spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hunter, I.
Right arrow Articles by Obrink, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hunter, I.
Right arrow Articles by Obrink, B.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Journal of Cell Science, Vol 107, Issue 5 1205-1216, Copyright © 1994 by Company of Biologists


JOURNAL ARTICLES

Differential regulation of C-CAM isoforms in epithelial cells

I Hunter, M Lindh and B Obrink
Department of Cell and Molecular Biology, Medical Nobel Institute, Stockholm, Sweden.

C-CAM is a Ca(2+)-independent cell adhesion molecule (CAM) that mediates intercellular adhesion of isolated rat hepatocytes. It is widely distributed in epithelia, where its presence both at lateral cell borders and on apical cell surfaces suggests that it may have diverse biological functions. Two major isoforms, C-CAM1 and C-CAM2, which differ in the lengths of their cytoplasmic domains, have been identified. The lack of suitable in vitro systems has so far prevented a detailed study of the physiological role of C-CAM in epithelia. We now report on the identification, biochemical characterization and functional analysis of C-CAM isoforms in the established epithelial cell line NBT II, derived from a chemically induced carcinoma of rat bladder. C-CAM in NBT II cells is a 110-115 kDa cell surface glycoprotein located predominantly at sites of cell-cell contact but also present on the apical cell surface. Northern blotting analysis revealed the presence of both C-CAM1 and C-CAM2, with the major transcripts for both isoforms present within the 4.0 kb size range. The dissociation of NBT II cell colonies by anti-C-CAM antibodies indicated that at least one function of C-CAM in these cells is to mediate intercellular adhesion. The maintenance of extensive cell-cell contacts and the expression of C-CAM at the contact sites in cells grown in low Ca2+ medium suggested that, like its counterpart in hepatocytes, C-CAM in NBT II cells may be a Ca(2+)-independent cell-cell adhesion molecule. The co-localization and coordinate reorganization of both C-CAM and actin by anti-C-CAM antibodies indicated that these two proteins were associated and suggested that interactions with the cytoskeleton may be important for the regulation of C-CAM function. The specific upregulation of C-CAM1 in cells induced to undergo epithelial to mesenchymal-like transitions (EMT) by the serum substitute Ultroser G suggested that C-CAM isoforms are important modulators of the adhesive properties of these cells.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
J. Cell Sci.Home page
E. Klaile, M. M. Muller, C. Kannicht, B. B. Singer, and L. Lucka
CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration
J. Cell Sci., December 1, 2005; 118(23): 5513 - 5524.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
M. M. Muller, B. B. Singer, E. Klaile, B. Obrink, and L. Lucka
Transmembrane CEACAM1 affects integrin-dependent signaling and regulates extracellular matrix protein-specific morphology and migration of endothelial cells
Blood, May 15, 2005; 105(10): 3925 - 3934.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
U. Sundberg, N. Beauchemin, and B. Obrink
The cytoplasmic domain of CEACAM1-L controls its lateral localization and the organization of desmosomes in polarized epithelial cells
J. Cell Sci., March 1, 2004; 117(7): 1091 - 1104.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
U. Sundberg and B. Obrink
CEACAM1 isoforms with different cytoplasmic domains show different localization, organization and adhesive properties in polarized epithelial cells
J. Cell Sci., March 15, 2002; 115(6): 1273 - 1284.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
S. M. Watt, A. M. Teixeira, G.-Q. Zhou, R. Doyonnas, Y. Zhang, F. Grunert, R. S. Blumberg, M. Kuroki, K. M. Skubitz, and P. A. Bates
Homophilic adhesion of human CEACAM1 involves N-terminal domain interactions: structural analysis of the binding site
Blood, September 1, 2001; 98(5): 1469 - 1479.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
B. B. Singer, I. Scheffrahn, and B. Öbrink
The Tumor Growth-inhibiting Cell Adhesion Molecule CEACAM1 (C-CAM) Is Differently Expressed in Proliferating and Quiescent Epithelial Cells and Regulates Cell Proliferation
Cancer Res., March 1, 2000; 60(5): 1236 - 1244.
[Abstract] [Full Text]


Home page
Mol. Biol. CellHome page
S. Sadekova, N. Lamarche-Vane, X. Li, and N. Beauchemin
The CEACAM1-L Glycoprotein Associates with the Actin Cytoskeleton and Localizes to Cell-Cell Contact through Activation of Rho-like GTPases
Mol. Biol. Cell, January 1, 2000; 11(1): 65 - 77.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
M. Edlund, I. Blikstad, and B.ör. Obrink
Calmodulin Binds to Specific Sequences in the Cytoplasmic Domain of C-CAM and Down-regulates C-CAM Self-association
J. Biol. Chem., January 19, 1996; 271(3): 1393 - 1399.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 1994