Arthrose pp 37-42 | Cite as

Die Matrixrezeptoren des Knorpels

  • J. A. Mollenhauer
Conference paper
Part of the Münsteraner Streitgespräche book series (MÜNSTREIT)

Zusammenfassung

Knorpelzellen sind in einer einzigartigen Lage. Anders als praktisch in allen übrigen Geweben des Körpers haben Knorpelzellen keinen direkten Kontakt zueinander. Sie schwimmen gewissermaßen in einem Matrixmeer, das eine makroskopische statistische Zusammensetzung aus einzelnen Matrixkomponenten ausweist, die aber inhomogen verteilt vorliegen und wahrscheinlich auch nur zum Teil direkt mit der Einzelzelle in Kontakt kommen. Daher wird die Information zum Stoffwechselgleichgewicht (Homöostase) und zur adaptiven Veränderung der Matrixstruktur einigen Schlüsselfaktoren zukommen, für die die Knorpelzelle Kennungsstrukturen, d. h. Rezeptoren besitzt. In diesem Fall kann die Information prinzipiell in drei Formen verfügbar sein:

  • Erkennung spezifischer Komponenten, wie zum Beispiel Kollagen-Typ II oder Aggrekan oder Hyaluronsäure;

  • Erkennung von Mengen spezifischer Komponenten über die Zahl verfüg¬barer Rezeptoren oder die Bindungskonstanten;

  • Erkennung von Druck-oder Zugkräften durch Molekülkomplexe wie fo¬kale Kontaktstellen und Verbiegung des Zytoskeletts oder Deformation von lonenkanälen.

