Integrins are a family of heterodimeric transmembrane glycoproteins that attach cells to extracellular proteins on the basement membrane. They consist of large (120-170 kD) and small ( 90-110 kD) subunits. Some integrins are important for direct cell to cell recognition and interaction, see figure 5. They contain binding sites for divalent cations (Mg2+ and Ca2+) which are required. Mamallian integrins form several families sharing common subunits with different subunits.
The integrins are exclusively expressed on leucocytes. The common unit is CD18 and the various subunits are CD11a,b,c, and d. Thus the four integrins are CD11a / CD18, CD11b / CD18, CD11c / CD18 and CD11d / CD18, see figure 6. integrins are activated by phosphorylation which results in a conformational change in the molecule. A mutation in the gene encoding CD18, the subunit of integrins results in the genetic disorder leukocyte adhesion deficiency (LAD). Patients with LAD are prone to recurrent bacterial infections due to an inability to recruit granulocytes in response to infection.
The main ligands for integrins are members of the immunoglobulin superfamily such as ICAM-1.