Abstract
Aconsiderable proportion of degenerative diseases is age-related. Advanced protein glycosylation increases with age and involves nonenzymatic covalent addition of carbohydrate to tissue proteins, and is a prominent feature of disorders affecting the normal biological functions of connective tissue, lens, blood vessels and nerves. In diabetes, tissue damage occurs over much shorter time periods than in normal individuals; thus, experimental studies have focused on diabetic models since the lesions are similar to those of old age.1 Advanced glycation end products modify structures and functions of the extracellular matrix, cell surface molecules including vitronectin, laminin, lens crystallin and collagens2 and may promote a generalized form of vasculopathy.3 Gangliosides have also been found to accumulate in senile cataracts; among them, sialyl-Lex neolacto-series gangliosides have been identified.4
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
Brownlee M. Advanced protein glycosylation in diabetes and aging. Ann Rev Med 1995; 46: 223–234.
Charonis AS, Reger LA, Dege JE et al. Laminin alterations after in vitro nonenzymatic glycosylation. Diabetes 1990; 39: 807814.
Cohen MP, Clements RS, Cohen JA et al. Glycated albumin promotes a generalized vasculopathy in the db/db mouse. Biochem Biophys Res Comm 1996; 218: 72–75.
Ogiso M, Okinaga T, Ohta M et al. Identification and synthetic pathway of sialylLewisx-containing neolacto-series ganglio-sides in lens tissues. 1. Characterization of gangliosides in human senile cataractous lens. Biochim Biophys Acta 1995; 1256: 166–174.
van Kamp GJ, Mulder K, Kuiper M et al. Changed transferrin sialylation in Parkinson’s disease. Clin Chim Acta 1995; 235: 159–167.
Hall NA, Patrick AD. Accumulation of dolichol-linked oligo-saccharides in ceroidlipofuscinosis (Batten disease). Am J Med Genetics Supplement 1988; 5: 221–223.
van Dessel G, Lagrou A, Hilderson H et al. Dolichyl-pyrophosphoryloligosaccharide protein oligosaccharide transferase in neuronal ceroid-lipofuscinosis. Biochem Cell Biol 1991; 70: 515–518.
Paton BC, Poulos A. Dolichol metabolism in cultured skin fibroblasts from patients with “neuronal” ceroid lipofuscinosis (Batten’s disease). J Inher Metab Dis 1984; 7: 112–116.
David MJ, Portoukalian J, Rebbaa A et al. Characterization of gangliosides from normal and osteoarthritic human articular cartilage. Arth Rheum 1993; 36: 938–942.
Mankin HJ, Lippiello L. The glycosaminoglycans of normal and arthritic cartilage. J Clin Invest 1971; 50: 1712–1719.
Richard M, Vignon E, Peschard M et al. Glycosyltransferase activities in chondrocytes from osteoarthritic and normal human articular cartilage. Biochem Int 1990; 22: 535542.
Schorderet M. Alzheimers disease: fundamental and therapeutic aspects. Experientia 1995; 51: 99–105.
Saito F, Tani A, Miyatake T et al. N-linked oligosaccharide of ß-amyloid precursor protein (3APP) of C6 glioma cells: putative regulatory role in 3APP processing. Biochem Biophys Res Comm 1995; 210: 703–710.
Griffith LS, Schmitz B. 0-linked Nacetylglucosamine is upregulated in Alzheimer brains. Biochem Biophys Res Comm 1995; 213: 424–431.
Graebert KS, Popp GM, Kehle T et al. Regulated 0-glycosylation of the Alzheimer 3-A4 amyloid precursor protein in thyrocytes. Eur J Cell Biol 1995; 66: 39–46.
Godfroid E, Octave J-N. Glycosylation of the amyloid peptide precursor containing the Kunitz protease inhibitor domain improves the inhibition of trypsin. Biochem Biophys Res Comm 1990; 171: 1015–1021.
Pepys MB, Rademacher TW, AmatayakulChantler S et al. Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. Proc Natl Acad Sci USA 1994; 91: 5202–5206.
