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Cell adhesion molecule
Cell Adhesion Molecules (CAMs) are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix (ECM) in the process called cell adhesion.
These proteins are typically transmembrane receptors and are composed of three domains: an intracellular domain that interacts with the cytoskeleton, a transmembrane domain and an extracellular domain that interacts either with other CAMs of the same kind (homophilic binding) or with other CAMs or the extracellular matrix (heterophilic binding).
Additional recommended knowledge
Families of CAMs
Most of the CAMs belong to 4 protein families: Ig (immunoglobulin) superfamily (IgSF CAMs), the integrins, the cadherins and the selectins.
Immunoglobulin superfamily CAMs (IgSF CAMs) are either homophilic or heterophilic and bind integrins or different IgSF CAMs.
The integrins are a family of heterophilic CAMs that bind IgSF CAMs or the extracellular matrix. They are heterodimers, consisting in two non-covalently linked subunits, called alpha and beta. 24 different alpha subunits are known that can link in many different combinations with the 9 different beta subunits, however not all combinations are observed.
Some sources (for example, MeSH) don't consider integrins to be cell adhesion molecules.
The cadherins are a family of homophilic CAMs, Ca2+ dependent. The most important members of this family are E-cadherins (epithelial), P-cadherins (placental) and N-cadherins (neural).
The selectins are a family of heterophilic CAMs that bind fucosylated carbohydrates, e.g. mucins. They are calcium-dependent. The three family members are E-selectin (endothelial), L-selectin (leukocyte) and P-selectin (platelet). The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 (PSGL-1), which is a mucin-type glycoprotein expressed on all white blood cells.
Neutrophils and eosinophils bind to E-selectin. One of the reported ligands for E-selectin is the sialylated Lewis X Ag (sLe(x)). Eosinophils, like neutrophils, use sialylated, protease-resistant structures to bind to E-selectin, although the eosinophil expresses much lower levels of these structures on its surface.  Ligands for P-selectin on eosinophils and neutrophils are similar sialylated, protease-sensitive, endo-beta-galactosidase-resistant structures, clearly different than those reported for E-selectin, and suggest disparate roles for P-selectin and E-selectin during recruitment during inflammatory responses. 
Neurological Diseases Associated With CAM's
Mental retardation and other neurological disorders are attributable in part to disruption of normal cell adhesion
Categories: Transmembrane receptors | Signal transduction | Membrane biology | Cell adhesion proteins
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Cell_adhesion_molecule". A list of authors is available in Wikipedia.|