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).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Bierhuizen, M.F.A., and Fukuda, M., 1992, Expression cloning of a cDNA encoding UDP-GlcNAc:Galβ1-3-GalNAc-R (GlcNAc to GalNAc) β1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumour antigen, Proc. Natl. Acad. Sci. 89:9326–9330.
Bonatti, S., Migliaccio, G., and Simons, K., 1989, Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum, J. Biol. Chem. 264:12590–12595.
Carlsson, S.R., Sasaki, H., and Fukuda, M., 1986, Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell, J. Biol. Chem. 261:12787–12795.
Casabò, L.G., Mamalaki, C., Kioussis, D., and Zamoyska, R., 1994, T cell activation results in physical modification of the mouse CD8β chain, J. Immunol. 152:397–404.
Cyster, J.G., Shotton, D.M., and Williams, A.F., 1991, The dimensions of the T lymphocyte glycoprotein leukosialin and identification of linear protein epitopes that can be modified by glycosylation, EMBO J. 10:893–902.
Fukuda, M., 1991, Leukosialin, a major O-glycan-containing sialoglycoprotein defining leukocyte differentiation and malignancy, Glycobiology 1:347–356.
Gerken, T.A., Butenhof, K.J., and Shogren, R., 1989, Effects of glycosylation on the conformation and dynamics of (O-linked glycoproteins: carbon-13 NMR studies of ovine submaxillary mucin, Biochemistry 28:5536–5543.
Gething, M-J., and Sambrook, J., 1992, Protein folding in the cell, Nature 355:33–45.
Karnitz, L., Sutor, S.L., Torigoe, T., Reed, J.C., Bell, M.P., McKean, D.J., Leibson, P.J., and Abraham, R.T., 1992, Effects of p56lck deficiency on the growth and cytolytic effector function of an interleukin-2-dependent cytotoxic T-cell line, Mol. Cell. Biol. 12:4521–4530.
Jackson, M.R., Nilsson, T., and Peterson, P.A., 1993, Retrieval of transmembrane proteins to the endoplasmic reticulum, J. Cell Biol. 121:317–333.
Jentoft, N., 1990, Why are proteins O-glycosylated?, Trends. Biochem. Sci. 15:291–294.
Leahy, D.J., Axel, R., and Hendrickson, W.A., 1992, Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution Cell 68:1145–1162.
Littman, D.R., Thomas, Y., Maddon, P.J., Chess, L., and Axel, R., 1985, The isolation and sequence of the gene encoding T8: a molecule defining functional classes of T lymphocytes, Cell 40:237–246.
Norment, A.M., and Littman, D.R., 1988, A second subunit of CD8 is expressed in human T cells, EMBO J. 7:3433–3439.
Pascale, M.C., Malagolini, N., Serafmi-Cessi, F., Migliaccio, G., Leone, A., and Bonatti, S., 1992a, Biosynthesis and oligosaccharide structure of human CD8 glycoprotein expressed in a rat epithelial cell line, J. Biol. Chem. 267:9940–9947.
Pascale, M.C., Erra, M.C., Malagolini, N., Serafini-Cessi, F., Leone, A., and Bonatti, S., 1992b, Post-translational processing of an O-glycosylated protein, the human CD8 glycoprotein, during the intracellular transport to the plasma membrane, J. Biol. Chem. 267:25196–25201.
Pelham, H.R.B., 1989, Control of protein exit from the endoplasmic reticulum, Annu. Rev. Cell Biol, 5:1–23.
Piller, F., Piller, V., Fox, R.I., and Fukuda, M., 1988, Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis, J. Biol. Chem. 263:15146–15150.
Piller, V., Piller, F., Klier, F.G., Fukuda, M., 1989, O-glycosylation of leukosialin in K562 cells, Eur. J. Biochem. 183:123–135.
Piller, F., Le Deist, F., Weinberg, K.I., Parkman, R., and Fukuda, M., 1991, Altered O-glycan synthesis in lymphocytes from patients with Wiskott-Aldrich syndrome, J. Exp. Med. 173:1501–1510.
Ramsdell, F., and Fowlkes, B.J., 1989, Engagement of CD4 and CD8 accessory molecules is required for T cell maturation, J. Immunol. 143:1467–1471.
Rose, M.C., Voter, W.A., Sage, H., Brown, C.F., and Kaufman, B., 1984, Effects of deglycosylation on the architecture of ovine submaxillary mucin glycoprotein, J. Biol. Chem. 259:3167–3172.
Rosenstein, Y., Ratnofsky, S., Burakoff, S.J., and Herrmann, S.H., 1989, Direct evidence for binding of CD8 to HLA class I antigens, J. Exp. Med. 169:149–160.
Salter, R.D., Benjamin, R.J., Wesley, P.K., Buxton, S.E., Garrett, T.P.J., Clayberger, C., Krensky, A.M., Norment, A.M., Littman, D.R., and Parham, P., 1990, A binding site for the T-cell co-receptor CD8 on the α3 domain of HLA-A2, Nature 345:41–46.
Saraste, J., and Kuismanen, E., 1984, Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface, Cell 38:535–549.
Serafmi-Cessi, F., Dall’Olio, F., Malagolini, N., and Campadelli-Fiume, G., 1989, Temporal aspects of O-glycosylation of glycoprotein C from herpes simplex virus type-1, Biochem. J. 262:479–484.
Serafini-Cessi, F., Malagolini, N., Dall’Olio, F., Pereira, L., and Campadelli-Fiume, G., 1985, Oligosaccharide chains of Herpes simplex virus type 2 glycoprotein gG2, Arch. Biochem. Biophys. 240:866–876.
Shogren, R., Gerken, T.A., and Jentoft, N., 1989, Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: light-scattering studies of ovine submaxillary mucin, Biochemistry 28:5525–5536.
Snow, P.M., and Terhorst, C., 1983, The T8 antigen is a multimeric complex of two distinct subunits on human thymocytes but consists of homomultimeric forms on peripheral blood T lymphocytes, J. Biol. Chem. 258:14675–14681.
Snow, P.M., Coligan, J.E., and Terhorst, C., 1985, Analysis of the structure of the human T cell surface antigen T8 by limited proteolysis and chemical cleavage, J. Biol. Chem. 260:2700–2708.
Turner, J.M., Brodsky, M.H., Irving, B.A., Levin, S.D., Perlmutter, R.M., and Littman, D.R., 1990, Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs, Cell 60:755–765.
Veillette, A., Bookman, M.A., Horak, E.M., and Bolen, J.B., 1988, The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck, Cell 55:301–308.
Wilson, I.B.H., Gavel, Y., and von Heijne, G., 1991, Amino acid distributions around O-linked glycosylation sites, Biochem. J. 275:529–534.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
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
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1885-3_12
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5768-1
Online ISBN: 978-1-4615-1885-3
eBook Packages: Springer Book Archive