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.