Abstract
animal cell plasma membranes contain asymmetrically-distributed glycoproteins and glycolipids which extend their carbohydrate-bearing portions directly into the extracellular environment, and there is currently a great deal of interest in the possible involvement of such molecules in the many aspects of cell recognition. The cell membranes of bacteria, fungi and higher plants are, in general, in contact with a complex carbohydrate-rich cell wall which complicates characterization of sugar-containing plasma membrane components. The cell wall, moreover, shields the underlying membrane from direct interaction with the cell surroundings, and the present chapter will accordingly be mainly concerned with the structure and function of the glycolipids and glycoproteins of animal cell plasma membranes.
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References
Cook, G. M. W. and Stoddart, R. W. (1973) Surface Carbohydrates of the Eukaryotic Cell, Academic Press, London.
Hughes, R. C. (1976) Membrane Glycoproteins—A Review of Structure and Function, Butterworths, London.
Cook, G. M. W. (1976) ‘Techniques for the analysis of membrane carbohydrates’ in Biochemical Analysis of Membranes (ed. A. H. Maddy ), Chapman and Hall, London, 283–351.
Chen, W. W. and Lennarz, W. J. (1978) ‘Enzymic excision of glucosyl units linked to the oligosaccharide chains of glycoproteins’ J. Biol. Chem., 253, 5780–5785.
Parodi, A. J. and Leloir, L. F. (1979) ‘ The role of lipid intermediates in the glycosylation of proteins in the eucaryotic cell’ Biochim. Biophys. Acta, 559, 1–37.
Robbins, P. W., Hubbard, S. C., Turco, S. J. and Wirth, D. F. (1977) ‘ Proposal for a common oligosaccharide intermediate in the synthesis of membrane glycoproteins’ Cell, 12, 893–900.
Staneloni, R. J. and Leloir, L. F. (1979) ‘ The biosynthetic pathway of the asparagine-linked oligosaccharides of glycoproteins’ Trends in Biochem. Sci., 65–67.
Sturgess, J., Moscarello, M. and Schachter, H. (1978) ‘ The structure and biosynthesis of membrane glycoproteins’ in Current Topics in Membranes and Transport, vol. 11 (ed. F. Bronner et al.), Academic Press, New York, 15–104.
Tabas, I. and Kornfeld, S. (1978) ‘ The synthesis of complex-type oligosaccharides. III’ J. Biol. Chem., 253, 7779–7786.
Waechter, C. J. and Lennarz, W. J. (1976) ‘ The role of polyprenol-linked sugars in glycoprotein synthesis’ Ann. Rev. Biochem., 45, 95–112.
Hakomori, S-I, Watanabe, K. and Laine, R. A. (1977) ‘ Glycosphingolipids with blood group A, H and I activity and their changes associated with ontogenesis and oncogenesis’ Pure App. Chem., 49, 1215–1227.
Hanfland, P. (1975) ‘ Characterization of B and H blood group active glycosphingolipids from human B erythrocyte membranes’ Chem. Phys. Lipids, 15, 105–124.
Gardas, A. (1978) ‘ Structure of an (A-blood group)—active glycolipid isolated from human erythrocytes’ Eur. J. Biochem., 89, 471–473.
Watkins, W. M. (1972) ‘ Blood group specific substances’ in Glycoproteins, their Composition, Structure and Function, Part B (ed. A. Gottschalk), Elsevier, Amsterdam, 830–891.
Blumenfeld, O. O. and Admany, A. M. (1978) ‘ Structural polymorphism within the amino-terminal region of MM, NN and MN glycoproteins (glycophorins) of the human erythrocyte membrane’ Proc. Natl. Acad. Sci., 75, 2727–2731.
Dahr, W., Uhlenbruck, G., Janssen, E. and Schmalisch, R. (1977) ‘ Different N-terminal amino acids in the MN-glycoprotein from MM and NN erythrocytes’ Hum. Genet., 35, 335–343.
