CELL-ADHESION ACTIVITY OF THE SHORT CYTOPLASMIC DOMAIN ISOFORM OF C-CAM (C-CAM2) IN CHO CELLS

Citation
H. Olsson et al., CELL-ADHESION ACTIVITY OF THE SHORT CYTOPLASMIC DOMAIN ISOFORM OF C-CAM (C-CAM2) IN CHO CELLS, FEBS letters, 365(1), 1995, pp. 51-56
Citations number
36
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
365
Issue
1
Year of publication
1995
Pages
51 - 56
Database
ISI
SICI code
0014-5793(1995)365:1<51:CAOTSC>2.0.ZU;2-B
Abstract
C-CAM is a Ca2+-independent rat cell adhesion molecule belonging to th e CEA gene family of!the immunoglobulin superfamily. Two major isoform s that differ in the length of their cytoplasmic domains exist, In pre vious studies it has been reported that only the long isoform (C-CAM1) but not the short isoform (C-CAM2) can mediate adhesion, However, in the mouse, isoforms with both long and short cytoplasmic domains have been reported to have adhesive activity. In order to analyze this appa rent conflict we transfected C-CAM1 or C-CAMZ into CHO Pro5 cells and examined their adhesive phenotype in an aggregation assay. We found th at in this cellular system both C-CAM1 and C-CAM2 could mediate cell-c ell adhesion in a Ca2+-independent and temperature-independent way. Th e results suggest that the cellular environment is important for the a ctivity of C-CAM isoforms.