α2β1 Integrin.

Madamanchi A, Santoro SA, Zutter MM
Adv Exp Med Biol. 2014 819: 41-60

PMID: 25023166 · DOI:10.1007/978-94-017-9153-3_3

The α2β1 integrin, also known as VLA-2, GPIa-IIa, CD49b, was first identified as an extracellular matrix receptor for collagens and/or laminins [55, 56]. It is now recognized that the α2β1 integrin serves as a receptor for many matrix and nonmatrix molecules [35, 79, 128]. Extensive analyses have clearly elucidated the α2 I domain structural motifs required for ligand binding, and also defined distinct conformations that lead to inactive, partially active or highly active ligand binding [3, 37, 66, 123, 136, 137, 140]. The mechanisms by which the α2β1 integrin plays a critical role in platelet function and homeostasis have been carefully defined via in vitro and in vivo experiments [76, 104, 117, 125]. Genetic and epidemiologic studies have confirmed human physiology and disease states mediated by this receptor in immunity, cancer, and development [6, 20, 21, 32, 43, 90]. The role of the α2β1 integrin in these multiple complex biologic processes will be discussed in the chapter.

MeSH Terms (9)

Animals Hemostasis Humans Immunity, Innate Integrin alpha2beta1 Neovascularization, Physiologic Protein Structure, Tertiary Signal Transduction Wound Healing

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