Abstract
The organic phase (or crystallite ghost) associated with each crystallite, together with the background material associated with each crystallite cluster, was demonstrated in calcified cartilage using basic chromium sulphate as a combined fixative, stain, and demineralizing agent. Subsequent treatment of the tissue with papain, or with hyaluronidase, suggests that the crystallite ghosts represented a protein-polysaccharide complex and that the background material was principally protein together with some acid polysaccharide. The relationship between inorganic and organic phases is discussed.
Résumé
La phase organique (ou fantôme des cristaux) associéc à chaque cristal, ainsi que la substance de base associée à chaque cristal, ainsi que la substance de base associée à chaque amas cristallin, sont mises en évidence au niveau du cartilage calcifié en utilisant le sulfate de chrome basique comme agent de fixation, de coloration et de déminéralisation. Le traitement ultérieur du tissu, à l'aide de papaïne ou d'hyaluronidase, indique que les fantômes cristallins constitutent un complexe protéino-polysaccharidique et que la substance de base est formée par une protéine associée à un polysaccharide acide. Les rapports entre phases inorganique et organique sont discutés.
Zusammenfassung
Die organische Phase (oder Kristallit-Schatten), die zu jedem Kristallit gehört, sowie das Hintergrundmaterial, das zu jeder Kristallitgruppe gehört, wurden in calcifiziertem Knorpel sichtbar gemacht. Zu diesem Zweck wurde basisches Chromsulfat als ein kombiniertes Fixierungs-, Färbe- und Demineralisierungsmittel verwendet. Nachfolgende Behandlung des Gewebes mit Papain oder Hyaluronidase läßt vermuten, daß die Kristallitschatten einen Proteinpolysaccharidkomplex darstellen und daß das Hintergrundmaterial hauptsächlich aus Protein mit einigen sauren Polysacchariden besteht. Die Beziehung zwischen anorganischen und organischen Phasen wird diskutiert.
Similar content being viewed by others
References
Anderson, D. R.: The ultrastructure of elastic and hyaline cartilage of the rat. Amer. J. Anat.114, 403–433 (1964).
Appleton, J.: Ultrastructural observations on early cartilage calcification. The use of chromium sulphate in decalcification. Calcif. Tiss. Res.5, 270–276 (1970).
Appleton, J.: The fine structure of the condylar cartilage of the rat mandible. Ph. D. Thesis, University of London (1969).
—, Blackwood, H. J. J.: Ultrastructural observations on early mineralization in cartilage. J. Bone Jt Surg. B51, 385 (1969) (Abstract).
Baker, J. R.: Cytological technique. The principles underlying routine methods. London: Methuen & Co. Ltd. 1963.
Bonucci, E.: Fine structure of early cartilage calcification. J. Ultrastruct. Res.20, 35–50 (1967).
—: Further investigation on the organic/inorganic relationships in calcifying cartilage. Calcif. Tiss. Res.3, 38–54 (1969).
Cameron, D. A.: The fine structure of bone and calcified cartilage. Clin. Orthop.26, 199–228 (1963).
Cessi, C., Bernhardi, G.: The kinetics of enzymatic degradation and the structure of protein-polysaccharide complexes of cartilage. In: Structure and function of connective and skeletal tissue. Proceedings of an advanced study institute organised under the auspices of N.A.T.O. St. Andrews (1964).
Fitton-Jackson, S.: Fibrogenesis and the formation of matrix. In: Bone as a tissue (K. Rodahl, J. T. Nicholson and E. M. Brown eds.), p. 165, New York: McGraw Hill 1960.
Frank, R. M., Nalbandian, J.: Aspects ultrastructuraux du mecanisme de la calcification. Arch. oral. Biol. (Spec. supp.) 95–109 (1963).
Glauert, A. M.: Section staining, cytology autogradiography and immunochemistry for biological specimens. In: Techniques for electron microscopy (Desmond H. Kay, ed.). Oxford: Blackwell Sci. Publ. 1965.
Gregory, J. D., Laurent, T. C., Roden, L.: Enzymatic degradation of chondromucoprotein. J. biol. Chem.329, 3312–3320 (1964).
Mathews, M. B.: Biophysical aspects of acid mucopolysaccharides relevant to connective tissue structure and function. In: The connective tissue (Bernard M. Wagner and David E. Smith, eds.). Baltimore: Williams & Wilkins Co. 1967.
—, Lozaityte, I.: Sodium chondroitin sulphate-protein complexes of cartilage I. Molecular weight and shape. Arch. Biochem.74, 158–174 (1958).
Matukas, V. J., Krikos, G. A.: Evidence for changes in protein-polysaccharide associated with the onset of calcification in cartilage. J. Cell Biol.39, 43–48 (1968).
Partridge, S. M., Davis, H. F., Adair, G. S.: The constitution of the chondroitin sulphate-protein complex in cartilage. Biochem. J.79, 15–26 (1961).
Pearse, A. G. E.: Histochemistry theoretical and applied. London: J. & A. Churchill Ltd. 1968.
Rönnholm, E.: The structure of the organic stroma of enamel during amelogenesis. J. Ultrastruct. Res.3, 368–389 (1962).
Sabatini, D. D., Bensch, K., Barnett, R. J.: Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. J. Cell Biol.17, 19–58 (1963).
Scott, D. B., Nylen, M. U.: A possible key to the mechanism of caries. Int. dent. J.12, 417–432 (1962).
Stowel, R. E., Zorzoli, A.: The action of ribonuclease on fixed tissues. Stain Technol.22, 51–61 (1947).
Sundström, B.: A new technique for decalcifying thin ground specimens of adult human enamel. Arch. oral. Biol.2, 1221–1231 (1966).
—, Zelander, T.: Routine decalcification of thin sawed sections of adult human enamel by means of basic chromium (III) sulphate solution of stable pH. Odont. Revy19, 249–263 (1968a).
——: On the morphological organisation of the organic matrix of adult human enamel after decalcification by means of a basic chromium (III) sulphate solution. Odont. Revy19, 264–278 (1968b).
Takuma, S.: Electron microscopy of the developing cartilagenous epiphysis. Arch. oral Biol.2, 111–119 (1960).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Appleton, J. Ultrastructural observations on the inorganic/organic rellationships in early cartilage calcification. Calc. Tis Res. 7, 307–317 (1971). https://doi.org/10.1007/BF02062620
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02062620