SOLUBLE FRAGMENTS OF E-CADHERIN CELL-ADHESION MOLECULE INCREASE IN URINARY-EXCRETION OF CANCER-PATIENTS, POTENTIALLY INDICATING ITS SHEDDING FROM EPITHELIAL TUMOR-CELLS

1994 ◽  
Author(s):  
M KATAYAMA ◽  
S HIRAI ◽  
M YASUMOTO ◽  
K NISHIKAWA ◽  
S NAGATA ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Urinary Excretion ◽  
Cancer Patients ◽  
Tumor Cells ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Epithelial Tumor ◽  
Epithelial Tumor Cells ◽  
E Cadherin

scholarly journals Syndecan-1 expression in mammary epithelial tumor cells is E-cadherin-dependent

1996 ◽  
Vol 109 (6) ◽  
pp. 1393-1403 ◽  
Author(s):  
S. Leppa ◽  
K. Vleminckx ◽  
F. Van Roy ◽  
M. Jalkanen
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Tumor Cells ◽  
Malignant Transformation ◽  
Mrna Levels ◽  
Epithelial Tumor ◽  
Cell Matrix ◽  
Epithelial Tumor Cells ◽  
E Cadherin ◽  
Cell Cell

E-cadherin is a Ca(2+)-dependent cell-cell adhesion molecule, which is mainly expressed in epithelial cells. Recent studies have shown that E-cadherin has an important role as an invasion suppressor molecule in epithelial tumor cells. Syndecan-1 is a cell surface proteoglycan that has been implicated in a number of cellular functions including cell-cell adhesion, cell-matrix anchorage and growth factor presentation for signalling receptors. Its suppression has also been shown to be associated with malignant transformation of epithelial cells. In order to better understand the coordinated regulation of cell-cell and cell-matrix interactions during malignant transformation, we have studied the expression of syndecan-1 in malignant mammary tumor cells genetically manipulated for E-cadherin expression. In invasive NM-e-ras-MAC1 cells, where E-cadherin was partially downregulated by specific antisense RNA, syndecan-1 expression was suppressed. Furthermore, transfection of E-cadherin cDNA into invasive NM-f-ras-TD cells resulted in the upregulation of syndecan-1 expression in association with decreased invasiveness. In both cases, regulation of syndecan-1 occurred post-transcriptionally, since syndecan-1 mRNA levels remained unchanged. Instead, a translational regulation is suggested, since syndecan-1 core protein synthesis was E-cadherin dependent. Another cell adhesion protein, beta 1-integrin was not affected by E-cadherin expression. The data provide an example of coordinated changes in the expression of two cell adhesion molecules, syndecan-1 and E-cadherin during epithelial cell transformation.

622: Von Hippel-Lindau Inactivation Downregulates the Cell-Cell Adhesion Molecule E Cadherin in Renal Cancer Cells

2005 ◽  
Vol 173 (4S) ◽  
pp. 170-170
Author(s):  
Maxine G. Tran ◽  
Miguel A. Esteban ◽  
Peter D. Hill ◽  
Ashish Chandra ◽  
Tim S. O'Brien ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cancer Cells ◽  
Renal Cancer ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Von Hippel Lindau ◽  
E Cadherin ◽  
Cell Cell

scholarly journals Role of Nectin in Formation of E-Cadherin–based Adherens Junctions in Keratinocytes: Analysis with the N-Cadherin Dominant Negative Mutant

2003 ◽  
Vol 14 (4) ◽  
pp. 1597-1609 ◽  
Author(s):  
Yoshinari Tanaka ◽  
Hiroyuki Nakanishi ◽  
Shigeki Kakunaga ◽  
Noriko Okabe ◽  
Tomomi Kawakatsu ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Adherens Junctions ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Adhesion Activity ◽  
Negative Mutant ◽  
E Cadherin ◽  
Cell Cell

E-Cadherin is a Ca2+-dependent cell-cell adhesion molecule at adherens junctions (AJs) of epithelial cells. A fragment of N-cadherin lacking its extracellular region serves as a dominant negative mutant (DN) and inhibits cell-cell adhesion activity of E-cadherin, but its mode of action remains to be elucidated. Nectin is a Ca2+-independent immunoglobulin-like cell-cell adhesion molecule at AJs and is associated with E-cadherin through their respective peripheral membrane proteins, afadin and catenins, which connect nectin and cadherin to the actin cytoskeleton, respectively. We showed here that overexpression of nectin capable of binding afadin, but not a mutant incapable of binding afadin, reduced the inhibitory effect of N-cadherin DN on the cell-cell adhesion activity of E-cadherin in keratinocytes. Overexpressed nectin recruited N-cadherin DN to the nectin-based cell-cell adhesion sites in an afadin-dependent manner. Moreover, overexpression of nectin enhanced the E-cadherin–based cell-cell adhesion activity. These results suggest that N-cadherin DN competitively inhibits the association of the endogenous nectin-afadin system with the endogenous E-cadherin-catenin system and thereby reduces the cell-cell adhesion activity of E-cadherin. Thus, nectin plays a role in the formation of E-cadherin–based AJs in keratinocytes.

scholarly journals Cytoplasmic accumulation of activated leukocyte cell adhesion molecule is a predictor of disease progression and reduced survival in oral cancer patients

2009 ◽  
Vol 124 (9) ◽  
pp. 2098-2105 ◽  
Author(s):  
Meenakshi Sawhney ◽  
Ajay Matta ◽  
Muzafar A. Macha ◽  
Jatinder Kaur ◽  
Siddhartha DattaGupta ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Oral Cancer ◽  
Disease Progression ◽  
Cancer Patients ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Oral Cancer Patients ◽  
Cytoplasmic Accumulation

Differences in Repair of DNA Cross-links between Lymphocytes and Epithelial Tumor Cells from Colon Cancer Patients Measured In vitro with the Comet Assay

2009 ◽  
Vol 15 (17) ◽  
pp. 5466-5472 ◽  
Author(s):  
Mercedes Herrera ◽  
Gemma Dominguez ◽  
Jose M. Garcia ◽  
Cristina Peña ◽  
Carmen Jimenez ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Comet Assay ◽  
Cancer Patients ◽  
Tumor Cells ◽  
Epithelial Tumor ◽  
Cross Links ◽  
Epithelial Tumor Cells
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