 2003

Intl Journal of Cancer

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Key words: colon carcinoma cells; E-cadherin; mucins; heparan sulfate proteoglycansEpithelial E-cadherin, a component of the adherens junctions, is crucial for the organization and maintenance of differentiated epithelia. 1 The extracellular NH2-terminal domain of this transmembrane glycoprotein mediates cell-cell adhesion in a homophilic and Ca 2ϩ -dependent way. The COOH-terminal domain binds to the actin cytoskeleton via ␣-catenin and ␤-catenin or plakoglobin. 2 Studies in cancer cell lines have shown that changes in the structure or in the expression of the components of the E-cadherin/␤-catenin complex result in the suppression of cell-cell adhesion and in the expression of an invasive phenotype. [3][4][5][6][7][8] In cancer, the maintenance of the epithelia is lost and dissociation of cells is associated with metastatic dissemination. This phenomenon can occur through a decrease in the expression level of E-cadherin and, regarding colon cancer, such decrease has been related to the tumor grade and clinical outcome. 9 At the genomic level, loss of E-cadherin expression does not occur as a result of mutation of E-cadherin gene, whereas mutations of ␤-catenin were found in a small proportion of colon cancers. 10 -12 In another way, E-cadherin-mediated cell-cell adhesion may be modulated by the mucin-like glycoprotein MUC1, which is often overexpressed in cancer. MUC1, also termed episialin, is a membrane-associated glycoprotein composed of a membrane anchor and a mucin-like ectodomain. 13 In human ZR-75-1 breast cancer cells, the cytoplasmic domain of MUC1 was shown to bind ␤-catenin, leading to a decrease of E-cadherin-catenin complex and an anti-adhesion effect. 14 On the other hand, MUC1 was shown to cause steric hindrance of adhesion molecules like E-cadherin, through its large negatively charged extracellular domain, which contains many oligosaccharide side chains. 15,16 Proteoglycans were also shown to disturb the function of E-cadherin through steric hindrance in variants of the murine mammary gland cell line NMuMG and the canine epithelial kidney cell line MDCK. 17 During colorectal carcinogenesis, the expression of MUC1 was found upregulated, particularly in later stages of the disease. 18 -20 On the other hand, de novo appearance of a secreted mucin normally found in the stomach, MUC5AC, has been described in colon carcinomas. [21][22][23] Thus, mucinous differentiated cells are present in colorectal carcinomas and more particularly in mucinous carcinomas and in signet ring cell carcinomas. Until now, the significance of a differentiation characteristic into a mucin-secreting phenotype with regard to the tumor development is still unknown.To investigate the role of mucins in the invasive properties of colon carcinoma cells, the HT-29 cell line is an appropriate model, as the cells of this cell line express different phenotypes: besides a majority of undifferentiated cells (Ͼ95%), a small proportion of cells presents a capacity to differentiate into a mucinous phenotype or into an enterocyte-like ...

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Section: Antibodiesmentioning

confidence: 99%

Requirement of both mucins and proteoglycans in cell‐cell dissociation and invasiveness of colon carcinoma HT‐29 cells

Truant

Bruyneel

Gouyer

et al. 2003

Intl Journal of Cancer

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“…We used the following antibodies: HECD-1 (Takara Shuzo, Kyoto, Japan) and MB2 (Bracke et al, 1993) mouse monoclonal antibodies against human Ecadherin; a nity-puri®ed rabbit polyclonal antibody 1522, raised against the b-catenin-speci®c synthetic peptide C-PGDSNQLAWFDTDL (Vermeulen et al, 1995b); a nitypuri®ed rabbit polyclonal antibody 1597 raised against the aE-catenin-speci®c synthetic peptide C-HVDPVQALSEFK (Vermeulen et al, 1995a).…”

Section: Immunoprecipitation Western Blotting and Immunocytochemistrymentioning

confidence: 99%

The αE-catenin gene (CTNNA1) acts as an invasion-suppressor gene in human colon cancer cells