Furthmayr, H. (1978) ‘ Structural comparison of glycophorins and immunochemical analysis of genetic variants’ Nature, 271, 519–524.
Lisowska, E. and Wasniowska, K. (1978) Immunochemical characterization of cyanogen bromide degradation products of M and N blood group glycopeptides’ Eur. J. Biochem., 88, 247–252.
Sadler, J. E., Paulson, J. C. and Hill, R. L. (1979) ‘ The role of sialic acid in the expression of human MN blood group antigens’ J. Biol. Chem., 254, 2112–2119.
Springer, G. F. and Yang, H. J. (1977) ‘ Isolation and partial characterization of blood group M- and N- specific glycopeptides and oligosaccharides from human erythrocytes’ Immunochemistry, 14, 497–502.
Tomita, M., Furthmayr, H. and Marchesi, V. T. (1978) ‘ Primary structure of human erythrocyte glycophorin A. Isolation and characterization of peptides and complete amino acid sequence’ Biochemistry, 17, 4756–4770.
Barnstaple, C. J., Jones, E. A. and Crumpton, M. J. (1978) ‘ Isolation, structure and genetics of HLA-A, -B, -C and -DRw (Ia) antigens’ Br. Med. Bull., 34, 241–246.
Bodmer, W. F. (1978) ‘ The HLA system: introduction’ Br. Med. Bull., 34, 213–216.
Cunningham, B. A. (1977) ‘ The structure and function of histocompatibility antigens’ Scientific American, 237, 96–107.
Letarte, M. (1978) ‘ Glycoprotein antigens of murine lymphocytes’ in Current Topics in Membranes and Transport, vol. 11 (ed. F. Bronner et al.), Academic Press, New York, 463–512.
McKenzie, I. F. C., Clarke, A. and Parish, C. R. (1977) ‘ Ia antigenic specificities are oligosaccharide in nature: Hapten inhibition studies’ J. Exp. Med., 145, 1039–1053.
Snary, D., Barnstaple, C., Bodmer, W. F., Goodfellow, P. and Crumpton, M. J. (1977) ‘ Human la antigens—purification and molecular structure’ Cold Spring Harbor Symp. Quant. Biol., 41, 379–386.
Springer, T. A., Kaufman, J. F., Terhorst, C., and Strominger, J. L. (1977) ‘ Purification and structural characterization of human HLA-linked B-cell antigens’ Nature, 268, 213–218.
Williams, A. F., McMaster, R., Standring, R. and Sunderland, C. A. (1978) ‘ Differentiation antigens and glycoproteins of lymphocytes’ Trends in Biochem. Sci., 272–274.
Draper, R. K., Chin, D. and Simon, M. 1. (1978) ‘ Diphtheria toxin has the properties of a lectin’ Proc. Natl. Acad. Sci., USA, 75, 261–265.
Kohn, L. D. (1978) ‘ Relationships in the structure and function of receptors for glycoprotein hormones, bacterial toxins and interferon’ in Receptors and Recognition, vol. AS (ed. P. Cuatrecasas and M. L. Greaves ), Chapman and Hall, London, 133–212.
Pappenheimer, Jr., A. M. (1978) ‘ Diphtheria: molecular biology of an infectious process’ Trends in Biochem. Sci., N220–224.
van Heyningen, W. E. (1974) ‘ Gangliosides as membrane receptors for tetanus toxin, cholera toxin and serotonin‘ Nature, 249, 415–417.
Aminoff, D., Bell, W. C. and Vorder Bruegge, W. G. (1978) ‘ Cell surface carbohydrate recognition and the viability of erythrocytes in circulation’ in Cell Surface Carbohydrates and Biological Recognition (ed. V. J. Marchesi et al.), Alan R. Liss, Inc., New York, 569–581.
Ashwell, G. and Morel], A. G. (1977) ‘ Membrane glycoproteins and recognition phenomena’ Trends in Biochem. Sci., 76–78.
