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Cell adhesion activity of the short cytoplasmic domain isoform of C‐CAM (C‐CAM2) in CHO cells
Author(s) -
Olsson Helena,
Wikström Kristina,
Kjellström Gunilla,
Öbrink Björn
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00436-d
Subject(s) - gene isoform , chinese hamster ovary cell , cytoplasm , chemistry , microbiology and biotechnology , biophysics , biology , biochemistry , gene , receptor
C‐CAM is a Ca 2+ ‐independent rat cell adhesion molecule belonging to the CEA gene family of the immunoglobulin superfamily. Two major isoforms that differ in the length of their cytoplasmic domains exist. In previous 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 apparent conflict we transfected C‐CAM1 or C‐CAM2 into CHO Pro5 cells and examined their adhesive phenotype in an aggregation assay. We found that in this cellular system both C‐CAM1 and C‐CAM2 could mediate cell‐cell adhesion in a Ca 2+ ‐independent and temperature‐independent way. The results suggest that the cellular environment is important for the activity of C‐CAM isoforms.