Expression of the cell–cell adhesion molecule E-cadherin in tongue carcinoma cell lines

1994 ◽  
Vol 108 (11) ◽  
pp. 957-961 ◽  
Author(s):  
A. R. Kinsella ◽  
G. L. Bowie ◽  
J. K. Fields ◽  
A. S. Jones

AbstractA reduction in cell adhesiveness and cell invasion are essential steps in tumour progression. In the present study six tongue carcinoma cell lines were compared with regard to their invasive potential in two in vitro invasion assay systems and for their patterns of expression of the cell–cell adhesion molecule E-cadherin. The three cell lines negative for E-cadherin expression were invasive in both assays. One cell line with strong E-cadherin expression was strongly invasive and one weakly invasive. One cell line with reduced E-cadherin expression was weakly invasive. There was no significant pattern to these findings (x2 = 0.375; p = 0.54). This supports previous studies from this group that suggest that E-cadherin is only one of the presumably many molecules involved in tumour progression in squamous cell carcinoma of the tongue.

1995 ◽  
Vol 15 (9) ◽  
pp. 4819-4824 ◽  
Author(s):  
J M Daniel ◽  
A B Reynolds

The tyrosine kinase substrate p120cas (CAS), which is structurally similar to the cell adhesion proteins beta-catenin and plakoglobin, was recently shown to associate with the E-cadherin-catenin cell adhesion complex. beta-catenin, plakoglobin, and CAS all have an Arm domain that consists of 10 to 13 repeats of a 42-amino-acid motif originally described in the Drosophila Armadillo protein. To determine if the association of CAS with the cadherin cell adhesion machinery is similar to that of beta-catenin and plakoglobin, we examined the CAS-cadherin-catenin interactions in a number of cell lines and in the yeast two-hybrid system. In the prostate carcinoma cell line PC3, CAS associated normally with cadherin complexes despite the specific absence of alpha-catenin in these cells. However, in the colon carcinoma cell line SW480, which has negligible E-cadherin expression, CAS did not associate with beta-catenin, plakoglobin, or alpha-catenin, suggesting that E-cadherin is the protein which bridges CAS to the rest of the complex. In addition, CAS did not associate with the adenomatous polyposis coli (APC) tumor suppressor protein in any of the cell lines analyzed. Interestingly, expression of the various CAS isoforms was quite heterogeneous in these tumor cell lines, and in the colon carcinoma cell line HCT116, which expresses normal levels of E-cadherin and the catenins, the CAS1 isoforms were completely absent. By using the yeast two-hybrid system, we confirmed the direct interaction between CAS and E-cadherin and determined that CAS Arm repeats 1 to 10 are necessary and sufficient for this interaction. Hence, like beta-catenin and plakoglobin, CAS interacts directly with E-cadherin in vivo; however, unlike beta-catenin and plakoglobin, CAS does not interact with APC or alpha-catenin.


1989 ◽  
Vol 169 (6) ◽  
pp. 2233-2238 ◽  
Author(s):  
L L Lanier ◽  
R Testi ◽  
J Bindl ◽  
J H Phillips

Neural cell adhesion molecule (N-CAM) is a membrane glycoprotein expressed on neural and muscle tissues that is involved in homotypic adhesive interactions. We have demonstrated that N-CAM also is expressed on hematopoietic cells, and is recognized by the anti-Leu-19 mAb. Leu-19 is preferentially expressed on NK cells and T lymphocytes that mediate MHC-unrestricted cytotoxicity, but is also present on some myeloid leukemia cell lines. On NK cells, T cells, the KG1a.5 hematopoietic cell line, and a neuroblastoma cell line, Leu-19 is a approximately 140-kD polypeptide with N-linked carbohydrates and abundant sialic acid residues. Sequential immunoprecipitation and peptide mapping demonstrated that the Leu-19 and N-CAM molecules expressed on leukocyte and neuroblastoma cell lines are similar structures. These findings suggest that the Leu-19 antigen on leukocytes may be involved in cell adhesion, analogous to the function on N-CAM on neural cells.


1991 ◽  
Vol 113 (1) ◽  
pp. 173-185 ◽  
Author(s):  
U H Frixen ◽  
J Behrens ◽  
M Sachs ◽  
G Eberle ◽  
B Voss ◽  
...  

The ability of carcinomas to invade and to metastasize largely depends on the degree of epithelial differentiation within the tumors, i.e., poorly differentiated being more invasive than well-differentiated carcinomas. Here we confirmed this correlation by examining various human cell lines derived from bladder, breast, lung, and pancreas carcinomas. We found that carcinoma cell lines with an epithelioid phenotype were noninvasive and expressed the epithelium-specific cell-cell adhesion molecule E-cadherin (also known as Arc-1, uvomorulin, and cell-CAM 120/80), as visualized by immunofluorescence microscopy and by Western and Northern blotting, whereas carcinoma cell lines with a fibroblastoid phenotype were invasive and had lost E-cadherin expression. Invasiveness of these latter cells could be prevented by transfection with E-cadherin cDNA and was again induced by treatment of the transfected cells with anti-E-cadherin mAbs. These findings indicate that the selective loss of E-cadherin expression can generate dedifferentiation and invasiveness of human carcinoma cells, and they suggest further that E-cadherin acts as an invasion suppressor.


2005 ◽  
Vol 173 (4S) ◽  
pp. 170-170
Author(s):  
Maxine G. Tran ◽  
Miguel A. Esteban ◽  
Peter D. Hill ◽  
Ashish Chandra ◽  
Tim S. O'Brien ◽  
...  

2017 ◽  
Vol 13 (5) ◽  
pp. 3951-3957 ◽  
Author(s):  
Xiaofeng Wang ◽  
Xin Liu ◽  
Cong Liu ◽  
Ming Ren ◽  
Sujie Gao ◽  
...  

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