C-CAM is a member of the carcinoembryonic antigen family (CEA) of the rat,
which mediates cell adhesion in vitro and binds to signal transduction mole
cules. In many tissues C-CAM is expressed in the apical domain of the plasm
a membrane in close contact with intracellular cortical microfilaments, e.g
., in the microvilli of the brush borders of enterocytes, Regarding this su
bcellular localisation, we have investigated the C-CAM interaction with the
cytoskeleton. The association of C-CAM with detergent-insoluble structures
increased when the small intestinal mucosa was extracted under conditions
known to preserve the cytoskeleton of the brush borders. We found a coimmun
oprecipitation of actin with C-CAM of the small intestine mucosa which incr
eased in the presence of the chemical cross-linker DSP, allowing the demons
tration of complexes between C-CAM and actin of different molecular masses,
A recombinant fusion protein of the cytoplasmic domain of the long isoform
of C-CAM bound specifically to purified actin in a cosedimentation assay.
These results suggest an intrinsic actin-binding activity of C-CAM. (C) 199
9 Academic Press.