Alpha-V beta-3

Alpha-V beta-3 (also known as αvβ3 or integrin αvβ3) is a type of integrin, a group of proteins that mediate the attachment between a cell and its surroundings, such as other cells or the extracellular matrix (ECM). This integrin is a receptor for vitronectin, but can also bind to other ECM proteins such as fibronectin, fibrinogen, prothrombin, osteopontin, and thrombospondin.

Structure

The αvβ3 integrin is a heterodimeric protein, meaning it is composed of two different subunits, the alpha (α) and beta (β) subunits. Each subunit has a large extracellular domain, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain is responsible for binding to the ECM, while the cytoplasmic tail is involved in signaling to the inside of the cell.

Function

The primary function of αvβ3 is to mediate cell adhesion to the ECM. This is important for a variety of biological processes, including cell migration, cell proliferation, and cell survival. In addition, αvβ3 plays a key role in angiogenesis, the process of new blood vessel formation. This makes it a potential target for anti-angiogenic therapies, which aim to inhibit the growth of new blood vessels in order to starve tumors of nutrients.

Clinical significance

Due to its role in angiogenesis, αvβ3 has been implicated in a number of diseases, including cancer, rheumatoid arthritis, osteoporosis, and atherosclerosis. In particular, it has been found to be overexpressed on the surface of many types of cancer cells, making it a potential target for cancer therapy.

See also

• Integrin
• Extracellular matrix
• Angiogenesis
• Cancer therapy