The carcinoembryonic-antigen-related cell-adhesion molecule (CEACAM) family of proteins has been implicated in various intercellular-adhesion and intracellular-signalling-mediated effects that govern the growth and differentiation of normal and cancerous cells. CEACAM1, also known as biliary glycoprotein I (BGP I) and CD66a, is a member of the carcinoembryonic antigen (CEA) gene family which belongs to the immunoglobulin superfamily. The highly glycosylated CEACAM1 contains one N-terminal V-type Ig-like domain and three C2-type Ig-like domains within its ECD, and one ITIM motif and a calmodulin binding site in the cytoplasmic region. CEACAM1 is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. It was described as an adhesion molecule mediating cell adhesion via both homophilic and heterophilic manners, and was detected on leukocytes, epithelia, and endothelia. Studies have revealed that CEACAM1 performs actions in multiple cellular processes including tissue differentiation, angiogenesis, apoptosis, metastasis, as well as the modulation of innate and adaptive immune responses.
Carcinoembryonic antigen-related cell adhesion molecule 21 is a protein that in humans is encoded by the CEACAM21 gene. It belongs to the immunoglobulin superfamily. CEA family.containing 1 Ig-like C2-type (immunoglobulin-like) domain.It was found to be a cell-cell adhesion molecule detected on leukocytes, epithelia, and endothelia. The encoded protein mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. Multiple cellular activities have been attributed to the encoded protein, including roles in the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses.
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3 (CEACAM3) belongs to the immunoglobulin superfamily and CEA family. CEACAM3 was originally described in bile ducts of liver as biliary glycoprotein. Subsequently, it was found to be a cell-cell adhesion molecule detected on leukocytes, epithelia, and endothelia. CEACAM3 mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. In addition, it is associated with the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses.
Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) belong to a group of mammalian immunoglobulin related glycoproteins. They play critical roles in cell–cell recognition. CEACAM5, also called CEA and CD66e, is characterized by having seven extracellular Ig domains and a glycosylphosphatidylinositol (GPI) anchor. CEACAM5 is expressed primarily by epithelial cells, and functions as a calcium-independent adhesion molecule through homophilic and heterophilic interactions with CEACAM1. Studies have shown that CEACAM5 is overexpressed in a majority of carcinomas, and its overexpression can protect tumor cells from apoptosis. It is commonly used as a cancer marker.
Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) belong to a group of mammalian immunoglobulin related glycoproteins. They play critical roles in cell–cell recognition. CEACAM5; also called CEA and CD66e; is characterized by having seven extracellular Ig domains and a glycosylphosphatidylinositol (GPI) anchor. CEACAM5 is expressed primarily by epithelial cells; and functions as a calcium-independent adhesion molecule through homophilic and heterophilic interactions with CEACAM1. Studies have shown that CEACAM5 is overexpressed in a majority of carcinomas; and its overexpression can protect tumor cells from apoptosis. It is commonly used as a cancer marker.
CEACAM5; also known as CEA or D66e; belongs to the large CEACAM subfamily of immunoglobulin superfamily. CEACAM5 is expressed primarily by epithelial cells; and is synthesized as a glycoprotein with a MW of 180 kDa comprising 60% carbohydrate. CEACAM5 contains one Ig-like V-type domain at the N-terminus; followed by six Ig-like C2-type domain and a GPI anchor; and exists as a homodimer. CEACAM5 and CEACAM6 are overexpressed in many cancers and are associated with adhesion and invasion. CEACAM5 can mediate cell-cell adhesion through homotypic and heterotypic interactions. It functions as a homotypic intercellular adhesion molecule and serves as a widely used tumor marker; since it is expressed at higher levels in tumorous tissues than in corresponding normal tissues. CEACAM5 has also been shown to contribute to tumorigenicity by inhibiting cellular differentiation. In addition; CEACAM5 is identified as the host receptor for the Dr family of adhesins of E.Coli; and the binding of E.coli Dr adhesins leads to dissociation of the CEACAM5 homodimer.
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