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. 1979 Jun 1;179(3):561–572. doi: 10.1042/bj1790561

Proteoglycans of the intervertebral disc. Homology of structure with laryngeal proteoglycans.

R L Stevens, R J Ewins, P A Revell, H Muir
PMCID: PMC1186664  PMID: 475766

Abstract

The structure of the proteoglycans from normal pig nucleus pulposus and relatively normal human annulus fibrosus and nucleus pulposus was investigated in detail and the results were compared with the current structural model of proteoglycans of hyaline cartilage. Like proteoglycans of cartilage, those of intervertebral disc contain keratan sulphate and chondroitin sulphate attached to a protein core; they are able to aggregate to hyaluronic acid; the protein core likewise has three regions, one lacking glycosaminoglycans, another rich in keratan sulphate and a third region rich in chondroitin sulphate. However, disc proteoglycans contain more keratan sulphate and protein and less chondroitin sulphate and are also considerably smaller than cartilage proteoglycans. In proteoglycans of human discs, these differences appeared to be due principally to a shorter region of the core protein bearing the chondroitin sulphate chains, whereas in proteoglycans of pig discs their smaller size and relatively low uronic acid content were due to shorter chondroitin sulphate chains. There were subtle differences between proteoglycans from the nucleus and annulus of human discs. In the latter a higher proportion of proteoglycans was capable of binding to hyaluronate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ANDERSON B., HOFFMAN P., MEYER K. THE O-SERINE LINKAGE IN PEPTIDES OF CHONDROITIN 4- OR 6-SULFATE. J Biol Chem. 1965 Jan;240:156–167. [PubMed] [Google Scholar]
  2. Adams P., Muir H. Qualitative changes with age of proteoglycans of human lumbar discs. Ann Rheum Dis. 1976 Aug;35(4):289–296. doi: 10.1136/ard.35.4.289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BITTER T., MUIR H. M. A modified uronic acid carbazole reaction. Anal Biochem. 1962 Oct;4:330–334. doi: 10.1016/0003-2697(62)90095-7. [DOI] [PubMed] [Google Scholar]
  4. BOAS N. F. Method for the determination of hexosamines in tissues. J Biol Chem. 1953 Oct;204(2):553–563. [PubMed] [Google Scholar]
  5. Baker J. R., Rodén L., Stoolmiller A. C. Biosynthesis of chondroitin sulfate proteoglycan. Xylosyl transfer to Smith-degraded cartilage proteoglycan and other exogenous acceptors. J Biol Chem. 1972 Jun 25;247(12):3838–3847. [PubMed] [Google Scholar]
  6. Clamp J. R., Dawson G., Hough L. The simultaneous estimation of 6-deoxy-L-galactose (L-fucose), D-mannose, D-galactose, 2-acetamido-2-deoxy-D-glucose (N-acetyl-D-glucosamine) and N-acetylneuraminic acid (sialic acid) in glycopeptides and glycoproteins. Biochim Biophys Acta. 1967 Nov 28;148(2):342–349. doi: 10.1016/0304-4165(67)90129-8. [DOI] [PubMed] [Google Scholar]
  7. Elson L. A., Morgan W. T. A colorimetric method for the determination of glucosamine and chondrosamine. Biochem J. 1933;27(6):1824–1828. doi: 10.1042/bj0271824. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Emes J. H., Pearce R. H. The proteoglycans of the human intervertebral disc. Biochem J. 1975 Mar;145(3):549–556. doi: 10.1042/bj1450549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Eyre D. R., Muir H. The distribution of different molecular species of collagen in fibrous, elastic and hyaline cartilages of the pig. Biochem J. 1975 Dec;151(3):595–602. doi: 10.1042/bj1510595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gower W. E., Pedrini V. Age-related variations in proteinpolysaccharides from human nucleus pulposus, annulus fibrosus, and costal cartilage. J Bone Joint Surg Am. 1969 Sep;51(6):1154–1162. [PubMed] [Google Scholar]
