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Chemical composition of normal and osteoarthrotic cancellous bone of the femoral head

Studies of EDTA extracts and collagenase digests

  • Clinical and Experimental Forum
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Summary

Using EDTA extraction and collagenase digestion, cancellous bone from the femoral heads of ten normal and eight osteoarthrotic individuals was analyzed for its content of collagen, sialoprotein, proteoglycan, and carbohydrate. The EDTA extractability of the matrix proteins of the osteoarthrotic bone was significantly increased (P< 0.001), as was the soluble collagenase-resistant fraction (SCRF). EDTA residues, bone matrix size, the collagenase-resistant fraction (CRF), and the insoluble collagenase-resistant fraction (ICRF) of the osteoarthrotic cases were not different from those of the controls. The amounts of carbohydrate and proteoglycans were considerably elevated in the bone matrix of the osteoarthrotic bone (P<0.01 and P<0.001, respectively). In the EDTA extracts, sialoprotein and proteoglycan contents were found in significant higher amounts (P<0.05 and P<0.01, respectively) in the osteoarthrotic cases. In the SCRF, the hexose and sialic acid contents were higher in the osteoarthrotic bone (P<0.01), while in the ICRF all the analyses were significantly increased in the osteoarthrotic bone (P<0.001). The ratios of collagen to non-collagenaus components were lower in the osteoarthrotic than in normal bones. The quantitative and qualitative variations in cancellous bone proteins from the femoral head in osteoarthrosis found in this study suggest that alterations in subchondral bone play a role in the pathophysiology of cartilage degeneration in osteoarthrosis.

Zusammenfassung

Mittels EDTA Extraktion und Kollagenase-Fermentierung wurde der Gehalt an Kollagen, Sialoprotein, Proteoglycan und Karbohydrat im Knochenmaterial der Hüftköpfe von 10 normalen und 8 osteoarthrotischen Personen analysiert. Die EDTA Extrahierbarkeit der Matrixproteine des osteoarthrotischen Knochens war signifikant gestiegen (P>0,001) ebenso wie der lösliche Kollagenase resistente Teil (LKRT). EDTA Reste, die Größe der Knochenmatrix, der Kollagenase resistente Teil (KRT) and der unlösliche Kollagenase resistente Teil (UKRT) der osteoarthrotischen Hüftköpfe unterschieden sich nicht von den Kontrollfällen. Die Mengen von Karbohydrat und Proteoglycan waren deutlich erhöht in der Knochenmatrix der osteoarthrotischen Knochen (P<0,01 bzw. P<0,001). In den EDTA Extrakten war der Gehalt an Sialoprotein und Proteoglycan bei den osteoarthrotischen Hüftköpfen deutlich höher (P< 0,05 bzw. P< 0,01). Im LKRT war der Gehalt an Hexose and sialischer Säure höher im osteoarthrotischen Knochen (P<0,01), während im UKRT alle Analysen deutlich h6her waren im osteoarthrotischen Knochen (P<0,001). Das Verhältnis von Kollagen zum kollagefreien Anteil war niedriger im osteoarthrotischen als im normalen Knochen. Quantitative and qualitative Veränderungen in Knochenproteinen des osteoarthrotischen Hüftkopfes, wie sie die vorliegende Studie ausweist, lassen vermuten, daß Veranderungen im subchondralen Knochen eine wichtige Rolle spielen in der Pathophysiologie der Degeneration des Gelenkknorpels bei Osteoarthrosis.

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References

  1. Aminoff D (1961) Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysate of sialomucoids. Biochem J 81:384–392

    Google Scholar 

  2. Bitter J, Muir HM (1962) A modified uronic acid carbazole reaction. Anal Biochem 4:330–334

    Google Scholar 

  3. Bullet AJ (1968) Stimulation of protein-chondroitin sulfate synthesis by normal and osteoarthritic articular cartilage. Arthritis Rheum 11:663–673

    Google Scholar 

  4. Burton-Wurster N, Hui-Chou CS, Greison HA, Lust G (1982) Reduced deposition of collagen in the degenerated articular cartilage of dogs with degenerative joint disease. Biochim Biophys Acta 718:74–84

    Google Scholar 

  5. Carter DR, Spengler DM (1978) Mechanical properties and composition of cortical bone. Clin Orthop 135:192–217

    Google Scholar 

  6. Collins DH, Mc Elligott TF (1960) Sulphate (35SO4) uptake by chondrocytes in relation to histological changes in osteoarthritic human articular cartilage. Ann Rheum Dis 19:318–330

    Google Scholar 

  7. Dequeker J, Burssens A, Creytens G, Bouillon R (1975) Ageing of bone: its relation to osteoporosis and osteoarthrosis in postmenopausal women. Front Horm Res 3:116–130

    Google Scholar 

  8. Gay S, Miller EJ (1978) Collagen in the physiology and pathology of connective tissue. Fischer, Stuttgart New York

    Google Scholar 

  9. Ghosh P, Taylor TKF, Braund KG, Larsen LH (1976) The collagenous and noncollagenous proteins of the canine intervertebral disc and their variation with age, spinal level and breed. Gerontology 22:124–134

    Google Scholar 

  10. Glimcher MJ (1981) On the form and function of bone: from molecules to organs. Wolfl's law revisited. In: Veis A (ed) The chemistry and biology of mineralized connective tissues. Elsevier North-Holland, Amsterdam, pp 617–675

    Google Scholar 

  11. Hancock DA, Asiedu-Offei S, Atkinson PJ, Reed GW, Wright K (1978) Femoral bone mass in patients with rheumatoid arthritis and osteoarthritis. Rheumatol Rehabil 17:65–71

