Abstract
At present the integrin superfamily consists of 15 α and 8 β subunits found in 20 heterodimeric combinations of receptor (Hynes 1992; Pardi et al 1992; Springer 1990). Leukocytes express at least 13 of these receptors (Hogg 1991). However, it is only the β2 integrins LFA-1, CR3/Mac-1 and p150,95 and the “homing receptor” β7 integrins, α4β7 and αHML-1β7 which are exclusively found on leukocytes. The VLA integrins of the β1 family which have specificity for extracellular matrix proteins such as fibronectin and collagen are expressed by leukocytes and also by other types of cells. This wide range of integrins renders immune cells well-equipped to enter into cell-cell adhesions and to interact with the subendothelial matrix. Many of these receptors are expressed at enhanced levels in memory T cells compared to naive T cells (Buckle and Hogg 1990; Sanders et al 1988). For example, the level of LFA-1 increases from 50–60,000 to 300,000 sites per memory T cell. Adhesion receptors are thought to have a major role in the response of memory T cells to antigen by enabling them to act rapidly through the promotion of cell-cell contact and also by facilitating movement into tissues.
Keywords
- Collagen Binding
- Cell BioI
- Malaria Infected Erythrocyte
- Divalent Cation Binding Site
- Extracellular Matrix Protein Binding
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Hogg, N. et al. (1993). Integrins and their Activation. In: Gergely, J., et al. Progress in Immunology Vol. VIII. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-51479-1_37
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DOI: https://doi.org/10.1007/978-3-642-51479-1_37
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