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Literatur

  1. 1.
    Billinghurst RC, Dahlberg L, Ionescu M, Reiner A, Bourne R, Rorabeck C, Mitchell P, Hambor J, Diekmann O, Tschesche H, Chen J, van Wart H, Poole AR (1997) Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage. J Clin Invest 99:1534–1545PubMedCrossRefGoogle Scholar
  2. 2.
    Homandberg GA, Hui F (1994) High concentrations of fibronectin fragments cause short-term catabolic effects in cartilage tissue while lower concentrations cause continuous anabolic effects. Arch. Biochem. Biophys 311:213–218Google Scholar
  3. 3.
    Ivaska J, Heino J (2000) Adhesion receptors and cell invasion: mechanisms of integrin-guided degradation of extracellular matrix. Cell Mol Life Sci 57:16–24PubMedCrossRefGoogle Scholar
  4. 4.
    Jennings LA, Cole AA, Kuettner KE, Mollenhauer JM (2003) In vitro activation of matrix metalloproteinase-3 (MMP-3) by defined collagen frgaments in human articular cartilage. Orthop Res Trans, p 28Google Scholar
  5. 5.
    Jiang H, Peterson RS, Wank W, Bartnik E, Knudson CB, Knudson W (2002) A requirement for the CD44 cytoplasmic domains for hyaluronan binding, pericellular matrix assembly, and receptor-mediated endocytosis in COS-7 cells. J Biol Chem 277:10531–10538PubMedCrossRefGoogle Scholar
  6. 6.
    Knudson CB (1993) Hyaluronan receptor-directed assembly of chondrocyte pericellular matrix. J Cell Biol 120:825–834PubMedCrossRefGoogle Scholar
  7. 7.
    Knudson W, Loeser R (2002) CD44 and integrin matrix receptors participate in cartilage homeostasis. Cell Mol Life Sci 59:36–44PubMedCrossRefGoogle Scholar
  8. 8.
    Knudson W, Aguiar DJ, Hua Q, Knudson CB (1996) CD44-anchored hyaluronanrich pericellular matrices: An ultrastructural and biochemical analysis. Exp Cell Res 228:216–228PubMedCrossRefGoogle Scholar
  9. 9.
    Knudson W, Casey B, Nishida Y, Eger W, Kuettner KE, Knudson CB (2000) Hyaluronan oligosaccharides perturb cartilage matrix homeostasis and induce chondrogenic chondrolysis. Arthritis Rheum 43:1165–1174PubMedCrossRefGoogle Scholar
  10. 10.
    Lokeshwar VB, Fregien N, Bourguignon LYW (1994) Ankyrin-binding domain of CD44(GP85) is required for the expression of hyaluronic acid-mediated adhesion function. J Cell Biol 126:1099–1109PubMedCrossRefGoogle Scholar
  11. 11.
    Lopez-Armada MJ, Gonzalez E, Gomez-Guerrero C, Egido J (1997) The 80-kD fibronectin fragment increases the production of fibronectin and tumour necrosis factor-alpha (TNF-alpha) in cultured mesangial cells. Clin Exp Immunol 107:398–403PubMedCrossRefGoogle Scholar
  12. 12.
    Mackay AR, Gomez DE, Nason AM, Thorgeirsson UP (1994) Studies on the effects of laminin, E-8 fragment of laminin and synthetic laminin peptides PA22–2 and YIGSR on matrix metalloproteinases and tissue inhibitor of metalloproteinase expression. Lab Invest 70:800–806PubMedGoogle Scholar
  13. 13.
    Maleski MP, Knudson CB (1996) Matrix accumulation and retention in embryonic cartilage and in vitro chondrogenesis. Connect Tis Res 34:75–86CrossRefGoogle Scholar
  14. 14.
    Mollenhauer J, Madsen L, Hutchins JT, Pfohl JL, Worley III JA, Thompson SA (2001) The benzodiazepine BDA 452 regulates protein synthesis and matrix degradation in chondrocytes challenged with IL-1 or collagen fragments. Orthop Res Trans 26:154Google Scholar
  15. 15.
    Paniccia R, Riccioni T, Zani BM, Zigrino P, Scotlandi K, Teti A (1995) Calcitonin down-regulates immediate cell signals induced in human osteoclast-like cells by the bone sialoprotein-IIA fragment through a postintegrin receptor mechanism. Endocrinology 136:1177–1186PubMedCrossRefGoogle Scholar
  16. 16.
    Penc SF, Blumenstock FA, Kaplan JE (1998) A 70-kDa amino-terminal fibronectin fragment supports gelatin binding to macrophages and decreases gelatinase activity. J Leukoc Biol 64:351–357PubMedGoogle Scholar
  17. 17.
    Pure E, Camp RL, Peritt D, Panettieri RA, Lazaar AL, Nayak S (1995) Defective phosporylation and hyaluronate binding of CD44 with point mutations in the cytoplasmic domain. J Exp Med 181:55–62PubMedCrossRefGoogle Scholar
  18. 18.
    Reid DL, Aydelotte MB, Mollenhauer J (2000) Integrins compared with anchorin CII: Distribution, repopulation and functional analysis in cultured bovine chondrocytes from superficial and deep layers of articular cartilage. J Orthop Res 18:364–373PubMedCrossRefGoogle Scholar
  19. 19.
    Rojas E, Pollard HP, Haigler HT, Parra C, Burns AL (1990) Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J Biol Chem 265:21207–21215PubMedGoogle Scholar
  20. 20.
    Rudzki Z, Jothy S (1997) CD44 and the adhesion of neoplastic cells. Mol Pathol 50:57–71PubMedCrossRefGoogle Scholar
  21. 21.
    Schönherr E, Broszat M, Brandan E, Bruckner P, Kresse H (1998) Decorin core protein fragment Leu155-Va1260 interacts with TGF-beta but does not compete for decorin binding to type I collagen. Arch Biochem Biophys 355:241–248PubMedCrossRefGoogle Scholar
  22. 22.
    Shepard D (2000) In vivo function of integrins: lessons from null mutations in mice. Matrix Biol 19:203–209CrossRefGoogle Scholar
  23. 23.
    Sneath RJ, Manham DC (1998) The normal structure and function of CD44 and its role in neoplasia. Mol Pathol 51:191–200PubMedCrossRefGoogle Scholar
  24. 24.
    Tavella S, Bellese G, Castagnola P, Martin I, Piccini D, Doliana R, Colombatti A, Cancedda R, Tacchetti C (1997) Regulated expression of fibronectin, laminin and related integrin receptors during the early chondrocyte differentiation. J Cell Sci 110:2261–2270PubMedGoogle Scholar
  25. 25.
    Underhill CB (1992) CD44: The hyaluronan receptor. J Cell Sci 103:293–298PubMedGoogle Scholar
  26. 26.
    Walsh KB, Cannon SD, Wuthier RE (1992) Characterization of a delayed rectifier potassium current in chicken growth plate cartilage. Am J Physiol 262:C1335–1340PubMedGoogle Scholar
  27. 27.
    Xie DL, Hui F, Meyers R, Homandberg GA (1994) Cartilage chondrolysis by fibronectin fragments is associated with release of several proteinases: stromelysin plays a major role in chondrolysis. Arch Biochem Biophys 311:205–212PubMedCrossRefGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 2004

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  • J. A. Mollenhauer

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