α2β1 Integrin

Adv Exp Med Biol. 2014;819:41-60. doi: 10.1007/978-94-017-9153-3_3.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Animals
  • Hemostasis
  • Humans
  • Immunity, Innate
  • Integrin alpha2beta1 / chemistry
  • Integrin alpha2beta1 / physiology*
  • Neovascularization, Physiologic
  • Protein Structure, Tertiary
  • Signal Transduction
  • Wound Healing

Substances

  • Integrin alpha2beta1