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The neural cell adhesion molecule, or NCAM for short, is a molecule found in eukaryotes that mediates interactions among different types of neural cells throughout the body, often in conjunction with neurotransmitters. It belongs to the immunoglobulin family, and

Function

DNA codes for the production of RNA and proteins.

Disease

Mutations in NCAM proteins can also cause many different disorders of the gastrointestinal system. These can range from inherited diseases, such as Hirschsprung's disease, to noninherited diseases such as fetal alcohol syndrome and chronic intestinal obstruction in newborns. These diseases arise due to mutations in NCAM genes that prevent the protein from allowing pacemaker cells in the gut, called interstitial cells of Cajal, to communicate. For diseases affecting newborns, such as chronic intestinal obstruction, the symptoms can disappear with age if these interstitial cells of Cajal develop properly. For people with other diseases or for those that do not develop these cells with age, treatments such as enema are employed.

NCAM mutations have also been linked to the growth of tumor cells, and often are found in advanced-stage tumors. These mutations allow NCAM to facilitate the adhesion of tumor cells and allow the tumor to grow very large very rapidly. The mutations also allow the cancer cells to more easily move through the body, invade healthy tissues, and form tumors there, as the mutated NCAM allows the cancer cells to bind to other autocrine/paracrine cells. The most effective treatment for cancers with NCAM mutations is full removal of the tumor, but this is most effective in very early stage tumors. Currently, different drugs that serve as NCAM immunotoxins are in trials to kill the mutated NCAM in more advanced tumors.

Structural highlights

NCAM consists of one distinct polypeptide chain, two copies of which combine to form a homodimer. Each polypeptide is 191 amino acids long and contains four chains: the A, B, C, and D chains.

The extracellular region of NCAM includes five immunoglobulin and two fibronectin type III domains (https://www.sciencedirect.com/science/article/pii/B9780128007815000116).

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