Gesner, B. M., Woodruff, J. J. and McCluskey, R. T. (1969) ‘ An autoradiographic study of the effect of neuraminidase or trypsin on transfused lymphocytes’ Amer. J. Pathol., 57, 215–224.
Paulson, J. C., Hill, R. L., Tanabe, T. and Ashwell, G. (1977) ‘ Reactivation of asialo-rabbit liver binding protein by resialylation with ß-D-galactoside a2– 6 sialyltransferase’ J. Biol. Chem., 252, 8624–8628.
Gottschalk, A., Belyavin, G. and Biddle, F. (1972) ‘ Glycoproteins as influenza virus haemagglutinin inhibitors and as cellular virus receptors’ in Glycoproteins, Their Composition, Structure and Function Part B (ed. A. Gottschalk ), Elsevier, Amsterdam, 1082–1096.
Helenius, A., Morein, B., Fries, E., Simons, K., Robinson, P., Schirrmacher, V., Terhorst, C. and Strominger, J. L. (1978) ‘ Human (HLA-A and HLA-B) and murine (H-2K and H-2D) histocompatibility antigens are cell surface receptors for Semliki Forest virus’ Proc. Natl. Acad. Sci., USA, 75, 3846–3850.
Ofek, I., Beachey, E. H. and Sharon, N. (1978) ‘ Surface sugars of animal cells as deter- minants of recognition in bacterial adherence’ Trends in Biochem. Sci., 159–160.
Waterfield, M. D., Espelie, K. and Elder, K. (1979) ‘ Structure of the haemagglutinin of influenza virus’ Br. Med. Bull., 35, 57–63.
Frazier, W. A. (1978) ‘The role of cell surface components in the morphogenesis of the cellular slime molds’ Trends in Biochem. Sci., 130–133.
Glaser, L. (1978) ‘ Cell-cell adhesion studies with embryonal and cultured cells’ Rev. Physiol. Pharmacol., 83, 89–122.
Hynes, R. O. and Destree, A. T. (1978) ‘Relationships between fibronectin (LETS protein) and actin’ Cell, 15, 875–886.
Pena, S. D. J. and Hughes, R. C. (1978) ‘Fibronectin-plasma membrane interaction in the adhesion and spreading of hamster fibroblasts’ Nature, 276, 80–83.
Rees, D. A., Lloyd, C. W. and Thom, D. (1977) ‘ Control of grip and stick in cell adhesion
through lateral relationships of membrane glycoproteins’ Nature,267 124–128.
Thom, D., Powell, A. J. and Rees, D. A. (1979) ‘ Mechanisms of cellular adhesion IV. Role of serum glycoproteins in fibroblast spreading on glass’ J. Cell. Sci., 35, 281–305.
Yamada, K. M. and Olden, K. (1978) ‘Fibronectins—adhesive glycoproteins of cell surface and blood’ Nature, 275, 179–184.
Bramwell, M. E. and Harris, H. (1979) ‘Some further information about the abnormal membrane glycoprotein associated with malignancy’ Proc. R. Soc. London, B, 203, 93–99.
Hakomori, S-I. (1975) ‘ Structures and organization of cell surface glycolipids. Dependency on cell growth and malignant transformation’ Biochim. Biophys. Acta, 417, 55–89.
Nicolson, G. L. (1976) ‘ Trans-membrane control of the receptors on normal and tumour cells. II. Surface changes associated with transformation and malignancy’ Biochim. Biophys. Acta, 458, 1–72.
Nicolson, G. L. (1979) ‘Cancer metastasis’ Scientific American, 240, 50–60. Old, L. J. (1977) ‘ Cancer immunology’ Scientific American, 236, 62–79.
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© 1980 R. Harrison, G. G. Lunt
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Harrison, R., Lunt, G.G. (1980). Glycoproteins, Glycolipids and Cellular Recognition. In: Biological Membranes. Tertiary Level Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-4616-7_7
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DOI: https://doi.org/10.1007/978-1-4757-4616-7_7
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