CD11a is a 170-180 kD type I transmembrane glycoprotein also known as LFA-1α chain and integrin αL subunit. CD11a non-covalently associates with integrin β2 (CD18) to form LFA-1. It is expressed on all leukocytes, including B and T lymphocytes, monocytes, macrophages, neutrophils, basophils and eosinophils. It is absent on non-hematopoietic tissues and platelets. CD11a plays a central role in leukocyte cell-cell interactions and is important in lymphocyte costimulation. CD11a/CD18 binds to ICAM-1 (CD54), ICAM-2 (CD102), and ICAM-3 (CD50).
Human ITGAM (Integrin alpha M subunit) is a 127kDa (predicted) glycoprotein, a member of the Integrin family of proteins. The Integrin family proteins are heterodimeric transmembrane receptors composed of an alpha and a beta subunit. The Integrin alpha M subunit, also known as MAC-1 alpha subunit or CD11b, combines with the Integrin beta 2 subunit (CD18) to form the non-covalent heterodimer Integrin alpha M/ beta 2, also known as MAC-1 and complement receptor type 3 (CR3).
Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This protein combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as inactivated-C3b (iC3b) receptor 4 (CR4). The alpha X beta 2 complex seems to overlap the properties of the alpha M beta 2 integrin in the adherence of neutrophils and monocytes to stimulated endothelium cells, and in the phagocytosis of complement coated particles. Two transcript variants encoding different isoforms have been found for this gene.
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