    Google Scholar 

  12. Herring GM (1968) Studies on the protein-bound chondroitin sulphate of bovine cortical bone. Biochem J 107:41–50

    Google Scholar 

  13. Herring GM, Ashton BA, Chipperfield AR (1974) The isolation of soluble proteins, glycoproteins, and proteoglycans from bone. Prep Biochem 4:179–200

    Google Scholar 

  14. Herring GM (1976) A comparison of bone matrix and tendon with particular reference to glycoprotein content. Biochem J 159:749–755

    Google Scholar 

  15. Herring GM (1977) Methods for the study of the glycoprotein and proteoglycans of bone using bacterial collagenase. Calcif Tissue Res 24:22–36

    Google Scholar 

  16. Inerot S, Heinegard D, Audell L, Olsson SE (1978) Articular cartilage proteoglycans in aging and osteoarthritis. Biochem J 1:169–156

    Google Scholar 

  17. Kivirikko KI, Laitinen O, Prockop DJ (1967) Modifications of a specific assay for hydroxyproline in urine. Anal Biochem 19:249–255

    Google Scholar 

  18. Lippiello L, Hall D, Mankin HJ (1977) Collagen synthesis in normal and osteoarthritic human cartilage. J Clin Invest 59:593–600

    Google Scholar 

  19. Mc Devitt CA, Muir H (1976) Biochemical changes in the cartilage of the knee in experimental and natural osteoarthritis in the dog. J Bone Joint Surg [Br] 58:94–101

    Google Scholar 

  20. Mc Devitt C, Gilbertson E, Muir H (1977) An experimental model of osteoarthritis; early morphological and biochemical changes. J Bone Joint Surg [Br] 59:24–35

    Google Scholar 

  21. Mankin HJ, Lippiello L (1971) The glycosaminoglycans of normal and arthritic cartilage. J Clin Invest 50:1712–1719

    Google Scholar 

  22. Mankin HJ, Johnson ME, Lippiello L (1981) Biochemical and metabolic abnormalities in articular cartilage from osteoarthritic human hips. III. Distribution and metabolism of amino sugar-containing macromolecules. J Bone Joint Surg [Am] 63:131–139

    Google Scholar 

  23. Maroudas A, Venn M (1977) Chemical composition and swelling of normal and osteoarthrotic femoral head cartilage. II. Swelling. Ann Rheum Dis 36:399–406

    Google Scholar 

  24. Mbuyi JM, Dequeker J (1982) Biochemical analyses of EDTA extracts and collagenase digests from bone and skin of Wistar rats. Lab Anim 16:256–264

    Google Scholar 

  25. Mbuyi JM, Dequeker J (in press) Biochemical anatomy of human bone. A comparative study of compact and spongy bones in femur, rib and iliac crest

  26. Mitrovic D, Gruson M, Demignon J, Mercier P, Aprile F, De Seze S (1981) Metabolism of human femoral head cartilage in osteoarthrosis and subcapital fracture. Ann Rheum Dis 40:18–26

    Google Scholar 

  27. Nimni ME, Deshmukh K (1973) Differences in collagen metabolism between normal and osteoarthritic human articular cartilage. Science 181:751–752

    Google Scholar 

  28. Pugh JW, Radin EL, Rose RM (1974) Quantitative studies of human subchondral cancellous bone, its relationship to the state of its overlying cartilage. J Bone Joint Surg [Am] 56:313

    Google Scholar 

  29. Radin EL, Paul LL (1970) Does cartilage compliance reduce skeletal impact loads? Arthritis Rheum 13:139–143

    Google Scholar 

  30. Radin EL, Paul IL, Lowy M (1970) A comparison of the dynamic force-transmitting properties of subchondral bone and articular cartilage. J Bone Joint Surg [Am] 52:444–448

    Google Scholar 

  31. Roh YS, Dequeker J, Mulier JC (1974) Bone mass in osteoarthrosis, measured in vivo by photon absorption. J Bone Joint Surg [Am] 56:587–591

    Google Scholar 

  32. Sokoloff L (1979) Pathology and pathogenesis of osteoarthritis. In: McCarthy DJ (ed) Arthritis and allied conditions. Lea and Febiger, Philadelphia, pp 1135–1153

    Google Scholar 

  33. Saville PD (1967) A quantitative approach to simple diagnosis of osteoporosis: its application to the osteoporosis of rheumatoid arthritis. Arthritis Rheum 10:416

    Google Scholar 

  34. Schwartz ER, Leveille CR, Stevens JW, Won HOH (1981) Proteoglycan structure and metabolism in normal and osteoarthritic cartilage of guinea pigs. Arthritis Rheum 24:1528–1539

    Google Scholar 

  35. Sweet MBE, Thonar EJMA, Immelman AR, Solomon L (1977) Biochemical changes in progressive osteoarthrosis. Ann Rheum Dis 36:387–398

    Google Scholar 

  36. Weber K, Osborn M (1969) The reliability of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis. J Biol Chem 244:4406–4412

    Google Scholar 

  37. Yemm E, Willis AJ (1954) The estimation of carbohydrates in plant extracts by anthrone. Biochem J 57:508–514

    Google Scholar 

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Mbuyi-Muamba, J.M., Dequeker, J. Chemical composition of normal and osteoarthrotic cancellous bone of the femoral head. Arch. Orth. Traum. Surg. 102, 267–272 (1984). https://doi.org/10.1007/BF00436142

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  • DOI: https://doi.org/10.1007/BF00436142

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