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The structure of the keratan sulphate chains attached to fibromodulin from human articular cartilage

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Abstract

The small keratan sulphate proteoglycan, fibromodulin, has been isolated from pooled human articular cartilage. The main chain repeat region and the chain caps from the attached N-linked keratan sulphate chains have been fragmented by keratanase II digestion, and the oligosaccharides generated have been reduced and isolated. Their structures and abundance have been determined by high pH anion-exchange chromatography.

These regions of the keratan sulphate from human articular cartilage fibromodulin have been found to have the following general structure:

Significantly, both α(2-6)- and α(2-3)-linked N-acetyl-neuraminic acid have been found in the capping oligosaccharides. Fucose, which is α(1-3)-linked as a branch to N-acetylglucosamine, has also been found along the length of the repeat region and in the capping region. The chains, which have been found to be very highly sulphated, are short; the length of the repeat region and chain caps is ca. nine disaccharides.

These data demonstrate that the structure of the N-linked keratan sulphate chains of human articular cartilage fibromodulin is similar, in general, to articular cartilage derived O-linked keratan sulphate chains. Further, the general structure of the keratan sulphate chains attached to human articular cartilage fibromodulin has been found to be generally similar to that of both bovine and equine articular cartilage fibromodulin.

Abbreviations: KS, keratan sulphate; IEC, ion-exchange chromatography; ELISA, enzyme linked immunosorbent assay; Gal, β-D-galactose; Fuc, α-L-Fucose; GlcNAc, N-acetylglucosamine (2-acetamido-β-D-glucose); GlcNAc-ol, N-acetylglucosaminitol (2-acetamido-D-glucitol); NeuAc, N-acetyl-neuraminic acid; 6S/(6S), O-ester sulphate group on C6 present/sometimes present; NMR -nuclear magnetic resonance; HPAE, high pH anion-exchange; PED, pulsed electrochemical detection; HPLC, high performance liquid chromatography

