Skip to main content
SpringerLink
Log in

Localization of carboxy-terminal type II procollagen peptide (pCOL-II-C) in diseased cartilage

  • Original Articles
  • Published:
Journal of Orthopaedic Science

Abstract

A well characterized rabbit polyclonal antibody against human carboxy-terminal type II procollagen peptide (pCOL-II-C) was used to study the immunolocalization of pCOL-II-C in articular cartilage obtained from patients with osteoarthritis (OA), rheumatoid arthritis (RA), and control non-diseased joints. In moderately degenerative OA cartilage, immunoreactive chondrocytes were observed in all layers, particularly along the margins of fibrillation and fissures, in chondrocyte clusters and in osteochondrophytes. The grade of immunostaining in OA correlated directly with Mankin's histological-histochemical scores of 0–7, but there was an inverse correlation between grade of immunostaining and Mankin's scores of 8–14. The grade of immunostaining was significantly higher in OA than in RA and normal control cartilage. Since type II collagen is a unique component of articular cartilage, localization of pCOL-II-C could reflect the increased synthesis of type II collagen by chondrocytes in diseased cartilage.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Aigner T, Stöß H, Weseloh G, et al. Activation of collagen type II expression in osteoarthritic and rheumatoid cartilage. Virchows Arch B Cell Pathol 1992;62:337–45.

    CAS  Google Scholar 

  2. Arnett FC, Edworthy SM, Block DA, et al. The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis. Arthritis Rheum 1988;31:315–24.

    PubMed  CAS  Google Scholar 

  3. Brennan FM, Maini RN, Feldmann M. TNF α—a pivotal role in rheumatoid arthritis? Br J Rheum 1992;31:293–8.

    CAS  Google Scholar 

  4. Buckwalter JA, Mow VC, Ratcliffe A. Restoration of injured or degenerated articular cartilage. J Am Acad Orthop Surg 1994;2:192–201.

    PubMed  Google Scholar 

  5. Cheung HS, Lynch KL, Johnson RP, et al. In vitro synthesis of tissue-specific type II collagen by healing cartilage. Arthritis Rheum 1980;23:211–9.

    PubMed  CAS  Google Scholar 

  6. Choi HU, Tang L-H, Johnson TL, et al. Isolation and characterization of a 35000 molecular weight subunit fetal cartilage matrix protein. J Biol Chem 1983;258:655–61.

    PubMed  CAS  Google Scholar 

  7. Dean DD, Martel-Pelletier J, Pelletier J-P, et al. Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage. J Clin Invest 1989;84:678–85.

    PubMed  CAS  Google Scholar 

  8. Goldwasser M, Astley T, van der Rest M, et al. Analysis of the type of collagen present in osteoarthritic human cartilage. Clin Orthop 1982;167:296–302.

    PubMed  CAS  Google Scholar 

  9. Kowanko IC, Ferrante A. Granulocyte-macrophage colony-stimulating factor augments neutrophil-mediated cartilage degradation and neutrophil adherence. Arthritis Rheum 1991;34:1452–60.

    Article  PubMed  CAS  Google Scholar 

  10. Lotz M, Terkeltaub R, Villiger PM. Cartilage and joint inflammation. Regulation of IL-8 expression by human articular chondrocytes. J Immunol 1992;148:466–73.

    PubMed  CAS  Google Scholar 

  11. Mankin HK, Dorfman H, Lippiello L, et al. Biochemical and metabolic abnormalities in articular cartilage from osteoarthritic human hips. J Bone Joint Surg Am 1971;53:523–37.

    PubMed  CAS  Google Scholar 

  12. Mankin HJ, Brandt KD. Biochemistry and metabolism of articular cartilage in osteoarthritis. In: Moskowitz RW, Howell DS, Goldberg VM, Mankin HJ, editors. Osteoarthritis: Diagnosis and medical/surgical management. Philadelphia: WBSaunders, 1992:109–54.

    Google Scholar 

  13. Mayne R. Cartilage collagens. What is their function, and are they invoked in articular disease? Arthritis Rheum 1989;32:241–6.

    PubMed  CAS  Google Scholar 

  14. Nelson F, Reiner A, Ionescu M, et al. The content of the C-propeptide of type II collagen in articular cartilage is an index of synthesis of this molecule which is increased in osteoarthritis. Proceedings of the 40th Annual Meeting, Orthopaedic Research Society, Feb 21–24 1994, New Orleans, 216. Chicago: Rider Dickerson.

    Google Scholar 

  15. Niyibizi C, Wu J-J, Eyre DR. The carboxypropeptide trimer of type II collagen is a prominent component of immature cartilages and intervertebral-disc tissue. Biochim Biophys Acta 1987;916:493–9.

    PubMed  CAS  Google Scholar 

  16. Okada Y, Takeuchi N, Tomita K, et al. Immunolocalisation of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): Correlation with rheumatoid arthritis. Ann Rheum Dis 1989;48:645–53.

