Computational analysis of isoform-specific signal regulation by CEACAM1-A cell adhesion molecule expressed in PC12 cells.

Abstract

CEACAM1 is a signal-regulating, homophilic cell adhesion receptor system expressed in epithelia, vessel endothelia, and leukocytes. Here, we demonstrate that CEACAM1 is expressed also in PC12 cells, both as the common transmembrane isoforms, CEACAM1-L and CEACAM1-S, and as a novel, secreted, differentially spliced isoform. CEACAM1 can have both positive and negative effects on cell signaling. In an attempt to explain this dual behavior, we have initiated computational analysis of the signal-regulating effects of CEACAM1. This suggests that CEACAM1 can exert its signal-regulating activities by discriminating between binding of Src kinases and SHP phosphatases, respectively. Major factors that regulate this discrimination are the expression levels and expression ratios of transmembrane CEACAM1-L and CEACAM1-S, the concentration of secreted CEACAM1, and homophilic binding of CEACAM1 presented by neighboring cells.

Cite this paper

@article{Obrink2002ComputationalAO, title={Computational analysis of isoform-specific signal regulation by CEACAM1-A cell adhesion molecule expressed in PC12 cells.}, author={Bj{\"{o}rn Obrink and Hiroki Sawa and Inka Scheffrahn and Bernhard B. Singer and Kristmundur Sigmundsson and Ulla Sundberg and Robert Heymann and Nicole Beauchemin and Gehzi Weng and Prahlad T. Ram and Ravi Iyengar}, journal={Annals of the New York Academy of Sciences}, year={2002}, volume={971}, pages={597-607} }