  11. Hardingham T. E., Adams P. A method for the determination of hyaluronate in the presence of other glycosaminoglycans and its application to human intervertebral disc. Biochem J. 1976 Oct 1;159(1):143–147. doi: 10.1042/bj1590143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hardingham T. E., Ewins R. J., Muir H. Cartilage proteoglycans. Structure and heterogeneity of the protein core and the effects of specific protein modifications on the binding to hyaluronate. Biochem J. 1976 Jul 1;157(1):127–143. doi: 10.1042/bj1570127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hardingham T. E., Muir H. Hyaluronic acid in cartilage and proteoglycan aggregation. Biochem J. 1974 Jun;139(3):565–581. doi: 10.1042/bj1390565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hascall V. C., Sajdera S. W. Physical properties and polydispersity of proteoglycan from bovine nasal cartilage. J Biol Chem. 1970 Oct 10;245(19):4920–4930. [PubMed] [Google Scholar]
  15. Hascall V. C., Sajdera S. W. Proteinpolysaccharide complex from bovine nasal cartilage. The function of glycoprotein in the formation of aggregates. J Biol Chem. 1969 May 10;244(9):2384–2396. [PubMed] [Google Scholar]
  16. Heinegård D., Axelsson I. Distribution of keratan sulfate in cartilage proteoglycans. J Biol Chem. 1977 Mar 25;252(6):1971–1979. [PubMed] [Google Scholar]
  17. Heinegård D., Hascall V. C. Aggregation of cartilage proteoglycans. 3. Characteristics of the proteins isolated from trypsin digests of aggregates. J Biol Chem. 1974 Jul 10;249(13):4250–4256. [PubMed] [Google Scholar]
  18. Heinegård D. Polydispersity of cartilage proteoglycans. Structural variations with size and buoyant density of the molecules. J Biol Chem. 1977 Mar 25;252(6):1980–1989. [PubMed] [Google Scholar]
  19. Hopwood J. J., Robinson H. C. The alkali-labile linkage between keratan sulphate and protein. Biochem J. 1974 Jul;141(1):57–69. doi: 10.1042/bj1410057. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Hopwood J. J., Robinson H. C. The molecular-weight distribution of glycosaminoglycans. Biochem J. 1973 Dec;135(4):631–637. doi: 10.1042/bj1350631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Hopwood J. J., Robinson H. C. The structure and composition of cartilage keratan sulphate. Biochem J. 1974 Aug;141(2):517–526. doi: 10.1042/bj1410517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  23. Pearce R. H., Grimmer B. J. The chemical constitution of the proteoglycan of human intervertebral disc. Biochem J. 1976 Sep 1;157(3):753–763. doi: 10.1042/bj1570753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Robinson H. C., Hopwood J. J. The alkaline cleavage and borohydride reduction of cartilage proteoglycan. Biochem J. 1973 Jul;133(3):457–470. doi: 10.1042/bj1330457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Rosenberg L. C., Pal S., Beale R. J. Proteoglycans from bovine proximal humeral articular cartilage. J Biol Chem. 1973 May 25;248(10):3681–3690. [PubMed] [Google Scholar]
  26. Rosenberg L., Wolfenstein-Todel C., Margolis R., Pal S., Strider W. Proteoglycans from bovine proximal humeral articular cartilage. Structural basis for the polydispersity of proteoglycan subunit. J Biol Chem. 1976 Oct 25;251(20):6439–6444. [PubMed] [Google Scholar]
  27. Saito H., Yamagata T., Suzuki S. Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates. J Biol Chem. 1968 Apr 10;243(7):1536–1542. [PubMed] [Google Scholar]
  28. Sajdera S. W., Hascall V. C. Proteinpolysaccharide complex from bovine nasal cartilage. A comparison of low and high shear extraction procedures. J Biol Chem. 1969 Jan 10;244(1):77–87. [PubMed] [Google Scholar]
  29. Thyberg J., Lohmander S., Heinegård D. Proteoglycans of hyaline cartilage: Electron-microscopic studies on isolated molecules. Biochem J. 1975 Oct;151(1):157–166. doi: 10.1042/bj1510157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Tsiganos C. P., Muir H. Studies on protein-polysaccharides from pig laryngeal cartilage. Heterogeneity, fractionation and characterization. Biochem J. 1969 Aug;113(5):885–894. doi: 10.1042/bj1130885. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. WOESSNER J. F., Jr The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acid. Arch Biochem Biophys. 1961 May;93:440–447. doi: 10.1016/0003-9861(61)90291-0. [DOI] [PubMed] [Google Scholar]
  32. Wasteson A. A method for the determination of molecular weight dispersion in chondroitin sulphate on a microgram level. Biochim Biophys Acta. 1969 Feb 18;177(1):152–154. doi: 10.1016/0304-4165(69)90076-2. [DOI] [PubMed] [Google Scholar]

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