IgCAMs

Immunoglobulin superfamily cell adhesion molecules, commonly known as IgCAMs, are a large group of cell surface glycoproteins that play crucial roles in cell-cell adhesion, neuronal development, immune responses, and tissue organization. These molecules share a common structural feature: one or more immunoglobulin-like domains, which are conserved protein structures found in antibodies. The extracellular portion of IgCAMs typically consists of these immunoglobulin (Ig) domains, often interspersed with fibronectin type III (FnIII) domains. The intracellular portion interacts with the cytoskeleton, allowing IgCAMs to mediate cell adhesion and transmit signals into the cell.

IgCAMs are broadly classified into several families based on their structural similarities and functions. Prominent examples include the L1 family, N-CAMs (Neural Cell Adhesion Molecules), ICAMs (Intercellular Adhesion Molecules), and VCAMs (Vascular Cell Adhesion Molecules). These molecules can function as homophilic binders, meaning they bind to identical molecules on adjacent cells, or as heterophilic binders, interacting with different types of molecules. Their expression is widespread, with specific members being enriched in particular tissues, such as the nervous system where they are vital for synapse formation and neuronal wiring, and in the immune system where they facilitate leukocyte trafficking and immune cell interactions. Dysregulation of IgCAM expression or function is implicated in various diseases, including cancer metastasis, autoimmune disorders, and neurological conditions.