Vertebrate Integrins
The following are some of the integrins found in vertebrates:
| Name | Synonyms | Distribution | Ligands |
| α1β1 | Many | Collagens, laminins | |
| α2β1 | Many | Collagens, laminins | |
| α4β1 | VLA-4 | Hematopoietic cells | Fibronectin, VCAM-1 |
| α5β1 | fibronectin receptor | widespread | fibronectin and proteinases |
| α6β1 | laminin receptor | widespread | matrix macromolecules laminins |
| αLβ2 | LFA-1 | T-lymphocytes | ICAM-1, ICAM-2 |
| αMβ2 | Mac-1, CR3 | Neutrophils and monocytes | Serum proteins, ICAM-1 |
| αIIbβ3 | Fibrinogen receptor; gpIIbIIIa | Platelets | fibrinogen, fibronectin |
| αVβ3 | vitronectin receptor | activated endothelial cells, melanoma, glioblastoma | vitronectin, fibronectin, fibrinogen, osteopontin, Cyr61 |
| αVβ5 | widespread, esp. fibroblasts, epithelial cells | vitronectin and adenovirus | |
| αVβ6 | proliferating epithelia, esp. lung and liver | fibronectin; TGFβ1+3 | |
| α6β4 | Epithelial cells | Laminin |
Beta-1 integrins interact with many alpha integrin chains. Gene knockouts of integrins in mice are not always lethal, which suggests that during embryonal development, one integrin may substitute its function for another in order to allow survival. Some integrins are on the cell surface in an inactive state, and can be rapidly primed, or put into a state capable of binding their ligands, by cytokines. Integrins can assume several different well-defined shapes or "conformational states". Once primed, the conformational state changes to stimulate ligand binding, which then activates the receptors — also by inducing a shape change — to trigger outside-in signal transduction.
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