    Article  PubMed  CAS  Google Scholar 

  17. Okada Y, Shinmei M, Tanaka O, et al. Localization of matrix metalloproteinase 3 (stromelysin) in osteoarthritic cartilage and synovium. Lab Invest 1992;66:680–90.

    PubMed  CAS  Google Scholar 

  18. Pelletier JP, Martel-Pelletier J, Malemud CJ. Canine osteoarthritis: Effects of endogenous neutral metalloproteo-glycanases on articular cartilage proteoglycans. J Orthop Res 1988;6:379–88.

    Article  PubMed  CAS  Google Scholar 

  19. Peltonen L, Halila R, Ryhanen L. Enzymes converting procollagens to collagens. J Cell Biochem 1985;28:15–21.

    Article  PubMed  CAS  Google Scholar 

  20. Poole AR, Pidoux I, Reiner A, et al. Association of an extracellular protein (chondrocalcin) with the calcification of cartilage in endochondral bone formation. J Cell Biol 1984;98:54–65.

    Article  PubMed  CAS  Google Scholar 

  21. van der Rest M, Rosenberg LC, Olsen BR, et al. Chondrocalcin is identical with the C-propeptide, of type II procollagen. Biochem J 1986;237:923–5.

    PubMed  Google Scholar 

  22. Ronziére M-C, Richard-Blum S, Tiollier J, et al. Comparative analysis of collagens solubilized from human foetal, and normal osteoarthritic adult articular cartilage, with emphasis on type VI collagen. Biochim Biophys Acta 1990;1038:222–30.

    PubMed  Google Scholar 

  23. Ryu J, Treadwell BV, Mankin HJ. Biochemical and metabolic abnormalities in normal and osteoarthritic human articular cartilage. Arthritis Rheum 1984;27:49–57.

    PubMed  CAS  Google Scholar 

  24. Säämänen A-M, Tammi M, Kiviranta I, et al. Levels of chondroitin-6-sulfate and nonaggregating proteoglycans at articular cartilage contact sites in the knees of young dogs subjected to moderate running exercise. Arthritis Rheum 1989;32:1282–92.

    PubMed  Google Scholar 

  25. Shinmei M, Masuda K, Kikuchi T, et al. Interleukin 1, tumor necrosis factor, and interleukin 6 as mediators of cartilage destruction. Semin Arthritis Rheum 1989;18(Suppl):27–32.

    Article  PubMed  CAS  Google Scholar 

  26. Shinmei M, Inamori Y, Yoshihara Y, et al. The potential of cartilage markers in joint fluid for drug evaluation. In: Kuettner KE, Schleyerbach R, Peyron JG, Hascall VC, editors. Articular cartilage and osteoarthritis. New York: Raven 1992:597–609.

    Google Scholar 

  27. Shinmei M, Ito K, Matsuyama S, et al. Joint fluid carboxyterminal type II procollagen peptide as a marker of cartilage collagen biosynthesis. Osteoarthritis Cartilage 1993;1:121–8.

    Article  PubMed  CAS  Google Scholar 

  28. Tanaka O, Shinmei M, Kikuchi, T, et al. Immunohistochemical study of type II collagen C-propeptide (chondrocalcin) in diseased articular cartilage (in Japanese). J Jpn Orthop Assoc 1989;63(Suppl):S1198.

    Google Scholar 

  29. Uitto J, Allan RE, Polak KL. Conversion of type II procollagen to collagen. Eur J Biochem 1979;99:97–103.

    Article  PubMed  CAS  Google Scholar 

  30. van Beuningen HM, Arntz OJ, van den Berg WB. In vivo effects of interleukin-1 on articular cartilage. Arthritis Rheum 1991;34:606–15.

    PubMed  Google Scholar 

  31. Yaron I, Meyer FA, Dayer J-M, et al. Some recombinant human cytokines stimulate glycosaminoglycan synthesis in human synovial fibroblast cultures and inhibit in human articular cartilage cultures. Arthritis Rheum 1989;32:173–80.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Orthopaedic Surgery, National Defense Medical College, 3-2 Namiki, Tokorozawa, 359, Saitama, Japan

    Hideto Nakajima, Masayuki Shinmei & Toshiyuki Kikuchi

  2. Central Research Laboratory, National Defense Medical College, 3-2 Namiki, Tokorozawa, 359, Saitama, Japan

    Shigeo Matsuyama

  3. Pharmaceutical Products Research Laboratories, Teijin Iwakuni Research Center, 2-1 Hinode-cho, Iwakuni, 740, Yamaguchi, Japan

    Kazuhiko Ito & Hitomi Honda

Authors
  1. Hideto Nakajima
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Masayuki Shinmei
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Kazuhiko Ito
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Shigeo Matsuyama
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Toshiyuki Kikuchi
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Hitomi Honda
    View author publications

    You can also search for this author in PubMed Google Scholar

About this article

Cite this article

Nakajima, H., Shinmei, M., Ito, K. et al. Localization of carboxy-terminal type II procollagen peptide (pCOL-II-C) in diseased cartilage. J Orthop Sci 2, 229–238 (1997). https://doi.org/10.1007/BF02489043

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02489043

Key words

Search

Navigation