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References

  1. Sztrolovics R, Chen XN, Grover J, Roughley PJ, Korenberg JR (1994) Genomics 23: 715–17.

    Article  PubMed  CAS  Google Scholar 

  2. Heinegard D, Larsson T, Sommarin Y, Franzen A, Paulsson M, Hedbom E (1986) J Biol Chem 261: 13866–72.

    PubMed  CAS  Google Scholar 

  3. Oldberg A, Antonsson P, Lindblom K, Heinegard D (1989) EMBO J 8: 2601–4.

    PubMed  CAS  Google Scholar 

  4. Garg HG, Lyon NB (1991) Adv Carbohydr Chem Biochem 49: 239–61.

    PubMed  CAS  Google Scholar 

  5. Antonsson P, Heinegard D, Oldberg A (1993) Biochim Biophys Acta 1174: 204–6.

    PubMed  CAS  Google Scholar 

  6. Antonsson P, Heinegard D, Oldberg A (1991) J Biol Chem 266: 16859–61.

    PubMed  CAS  Google Scholar 

  7. Plaas AHK, Neame PJ, Nivens CM, Reiss L (1990) J Biol Chem 265: 20634–40.

    PubMed  CAS  Google Scholar 

  8. Lauder RM, Huckerby TN, Nieduszynski IA (1994) Biochem J 302: 417–23.

    PubMed  CAS  Google Scholar 

  9. Lauder RM, Huckerby TN, Nieduszynski IA (1995) Glycoconjugate J 12: 651–59.

    Article  CAS  Google Scholar 

  10. Lauder RM, Huckerby TN, Nieduszynski IA (1996) Eur J Biochem 242: 402–9.

    Article  PubMed  CAS  Google Scholar 

  11. Vogel KG, Paulsson M, Heinegard D (1984) Biochem J 223: 587–97.

    PubMed  CAS  Google Scholar 

  12. Hedbom E, Heinegard D (1989) J Biol Chem 264: 6898–905.

    PubMed  CAS  Google Scholar 

  13. Noyori K, Jasin HE (1994) Arthr Rheum 37: 1656–63.

    CAS  Google Scholar 

  14. Hedlund H, Mengarelliwidholm S, Heinegard D, Reinholt FP, Svensson O (1994) Matrix Biol 14: 227–32.

  15. Bray BA, Lieberman R, Meyer K (1967) J Biol Chem 242: 3373–80.

    PubMed  CAS  Google Scholar 

  16. Krusius T, Finne J, Margolis RK, Margolis RU (1986) J Biol Chem 261: 8237–42.

    PubMed  CAS  Google Scholar 

  17. Bhavanandan VP, Meyer K (1968) J Biol Chem 243: 1052–59.

    PubMed  CAS  Google Scholar 

  18. Nieduszynski IA, Huckerby TN, Dickenson JM, Brown GM, Tai GH, Morris HG, Eady S (1990) Biochem J 271: 243–45.

    PubMed  CAS  Google Scholar 

  19. Nakazawa K, Ito M, Yamagata T, Suzuki S (1989) In Keratan Sulphate: Chemistry, Biology and Chemical Pathology (Greiling H, Scott J eds) 99–110. London. The Biochemical Society.

    Google Scholar 

  20. Brown GM, Nieduszynski IA, Morris HG, Abram BL, Huckerby TN, Block JA (1995) Glycobiology 5: 311–7.

    PubMed  CAS  Google Scholar 

  21. Farndale RW, Sayers CA, Barrett AJ (1982) Connect Tiss Res 9: 247–48

    Article  CAS  Google Scholar 

  22. Dickenson JM, Huckerby TN, Nieduszynski IA (1992) Biochem J 282: 267–71.

    PubMed  CAS  Google Scholar 

  23. Vliegenthart JFG, Dorland L, Vanhalbeek H (1983) Adv Carbohydr Chem Biochemi 41: 209–374.

    Article  CAS  Google Scholar 

  24. Huckerby TN, Nieduszynski IA, Brown GM, Cockin GH (1991) Glycoconjugate J 8: 39–44.

    Article  CAS  Google Scholar 

  25. Dickenson JM, Huckerby TN, Nieduszynski IA (1991) Biochem J 278: 779–85.

    PubMed  CAS  Google Scholar 

  26. Tai GH, Morris HG, Brown GM, Huckerby TN, Nieduszynski IA (1992) Biochem J 286: 231–34.

    PubMed  CAS  Google Scholar 

  27. Macher BA, Buehler J, Scudder P, Knapp W, Feizi T (1988) J Biol Chem 263: 10186–91.

    PubMed  CAS  Google Scholar 

  28. Brown GM, Huckerby TN, Nieduszynski IA (1996) Biochem J 319: 137–41.

    PubMed  CAS  Google Scholar 

  29. Brown GM, Huckerby TN, Morris HG, Abram BL, Nieduszynski IA (1994) Biochemistry 33: 4836–46.

    Article  PubMed  CAS  Google Scholar 

  30. Tai GH, Huckerby TN, Nieduszynski IA (1994) Carbohydr Res 255: 303–9.

    Article  PubMed  CAS  Google Scholar 

  31. Brown GM, Huckerby TN, Morris HG, Nieduszynski IA (1992) Biochem J 286: 235–41.

    PubMed  CAS  Google Scholar 

  32. Feizi T. (1991) Trends Biochem Sci 16: 84–86

    Article  PubMed  CAS  Google Scholar 

  33. Hounsell EF. (1987) Chem Soc Rev 16: 161–85.

    Article  CAS  Google Scholar 

  34. Oeben M, Keller R, Stuhlsatz HW, Greiling H (1987) Biochem J 248: 85–93.

    PubMed  CAS  Google Scholar 

  35. Stuhlstatz HW, Keller R, Becker G, Oeben M, Lennartz L, Fisher DC, Greiling H (1989) In Keratan Sulphate: Chemistry, Biology and Chemical Pathology. (Greiling H, Scott J eds) 1–11. London. The Biochemical Society.

    Google Scholar 

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Authors and Affiliations

  1. Division of Biological Sciences, Institute of Environmental and Biological Sciences, University of Lancaster, Bailrigg Lancaster, LA1 4YQ, UK

    Robert M Lauder & Ian A Nieduszynski

  2. The Polymer Centre, School of Physics and Chemistry, Lancaster University, Bailrigg Lancaster, LA1 4YQ, UK

    Thomas N Huckerby

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  1. Robert M Lauder
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  2. Thomas N Huckerby
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Lauder, R.M., Huckerby, T.N. & Nieduszynski, I.A. The structure of the keratan sulphate chains attached to fibromodulin from human articular cartilage. Glycoconj J 14, 651–660 (1997). https://doi.org/10.1023/A:1018552913584

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