The mineralization of hair follicle tissue
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Abstract
Hair follicle tissue from uninjured skin induced mineral formation in calcium phosphate solutions at a level of supersaturation equal to the lowest level resulting in the crystal growth and secondary nucleation of synthetic hydroxypatite. This indicates that follicle tissue contains an effective nucleator of calcium phosphate; a nucleator which could be responsible for the initial localization of mineral deposits to this tissue during skin calcificationin vivo. Hair clippings devoid of follicle tissue showed only a moderate nucleating ability. Follicle tissue which had been lyophilized and stored lost its nucleating ability, but the fact that the ability could be partly restored by treatment of the tissue with mercaptoethanol suggested that sulphydryl groups could be involved in the mechanism. The mineral precipitated from the barbitone-buffered calcifying solutions was nodular in appearance and showed the presence of octacalcium phosphate as well as hydroxyapative by X-ray diffraction. Inhibition of crystal growth and secondary nucleation by soluble follicle protein extracted into calcifying solutions was demonstrated and distinguished from the nucleation of solid mineral, phase by insoluble follicle proteins.
Key words
Nucleation Hydroxyapatite Keratin Octacalcium phosphate AdsorptionRésumé
Des follicules pileux de revêtement cutané non traumatisé induisent une minéralisation à partir de solutions de phosphate de calcium à supersaturation égale à la concentration la plus faible provoquant la croissance cristalline et une nucléation secondaire d’hydroxyleapatite synthétique. Ce fait indique que ce tissu folliculaire contient un agent de nucléation efficace du phosphate de calcium, qui pourrait être responsable de la localisation initiale des dépôts minéraux pendant la calcification cutanéein vivo. Des cheveux, dépourvus de tissu folliculaire, ne provoquent qu’une faible nucléation. Du tissu folliculaire lyophilisé et conservé perd ses propriétés de nucléation, mais étant donné que cette propriété peut être restaurée par un traitement au mercaptoethanol, il est possible que des groupes sulfhydriles soient responsables de ce mécanisme. Le minéral prècipité à partir de solutions calcifiantes, tamponnées au barbitone, est d’aspect nodulaire et montre, par diffraction aux raysons X la présence de phosphate octocalcique et d’hydroxyleapatite. L’inhibition de la croissance cristalline et de la nucléation secondaire par des protéines, solubles folliculaires est démontrée. Elle est différente de la nucléation de la phase minérale solide par des protéines folliculaires insolubles.
Zusammenfassung
Haarfollikelgewebe von intakter Haut bewirkte Mineralbildung in Calciumphosphat-Lösungen, deren Konzentration der Übersättingung entsprach, bei welcher gerade noch Kristallwachstum und sekundäre Nukleation von synthetischem Hydroxyapatit, erfolgt. Dies deutet darauf hin, daß Follikelgewebe einen wirksamen Nukleator von Calciumphosphat enthält; dieser Nukleator könnte für die anfängliche Lokalisierung von Mineralablagerungen in diesen Gewebe während der hautverkalkung in vivo verantwortlich sein. Abgeschnittene Haare, welche kein Follikelgewebe enhielten, zeigten nur eine geringe Nukleationsfähigkeit. Wird Follikelgewebe lyophilisiert oder aufbewahrt, so verliert es seine Nukleationsfähigkeit, aber die Tatsache, daß diese Fähigkeit teilweise durch die Behandlung des Gewebes mit Mercaptoäthanol wiederhergestellt werden konnte, deutete darauf hin, daß Sulfydrylgruppen an dem Mechanismus beteiligt sein könnten. Das Mineral, das aus Barbital-gepufferten kalzifizierenden Lösungen entstand, hatte ein knotiges Aussehen und zeigte in der Röntgendiffraktion die Anwesenheit, von Octocalciumphosphat sowie Hydroxyapatit. Die Hemmung von Kristallwachstum und sekundärer Nukleation durch in kalzifizierende Lösungen extrahiertes lösliches Follikelprotein wurde demonstriert, und die unterschiedliche Nukleation der festen Mineralphase durch unlösliche Follikelproteine wurde gezeigt.
