Historical Background
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 αv subunit forms a complete integrin complex through heterodimerization with one of five β subunit binding partners: beta 1 (β1), beta 3 (β3), beta 5 (β5), beta 6 (β6), or beta 8 (β8). The first αv integrin characterized was αvβ3, which was originally termed the “vitronectin receptor,” as it bound to plasma-derived vitronectin. The αvβ3 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 αvβ3 displays highly promiscuous binding (Table 1). The other αv...
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Kerr, B.A., Byzova, T.V. (2018). Integrin Alpha V (ITGAV). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_619
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