Journal of Allergy and Clinical Immunology
3. Adhesion molecules and receptors
Section snippets
Integrins
Integrins1, 2, 3 are noncovalently linked αβ heterodimers. Each subunit has a large extracellular domain, a single transmembrane domain, and a short cytoplasmic domain (20-70 residues). In vertebrates there are 18 α subunits and 8 β subunits combining to form 24 integrins with diverse ligand recognition specificity, including cell-surface and extracellular matrix molecules. Some subunits occur only in a single integrin, whereas others occur in multiple integrins; for example, β1 occurs in 12
Selectins
The selectin family5, 6, 7 consists of 3 members of C-type lectins that bind glycoproteins and glycolipids bearing sialyl Lewis X (sLeX) in a calcium-dependent manner. The lectin domain is adjacent to a domain homologous to epidermal growth factor, a variable number of short consensus repeats (SCRs; a motif found in many complement regulatory proteins), a single transmembrane domain, and a C-terminal cytoplasmic domain. The size difference among the selectins largely reflects the number of
ICAM family
The 5 members of this subfamily8, 9, 10, 11, 12 share sequence homology of 30% to 50%. They are type I transmembrane glycoproteins composed of from 2 to 9 immunoglobulin superfamily domains, a hydrophobic transmembrane region, and a short cytoplasmic domain. ICAM-1 (CD54) has 5 extracellular immunoglobulin domains and is constitutively expressed on venular endothelium and some leukocytes. After stimulation with inflammatory cytokines (eg, TNF-α), most of the body's cell types can express
Leukocyte rolling
Migration of leukocytes from blood into tissue requires coordinated sequential interactions of numerous adhesion molecules. The simplest generic model posits that selectins initiate interactions of leukocytes with endothelial cells. Selectin binding takes place under dynamic conditions, where shear forces exerted by flowing blood act on leukocytes and platelets as they interact with each other and with endothelial cells. Selectin binding requires a threshold level of shear for leukocytes to
References (32)
Integrin regulation of lymphocyte trafficking: lessons from structural and signaling studies
Adv Immunol
(2007)- et al.
Structural basis for dimerization of ICAM-1 on the cell surface
Mol Cell
(2004) - et al.
ICAM-2 mediates neutrophil transmigration in vivo: evidence for stimulus specificity and a role in PECAM-1-independent transmigration
Blood
(2006) - et al.
Endothelial intercellular adhesion molecule (ICAM)-2 regulates angiogenesis
Blood
(2005) - et al.
Targeted gene deletion demonstrates that the cell adhesion molecule ICAM-4 is critical for erythroblastic island formation
Blood
(2006) - et al.
The JAM family of proteins
Adv Drug Deliv Rev
(2005) - et al.
Force as a facilitator of integrin conformational changes during leukocyte arrest on blood vessels and antigen-presenting cells
Immunity
(2007) - et al.
Platelet P-selectin is required for pulmonary eosinophil and lymphocyte recruitment in a murine model of allergic inflammation
Blood
(2005) - et al.
Golgi GDP-fucose transporter-deficient mice mimic congenital disorder of glycosylation iic/leukocyte adhesion deficiency II
J Biol Chem
(2007) - et al.
Leukocyte adhesion deficiency II patients with a dual defect of the GDP-fucose transporter
Blood
(2006)
Natural history and early diagnosis of LAD-1/variant syndrome
Blood
Cell adhesion molecules for targeted drug delivery
J Pharm Sci
Structural basis of integrin regulation and signaling
Annu Rev Immunol
Integrin ligands at a glance
J Cell Sci
Targeting integrin structure and function in disease
Adv Immunol
For catch bonds, it all hinges on the interdomain region
J Cell Biol
Cited by (0)
Disclosure of potential conflict of interest: The author has declared that he has no conflict of interest.