Abstract
The human CD8 glycoprotein is expressed on the surface of class I HLA-restricted T-lymphocytes (generally cytotoxic or suppressor cells). CD8 has been implicated as having various functional properties. (i) The extracellular moiety of CD8 recognizes a nonpolymorphic region of class I HLA molecules of antigen presenting cells (Rosenstein et al., 1989); during T-cell activation a ternary complex is formed, in which CD8 and T-cell receptor associate with the same HLA molecule, therefore CD8 operates as a co-receptor for target cells (Salter et al., 1990). (ii) The binding of CD8 with class I HLA molecules triggers an intracellular signal through the T-cell specific p56lck, a member of the src-familyof cytoplasmic protein-tyrosine kinases (Veillette et al., 1988; Turner et al., 1990); this molecule is associated noncovalently with the intracellular moiety of CD8 and this association appears to be necessary for maximal activation of cytotoxic T-lymphocytes (Karnitz et al., 1992). (iii) During T-cells maturation the expression of CD8 is crucial for the positive selection of mature class I-reactive T-cells (Ramsdell and Fowlkes, 1989).
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Serafini-Cessi, F., Martire, G., Malagolini, N., Pascale, M.C., Erra, M.C., Bonatti, S. (1995). Glycosylation and Maturation Rate of Membrane and Secretory Forms of Human CD8α Glycoprotein. In: Alavi, A., Axford, J.S. (eds) Glycoimmunology. Advances in Experimental Medicine and Biology, vol 376. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1885-3_12
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DOI: https://doi.org/10.1007/978-1-4615-1885-3_12
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