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References
- Bachra, B. N., Fischer, H. R. A.: Mineral deposition in collagenin vitro. Calc. Tiss. Res.2, 343–352 (1968).CrossRefGoogle Scholar
- Bachra, B. N., Trautz, O. R., Simon, S. L.: Precipitation of calcium carbonates and phosphates. II. A precipitation diagram for the system calcium-carbonate-phosphate and the heterogeneous nucleation of solids in the metastability region. In: Advances in fluorine research and dental caries prevention (J. L. Hardwick, H. R. Held and K. G. Konig, eds.), vol. 3, p. 101–118. London: Pergamon Press 1965.Google Scholar
- Blakey, P. R., Earland, C., Stell, J. G. P.: Calcification of keratin. Nature (Lond.)198, 481 (1963).CrossRefGoogle Scholar
- Brown, W. E., Smith, J. P., Lehr, J. R., Frazier, A. W.: Octacalcium phosphate and hydroxyapatite. Nature (Lond.)196, 1048–1054 (1962).CrossRefGoogle Scholar
- Cousins, F. B., Smillie, A. C.: Studies on a skin calcifying system. Aust. J. exp. Biol. med. Sci.43, 785–802 (1965).PubMedGoogle Scholar
- Crawford, J. E., Smith, B. R.: Adsorption of polyelectrolytes during crystallization of inorganic salts. J. Colloid Interface Sci.21, 623–625 (1966).CrossRefGoogle Scholar
- Fincham, A. G.: The natural mineralization of keratins. Thesis presented to the University of Leeds, England, for the degree Doctor of Philosophy, 1966.Google Scholar
- Fraser, I. E. B.: Proteins of keratin and their synthesis. I. Proteins of prekeratin and keratins. Aust. J. biol. Sci.22, 213–229 (1969).PubMedGoogle Scholar
- Glimcher, M. J., Krane, S. M.: The organization and structure of bone, and the mechanism of calcification. In: Treatise on collagen (G. N. Ramachandran, general ed.), vol. 2B, p. 67–251. London: Academic Press 1968.Google Scholar
- Johnson, W. C., Forbes, P. D., Graham, J. H., Gray, H. R.: Experimental cutaneous calcinosis. A histopathologic and histochemical study. J. invest. Derm.43, 453–466 (1964).PubMedCrossRefGoogle Scholar
- Likins, R. C., McCann, H. G., Posner, A. S., Scott, D. B.: Comparative fixation of calcium and strontium by synthetic hydroxyapatite. J. biol. Chem.235, 2152–2156 (1960).PubMedGoogle Scholar
- Melia, T. P., Moffitt, W. P.: Secondary nucleation from aqueous solution. Ind. Engng. Chem. (Fundamentals)3, 313–317 (1964).CrossRefGoogle Scholar
- Mercer, E. H.: Keratin and keratinization. An essay in molecular biology. London: Pergamon Press 1961.Google Scholar
- Pautard, F. G. E.: Calcification of keratin. In: Progress in the biological sciences in relation to dermatology (A. Rook and R. H. Champion, eds.), vol. 2, p. 227–239. Cambridge: Cambridge University Press 1964.Google Scholar
- Pearce, E. I. F., Cousins, F. B., Smillie, A. C.: The mineralization of hair follicle tissue. I. Anin vivo study. Calc. Tiss. Res.8, 228–236 (1972).CrossRefGoogle Scholar
- Rogers, G. E.: Newer findings on the enzymes and proteins of hair follicles. Ann. N.Y. Acad. Sci.83, 408–428 (1959).PubMedCrossRefGoogle Scholar
- Schibler, D., Fleisch, H.: Inhibition of skin calcification (calciphylaxis) by polyphosphates. Experientia (Basel)22, 367–373 (1966).Google Scholar
- Schiffmann, E., Corcoran, B. A., Martin, G. R.: The role of complexed heavy metals in initiating the mineralization of elastin and the precipitation of mineral from solution. Arch. Biochem.115, 87–94 (1966).PubMedCrossRefGoogle Scholar
- Selye, A.: Calciphylaxis. Chicago: University of Chicago Press 1962.Google Scholar
- Simpson, D. R.: Apatite and octa-calcium phosphate. Effects of carbon dioxide and halogens on formation. Science (N.Y.)154, 1660–1661 (1966).Google Scholar
- Sobel, A. E.: Multiple substances and mechanisms of nucleation. In: Second European Symposium on Calcified Tissues (L. J. Richelle and M. J. Dallemagne, eds.), p. 291–298. Liege: L’Universite de Liege 1965.Google Scholar
- Solomons, C. C., Neuman, W. F.: On the mechanisms of calcification. The remineralization of dentin. J. biol. Chem.235, 2502–2506 (1960).PubMedGoogle Scholar
- Toribara, T. Y.: Centrifuge type of ultrafiltration apparatus. Analyt. Chem.25, 1286 (1953).CrossRefGoogle Scholar
- Trautz, O. R.: X-ray diffraction of biological and synthetic apatites. Ann. N.Y. Acad. Sci.60, 696–712 (1955).PubMedCrossRefGoogle Scholar
- Turesky, S., Glickman, I., Krasnoff, M.: Crystal seeding by salivary calculus and its inhibitionin vitro. Arch. oral. Biol.10, 255–260 (1965).PubMedCrossRefGoogle Scholar
- Zapanta-Le Geros, R., Le Geros, J. P., Trautz, O. R.: The effect of various ions on the unit cell dimensions and crystallinity of the apatites. J. dent. Res.43, 775–776 (1964).Google Scholar