Skip to main content
Log in

Lectin-binding in normal and fibrillated articular cartilage of human patellae

  • Published:
Virchows Archiv A Aims and scope Submit manuscript

Summary

Fluorescein-isothiocyanate (FITC) labeled lectins were used to study the distribution of specific binding-sites in histological sections of normal and fibrillated articular cartilage of human patellae.

It has been shown that normal articular cartilage reveals lectin binding-sites for Concanavalin A (Con A) and wheat germ agglutinin (WGA), but not for soybean agglutinin (SBA), peanut agglutinin (PNA) and Ulex europaeus agglutinin (UEA).

In fibrillated cartilage the distribution pattern of Con A and WGA is completely changed. SBA, PNA and UEA show a distinct staining pattern in particular in the fibrillated areas of degenerated cartilage. Lectin-staining of the extracellular matrix and the chondrocytes in both normal and fibrillated cartilage did not show any correlation with material that was either PAS- or Alcian blue-positive. In comparison with the conventional PAS- and Alcian blue reaction lectin-staining proved to be superior.

Visualization of intra- and extracellular glycoconjugate-changes in normal and fibrillated cartilage in areas with no PAS and/or Alcian blue staining indicates that all layers of the cartilage are involved in the pathological process.

It is evident that lectins can demonstrate minute differences between normal and arthrotic cartilage and we therefore conclude that lectins are sensitive and specific tools for the study of degenerative joint diseases.

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

Access this article

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

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Brocklehurst R, Bayliss MT, Maroudas A, Coysh HL, Obst D, Freeman MAR, Revell PA, Ali SY (1984) The composition of normal and osteoarthritic articular cartilage from human knee joints. J Bone Jt Surg 66A:95–106

    Google Scholar 

  • Collins DH (1949) The pathology of articular and spinal diseases. Chap 5, 74–115, Arnold, London

    Google Scholar 

  • Corfield AP, Schauer R (1979) Current aspects of glycoconjugate biosynthesis. Biol Cell 36:213–219

    Google Scholar 

  • Dustmann HO, Puhl W, Krempien B (1974) Das Phänomen der Cluster im Arthroseknorpel. Arch Orthop Unfall-Chir 79:321–333

    Google Scholar 

  • Farnum CE, Wilsman NJ (1984) Lectin-binding histochemistry of non-decalcified growth plate cartilage: A post-embedment method for light microscopy of epon-embedded tissue. J Histochem Cytochem 32:593–607

    Google Scholar 

  • Ficat C, Maroudas A (1975) Cartilage of the patella. Topographical variation of glycosaminoglycan content in normal and fibrillated tissues. Ann Rheum Disc 34:515–519

    Google Scholar 

  • Goldstein IJ, Hayes CE (1978) The lectins: Carbohydrate binding proteins of plants and animals. Adv Carbohydr Chem Biochem 35:127–339

    Google Scholar 

  • Goodfellow J, Hungerford DS, Zindle M (1976) Patello-femoral joint mechanics and pathology. I. Functional anatomy of the patello-femoral joint. J Bone Jt Surg 58B:287–290

    Google Scholar 

  • Hascall VC, Hascall KG (1983) Proteoglycans. In: Hay ED (ed) Cell biology of the extracellular matrix. Plenum Press, New York and London

    Google Scholar 

  • Ippolito E, La Velle S, Pedrini V (1981) The effect of various decalcification agents on cartilage proteoglycans. Stain Technol 56:367–372

    Google Scholar 

  • Maquet P (1976) Biomechanics of the knee. Springer, Berlin, Heidelberg, New York

    Google Scholar 

  • Pearse AGE (1968) Histochemistry, theoretical and applied. Vol 1, Churchill, London

  • Ratcliffe A, Fryer PR, Hardingham TE (1984) The distribution of aggregating proteoglycans in articular cartilage: Comparison of quantitative immunoelectron microscopy with radioimmunoassay and biochemical analysis. J Histochem Cytochem 32:193–201

    Google Scholar 

  • Schünke M, Schumacher U, Tillmann B, Welsch U (1984) Lektinbindungsstellen in Stützgeweben. Verh Anat Ges, Anat Anz (in press)

  • Söderström KO, Malmi R, Karjalainen K (1984) Binding of fluorescein isothiocyanate conjugated lectins to rat spermatogenic cells in tissue sections. Enhancement of lectin fluorescence obtained by fixation in Bouin's fluid. Histochemistry 80:575–579

    Google Scholar 

  • Spicer SS, Schulte GN, Thomopoulus RT, Parmley RT, Takagi M (1983) Cytochemistry of complex carbohydrates by light and electron microscopy. Available methods and their application. In: Connective tissue diseases, Wagner BM, Fleischmeier R, Kaufman N (eds). Williams and Wilkins, Baltimore

    Google Scholar 

  • Stockwell RA (1970) Changes in the acid glycosaminoglycan content of the matrix of ageing human articular cartilage. Ann Rheum Disc 29:509–515

    Google Scholar 

  • Stoddart RW, Kiernan JA (1973) Histochemical detection of the α-d-arabinopyranoside configuration using fluorescent-labelled Concanavalin A. Histochemistry 33:87–94

    Google Scholar 

  • Toda N, Doi A, Jimbo A, Matsumoto I, Seno N (1981) Interaction of sulfated glycosaminoglycans with lectins. J Biol Chem 256:5545–5349

    Google Scholar 

  • Van der Valk MA, Hageman PH (1982) Distribution of lectin receptors in neonatal, embryonic and neoplastic mouse tissue. In: Lectins - Biology, Biochemistry, Clinical Biochemistry, vol 3, Bøg-Hanson TC, Spengler GA (eds) Walter de Gruyter, Berlin, New York

    Google Scholar 

  • Watanabe M, Muramatsu T, Shirane H, Ugai K (1981) Discrete distribution of binding sites for Dolichos biflorus agglutinin (DBA) and for Peanut agglutinin (PNA) in mouse organ tissues. J Histochem Cytochem 29:779–790

    Google Scholar 

  • Wiberg G (1941) Roentgenographic and anatomic studies on the femoropatellar joint. With special reference to the chondromalacia patellae. Acta Orthp Scand 12:319–410

    Google Scholar 

  • Yamada K (1978) Concanavalin A - peroxidase - diaminobenzidin - periodic acid-m-aminophenol- fast black K salt: A method for the dual staining of neutral complex carbohydrates. Histochem J 10:573–590

    Google Scholar 

  • Yamada K, Shimizu S (1977) The histochemistry of galactose residues of complex carbohydrates as studied by peroxidase-labelled Ricinus communis agglutinin. Histochemistry 53:143–156

    Google Scholar 

  • Zimmermann B, Thies M (1984) Alterations of lectin binding during chondrogenesis of mouse limb buds. Histochemistry 81:353–361

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Schünke, M., Schumacher, U. & Tillmann, B. Lectin-binding in normal and fibrillated articular cartilage of human patellae. Vichows Archiv A Pathol Anat 407, 221–231 (1985). https://doi.org/10.1007/BF00737079

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00737079

Key words

Navigation