CDCC (CHICKEN HOMOLOG TO A GENE DELETED IN COLORECTAL-CARCINOMA) IS AN EPITHELIAL ADHESION MOLECULE EXPRESSED IN THE BASAL CELLS AND INVOLVED IN EPITHELIAL-MESENCHYMAL INTERACTION

Citation
Cm. Chuong et al., CDCC (CHICKEN HOMOLOG TO A GENE DELETED IN COLORECTAL-CARCINOMA) IS AN EPITHELIAL ADHESION MOLECULE EXPRESSED IN THE BASAL CELLS AND INVOLVED IN EPITHELIAL-MESENCHYMAL INTERACTION, Developmental biology, 164(2), 1994, pp. 383-397
Citations number
30
Categorie Soggetti
Developmental Biology",Biology
Journal title
ISSN journal
00121606
Volume
164
Issue
2
Year of publication
1994
Pages
383 - 397
Database
ISI
SICI code
0012-1606(1994)164:2<383:C(HTAG>2.0.ZU;2-F
Abstract
Cloning of human DCC (deleted in colorectal carcinoma, Fearon ct al., 1990) showed that it is an immunoglobulin superfamiiy member homologou s to neural cell adhesion molecules (N-CAM). To explore the normal fun ction of this molecule, we have cloned a chicken homologue to DCC (cDC C) and raised an antibody to DCC. cDCC is a protein of 160 kDa with an expression pattern distinct from those of other immunoglobulin family members including N-CAM and Ng-CAM. Transgene expression of cDCC in f ibroblasts led to increased cell-cell adhesion. Localization studies i n chicken and mouse embryos showed that DCC is expressed in the epithe lia of skin, gut, lung, and bladder. In adult, the expression of DCC i s limited to the basal layer of stratified epithelium in skin, crypt r egions of intestinal villi, and stem cells in mammary duct. Cell aggre gation assay using embryonic chicken skin epithelial cells and antibod y to DCC showed it is a Ca2+ independent cell adhesion molecule. In ep ithelial-mesenchymal interactions during feather morphogenesis, antibo dy to DCC suppressed the formation of dermal condensations and the pol arized localization of NCAM and fibronectin. These results implied tha t DCC is an epithelial cell adhesion molecule required for mediating c ritical functions in epithelial-epithelial and epithelial-mesenchymal interactions. (C) 1994 Academic Press, Inc.