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Haptoglobin

A Potential Reporter Molecule for Glycosylation Changes in Disease

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Glycoimmunology

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 376))

Abstract

The acute-phase protein, haptoglobin, is elevated in many diseases; however, its glycosylation also changes, and the type of change observed can vary with disease. Increased fucosylation is a common finding, and the fucose-specific lectin, lotus tetragonolobus, can be used to differentiate different diseases (eg inflammatory conditions, liver diseases), and to monitor disease activity in cancer. Changes in N-acetyl neuraminic acid and N-acetylglu-cosamine suggest that particular carbohydrate structures predominate in certain diseases. Because haptoglobin glycosylation provides a record of previous intracellular events, it will help to improve our understanding of pathological processes and provide potential clinical markers for the future.

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References

  1. Dobryszycka W., 1993, Haptoglobin: retrospectives and perspectives, In: Mackiewicz A., Kushner, I., and Baumann H., eds. Acute phase proteins: molecular biology, biochemistry, and clinical applications, Boca Raton: CRC Press, 185–206.

    Google Scholar 

  2. Thompson, S., and Turner, O.A., 1987, Elevated levels of abnormally-fucosylated haptoglobins in cancer sera, Br.J.Cancer 56:605–610.

    Article  PubMed  CAS  Google Scholar 

  3. Katnik,I., Greber,J., and Dobryszycka,W., 1987, Affino-imniunoelectrophoresis of haptoglobin with wheat germ agglutinin. Diagnostic significance in ovarian cancer, Afch.Immunol.Therap.Exp. 35:547–551.

    CAS  Google Scholar 

  4. Thompson,S., Kelly,C.A., Griffiths,I.D. and Turner G.A., 1989, Abnormally-fucosylated serum haptoglobins in patients with inflammatory joint disease, Clin.Chim.Acta 184:251–258.

    Article  PubMed  CAS  Google Scholar 

  5. Thompson,S., Cantwell,B.M.J., Cornell,C., and Turner, G.A., 1991, Abnormally-fucosylated haptoglobin: a cancer marker for tumour burden but not gross liver metastasis, Br.J.Cancer 64:386–390.

    Article  PubMed  CAS  Google Scholar 

  6. Thompson,S., Record,C.O., and Turner,G.A., 1991, Studies of lotus-extracted haptoglobin in inflammatory bowel disease, Biochem.Soc.Trans. 19:264S

    PubMed  CAS  Google Scholar 

  7. Thompson,S., Matta,K.L., and Turner,G.A., 1991, Changes in fucose metabolism associated with heavy drinking and smoking: a preliminary report, Clin.Chim.Acta 201:59–64.

    Article  PubMed  CAS  Google Scholar 

  8. Thompson,S., Dargan,E., and Turner,G.A., 1992, Increased fucosylation and other carbohydrate changes in haptoglobin in ovarian cancer, Cancer Letters 66:43–48.

    Article  PubMed  CAS  Google Scholar 

  9. Chambers.W., Thompson,S., Skillen,A.W., Record,C.O., and Turner,G.A., 1993 Abnormally-fucosylated haptoglobin as a marker for alcoholic liver disease but not excessive alcohol consumption or non-alcoholic liver disease, Clin.Chim.Acta 219:177–182.

    Article  PubMed  CAS  Google Scholar 

  10. Thompson,S., Dargan,E., Griffiths,I.D., Kelly,C.A., Turner,G.A., 1993 The glycosylation of haptoglobin in rheumatoid arthritis, Clin.Chim.Acta 220,107–114.

    Article  PubMed  CAS  Google Scholar 

  11. Mann,A.C., Record,C.O., Self,C.H., and Turner,G.A., 1994 Monosaccharide composition of haptoglobin in liver diseases and alcohol abuse: large changes in glycosylation associated with alcoholic liver disease, Clin.Chim.Acta 227:69–78.

    Article  PubMed  CAS  Google Scholar 

  12. Dargan E., Thompson,S., Cantwell,B.M.J., Wilson,R.G., and Turner,G.A., 1994, Changes in the fucose content of haptoglobin in breast and ovarian cancer: association with disease progression, Glycosyl. &Dis. 1:37–43.