Fraser PE, Nguyen JT, Chin DT et al. Effects of sulfate ions on Alzheimer ß/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions. J Neurochem 1992; 59: 1531–1540.
Good AH, Cooper DKC, Malcolm AJ et al. Identification of carbohydrate structures that bind human antiporcine antibodies: Implications for discordant xenografting in humans. Transplant Proc 1992; 24: 559–562.
Oriol R, Ye Y, Koren E et al. Carbohydrate antigens of pig tissues reacting with human natural antibodies as potential targets for hyperacute vascular rejection in pig-to-man transplantation. Transplant 1993; 56: 1433–1442.
Oriol R, Ye Y, Koren E et al. Carbohydrate antigens of vascular endothelium and other pig tissues reacting with human natural antibodies. Transplant Proc 1994; 26: 1398.
Galili U, Macher B, Buehler J et al. Human natural anti-a-galactosyl IgG, II The specific recognition of a(1–3) linked galactose residues. J Exp Med 1985; 162: 573.
Galili U, Shohet SB, Kobrin E et al. Man, apes and old world monkeys differ from other mammals in the expression of a-galactosyl epitopes on nucleated cells. J Biol Chem 1988; 263: 17755–17762.
Thibaudeau K, Anegon I, Lemauff B et al. Human antibodies to porcine platelets. Transplantation 1994; 57: 1110–1115.
Platt JL, Lindman BJ, Chen H et al. Endothelial cell antigens recognized by xenoreactive human natural antibodies. Transplantation 1990; 50: 817–822.
Platt JL, Holzknecht ZE. Porcine platelet antigens recognized by human xenoreactive natural antibodies. Transplantation 1994; 57: 327–335.
Rollins S, Evans M, Johnson K et al. Molecular and functional analysis of porcine Eselectin reveals a potential role in xenograft rejection. Biochem Biophys Res Comm 1994; 204: 763–771.
Young DSF, Asano H, Takahashi M et al. Unpublished.
Tearle RG, Tange MJ, Zannettino ZL et al. The a-1,3-galactosyltransferase knockout mouse. Implications for xenotransplantation.Transplantation 1996; 61: 13–19.
Young DSF, Kadokura M, Brockhausen I et al. Human lectins induce apoptosis-another pathway to xenograft rejection. Transplantation Proceed 1996; 28: 611–612.
Soares M, Latinne D, Elsen M et al. In vivo depletion of xenoreactive natural antibodies with an anti-g monoclonal antibody. Transplant 1993; 56: 1427–1433.
Young DSF, Asano H, Brockhausen I et al. Isolation and use of specific human preformed antibodies recognizing pig xenoantigens. Proceed XVth World Congress of Transplantation 1994; Kyoto.
Gustafsson K, Strahan K, Preece A. al-3 Galactosyltransferase: a target for in vivo genetic manipulation in xenotransplantation. Immun Rev 1994; 141: 59–67.
Lemarchand P, Jones M, Yamada I et al. In vivo gene transfer and expression in normal uninjured blood vessels using replication-deficient recombinant adenovirus vectors. Circulation Res 1993; 72: 1132–1138.
Fodor W, Williams B, Matis L et al. Expression of a functional human complement inhibitor in a transgenic pig as a model for the prevention of xenogeneic hyperacute organ rejection. Proc Natl Acad Sci USA 1994; 91: 11153–11157.
Golub E, Green D. In: Sunderland MA. eds Immunology: A Synthesis. Sinauer 2nd Ed. 1991: 664–666
Koike C. Kannagi R, Takuma Y et al. Introduction of a(1,2)-fucosyltransferase and its effect on a-Gal epitopes in transgenic pig. Xenotransplantation 1996; 3: 81–86.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Brockhausen, I., Kuhns, W. (1997). Glycoproteins in Degenerative Disease and Xenograft Rejection. In: Glycoproteins and Human Disease. Medical Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-21960-7_18
Download citation
DOI: https://doi.org/10.1007/978-3-662-21960-7_18
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-21962-1
Online ISBN: 978-3-662-21960-7
eBook Packages: Springer Book Archive