Integrin Alpha V (ITGAV)
Reference work entry
The term “integrin” was coined by R.O. Hynes in 1986 to describe a family of adhesion proteins which integrate the cytoskeleton with the extracellular matrix and external stimuli. These integrins are composed of alpha and beta subunits to form a complete signaling molecule. The α v subunit forms a complete integrin complex through heterodimerization with one of five β subunit binding partners: beta 1 (β 1), beta 3 (β 3), beta 5 (β 5), beta 6 (β 6), or beta 8 (β 8). The first α v integrin characterized was α vβ 3, which was originally termed the “vitronectin receptor,” as it bound to plasma-derived vitronectin. The α vβ 3 integrin was purified from plasma in 1985 by R. Pytela and then cloned and sequenced in 1986 by S. Suzuki. The name “vitronectin receptor” was quickly proven to be a misnomer as α vβ 3 displays highly promiscuous binding (Table 1). The other α v...
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