    Google Scholar 

  13. Katnik,I., Jadach,J., Krotkiewski,H., and Gerber,J., 1994, Investigating the glycosylation of normal and ovarian cancer haptoglobins using digoxigenin-labelled lectins, Glycosyl. &Dis. 2:97-104. 11.

    Google Scholar 

  14. Turner,G.A., Skillen,A.W., Buamah,P., Guthrie,D., Welsh,J., Harrison,J., and Kowalski,A., 1985 Relation between raised concentrations of fucose, sialic acid, and the acute phase proteins in serum from patients with cancer: choosing suitable serum glycoprotein markers, J.Clin.Path.38:588–592.

    Article  PubMed  CAS  Google Scholar 

  15. Nilsson,B., Lowe,M., Osada,J., Ashwell,G., and Zopf,D., 1981, The carbohydrate structure of human haptoglobin 1-1, In: Yamakawa,T., et.al. eds. Glycoconjugates. Proc. 6th Int. Sym. Glyco. Tokyo: Japan Scientific Societies Press, 275–276.

    Google Scholar 

  16. Kaartinen V., and Mononen,I., 1988 Hemoglobin binding to deglycosylated haptoglobin, Biochim.Biophys.Acta 953:345–352.

    Article  PubMed  CAS  Google Scholar 

  17. Turner,G.A., 1992, N-glycosylation of serum proteins in disease and its investigation using lectins, Clin.Chim.Acta 208:149–171.

    Article  PubMed  CAS  Google Scholar 

  18. Anderson N.L., and Anderson N.G., 1979, Micoheterogeneity of serum transferrin, haptoglobin and α2HS glycoprotein examined by high resolution two-dimensional electrophoresis, Biochem.Biophys.Res.Comm. 88:258–265.

    Article  PubMed  CAS  Google Scholar 

  19. Katnik,I., 1984, Studies on haptoglobin binding to concanavalin A, Biochim.Biophy.Acta 790:8–14

    Article  CAS  Google Scholar 

  20. Katnik,I., 1987, Factors influencing the reaction of haptoglobin with concanavalin A in affino-immunoelectrophoresis, Arch. Immunol. Therap. Exp. 35: 267–275.

    CAS  Google Scholar 

  21. Katnik,I., and Dobryszycka,W., 1992, Development of concanavalin A-enzyme immunosorbent assay for glycated haptoglobin using polyclonal and monoclonal antibodies, J.Immuno. 13: 145–

    Article  CAS  Google Scholar 

  22. Thompson,S., Stappenbeck,R., Turner,G.A., 1989, A multiwell lectin-binding assay using lotus tetragonolobus for measuring different glycosylated forms of haptoglobin, Clin. Chim. Acta 180: 277–284.

    Article  PubMed  CAS  Google Scholar 

  23. Thompson S., Lathan J.A.E., and Turner G.A., 1987, A simple, reproducible and cheap batch method for the analysis of serum glycoproteins using Sepharose-coupled lectins and silver staining, Clin. Chim. Acta 167: 217–223.

    Article  PubMed  CAS  Google Scholar 

  24. Petryniak, J., and Goldstein, I.J., 1986, Immunochemical studies on the interaction between synthetic glycoconjugates and α-L-fucosyl binding lectins, Biochemistry 25: 2829–2838.

    Article  PubMed  CAS  Google Scholar 

  25. Debray, H., Decout, D., Strecker, G., Spik, G., and Montreuil J., 1981, Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycoproteins, Eur.J.Biochemistry 117, 41–55.

    Article  CAS  Google Scholar 

  26. van Dijk, W., Turner, G.A., and Mackiewicz, A., 1994, Changes in glycosylation of acute-phase proteins in health and disease: occurrence, regulation and function, Glycosylation. &Dis. 1: 5–14.

    CAS  Google Scholar 

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© 1995 Springer Science+Business Media New York

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Turner, G.A. (1995). Haptoglobin. 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_25

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  • DOI: https://doi.org/10.1007/978-1-4615-1885-3_25

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5768-1

  • Online ISBN: 978-1-4615-1885-3

  • eBook Packages: Springer Book Archive

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