Vermeulen

Nollet

Teugels³

et al. 1999

Oncogene

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The acquisition of invasiveness is a crucial step in the malignant progression of cancer. In cancers of the colon and of other organs the E-cadherin/catenin complex, which is implicated in homotypic cell-cell adhesion as well as in signal transduction, serves as a powerful inhibitor of invasion. We show here that one allele of the aE-catenin (CTNNA1) gene is mutated in the human colon cancer cell family HCT-8, which is identical to HCT-15, DLD-1 and HRT-18. Genetic instability, due to mutations in the HMSH6 (also called GTBP) mismatch repair gene, results in the spontaneous occurrence of invasive variants, all carrying either a mutation or exon skipping in the second aE-catenin allele. The aE-catenin gene is therefore, an invasionsuppressor gene in accordance with the two-hit model of Knudsen for tumour-suppressor genes.

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“…Each cell population (EF43.C, EF43.fgf-3 and EF43.fgf-4, as indicated) was tested at least twice and each test was performed in triplicate (2) III (3) III (2);IV (1) III (1);IV (2) Monolayer fragments were confronted with precultured heart fragments for 4 and 7 days. Histological evaluation was performed by three independent observers and invasion was scored according to Bracke et al (1993); grades I and II mean no occupation of the cardiac muscle and absence of invasion whereas grades III and IV indicate invasion because confronted cells are replacing less or more of the heart cells, respectively. The number of cultures are in parenthesis The cells were incubated during 24h on the top of type I collagen gel.…”

Section: In Vitro Invasive Propertiesmentioning

confidence: 99%

“…They were embedded in para n, serially sectioned and stained with hematoxylin and eosine. Histological evaluation was performed by three independent observers and invasion was scored according to Bracke et al (1993).…”

Section: In Vitro Cell Invasion Assaysmentioning

confidence: 99%

FGF-3 and FGF-4 elicit distinct oncogenic properties in mouse mammary myoepithelial cells

et al. 1998

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Fibroblast Growth Factors 3 (FGF-3) and 4 (FGF-4) were compared for the e ects they each exert on EF43 mouse cells. This non-transformed mammary cell line appears to be myoepithelial mainly because it expresses a-smooth muscle actin. The EF43 cells were infected with similar vectors that carry either the short fgf-3 sequence (the product of which goes into the secretory pathway), fgf-4 or the selection gene only as control. In syngeneic animals, EF43.fgf-3 cells were tumorigenic only when orthotopically implanted whereas EF43.fgf-4 cells invariably gave rise to aggressive tumors. However, both tumor types were metastatic as evidenced by the blue micrometastases observed when the implanted cells expressed lacZ. In vitro, the FGF-3 producing cells were strongly invasive in matrigel coated chambers whereas the EF43.fgf-4 cells only were invasive in type I-collagen gels. Interestingly, FGF-3 production greatly stimulated the synthesis of pro-MMP-9 (Matrix Metalloprotease-9) and, to a lesser extent, that of pro-MMP-2. FGF-3 also up-regulated the production of plasminogen activators. In contrast, FGF-4 had no e ect on these secretions and the medium conditioned by the EF43.fgf-4 cells displayed the largest plasminogen activator ± inhibitor activity. These results show that FGF-3 and FGF-4 have distinct mechanisms of action on myoepithelial cells.

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Insulin-like growth factor I activates the invasion suppressor function of E-cadherin in MCF-7 human mammary carcinoma cells in vitro

Cited by 89 publications

References 26 publications

Requirement of both mucins and proteoglycans in cell‐cell dissociation and invasiveness of colon carcinoma HT‐29 cells

Requirement of both mucins and proteoglycans in cell‐cell dissociation and invasiveness of colon carcinoma HT‐29 cells

The αE-catenin gene (CTNNA1) acts as an invasion-suppressor gene in human colon cancer cells

FGF-3 and FGF-4 elicit distinct oncogenic properties in mouse mammary myoepithelial cells

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