Thermal Transitions in Collagenous Tissues as Sensors of the Environment

  • B. J. Rigby
Part of the NATO Advanced Science Institutes Series book series (NSSA, volume 62)


Collagen is the family name of a group of genetically distinct protein molecules that has evolved as the major fibrous component of the extra-cellular matrix. The other components of this matrix — the weight fractions of which depend upon the function of the particular tissue — include the proteins elastin and keratin, mucopolysaccharides, proteoglycans, and lipids irrigated by a solution containing a number of inorganic ions notably Na+, Cl-, Ca++, K+, vitamins and free oxygen.


Thermal Transition Collagen Molecule Collagenous Tissue Total Amino Acid Content Shrinkage Temperature 


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  1. BAILEY, A.J., RANTA, M.A., NICHOLLS, A.C., PARTRIDGE, S.M. and ELSDEN, D.F. (1977): Isolation of -amino adipic acid from mature dermal collagen and elastin. Evidence for an oxidative pathway in the maturation of collagen and elastin. Biochem. Biophys. Res. Commun. 78: 1403–1410.CrossRefGoogle Scholar
  2. BERG, R.A. and PROCKOP, D.J. (1973): The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilising the triple-helix of collagen. Biochem. Biophys. Res. Commun. 52: 115–120.CrossRefGoogle Scholar
  3. BORNSTEIN, P. and TRAUB, W. (1979): The chemistry and biology of collagen. In The Proteins. 3rd Ed. (Eds. H. Neurath and R. Hill), Vol. IV, pp. 411–632. Academic Press, New York.Google Scholar
  4. COHEN, R.E., HOOLEY, C.J., and MCCRUM, N.G. (1976): Viscoelastic creep of collagenous tissue. J. Biomechanics 9: 175–184.CrossRefGoogle Scholar
  5. FLORY, P.J. and GARRETT, R.R. (1958): Phase transitions in collagen and gelatin systems. J. Amer. Chem. Soc. 80: 4836–4845.CrossRefGoogle Scholar
  6. GOULD, B.S. (1968): The role of certain vitamins in collagen formation. In Treatise on Collagen (Ed. B.S. Gould), Vol. 2, Part A, pp. 323–365 Academic Press, New York.Google Scholar
  7. GUSTAVSON, K.H. (1956): The Chemicstry and Reactivity of Collagen, pp. 224–227. Academic Press, New York.Google Scholar
  8. GUSTAVSON, K.H. (1960): Hydrothermal denaturation of collagen. Nature 188: 419–420.CrossRefGoogle Scholar
  9. HALEY, A.R. and SMITH, J.W. (1971): Calorimetry of rat tail tendon collagen before and after denaturation: The heat of fusion of its absorbed water. Biopolymers 10: 1681–1699.CrossRefGoogle Scholar
  10. KOWN, D.S., MASON, P. and RIGBY, B.J. (1964): Influence of the tendon membrane on swelling and thermal stability. Nature 201: 159–160.CrossRefGoogle Scholar
  11. LEACH, A.A. (1957): The amino acid composition of amphibian, reptile and avian gelatins. Biochem. J. 67: 83–87.Google Scholar
  12. MASON, P., and RIGBY, B.J. (1963): Thermal transitions in collagen. Biochem. Biophys. Acta 66: 448–450.CrossRefGoogle Scholar
  13. MITCHELL, T.W. and RIGBY, B.J. (1975): In vivo and in vitro ageing of collagen, examined using an isometric melting technique. Biochem. Biophys. Acta 393: 531–541.Google Scholar
  14. OTH, J.F.M., DUMITRU, E.T., SPURR, O.K., and FLORY, P.J. (1957): Phase equilibrium in the hydrothermal shrinkage of collagen. J. Amer. Chem. Soc. 79: 3288–3289.CrossRefGoogle Scholar
  15. RAMACHANDRAN, G.M. and RAMAKRISHNAN, C. (1976): Molecular structure. In Biochemistry of Collagen (Ed. G.N. Ramachandran and A.H. Reddi), pp. 45–84. Plenum, New York.Google Scholar
  16. RIGBY, B.J. (1967a): Relation between the shrinkage temperature of native collagen in acid solution and the melting temperature of the tropocollagen molecule. Biochem. Biophys. Acta 133: 272–277.Google Scholar
  17. RIGBY, B.J. (1967b): Correlation between serine and thermal stability of collagen. Nature 214: 87–88.CrossRefGoogle Scholar
  18. RIGBY, B.J. (1967c): Thermal transitions in some invertebrate collagens and their relation to amino acid content and environmental temperture. In Symposium on Fibrous Proteins (Ed. W.G. Crewther), pp. 217–225. Butterworths, Australia.Google Scholar
  19. RIGBY, B.J. (1968a): Temperature relationships of poikilotherms and the melting temperature of molecular collagen. Biol. Bull. 135: 223–229.CrossRefGoogle Scholar
  20. RIGBY, B.J. (1968b) Amino-acid composition and thermal stability of the skin collagen of the antarctic ice-fish. Nature. 219: 166–167.CrossRefGoogle Scholar
  21. RIGBY, B.J. (1971): The thermal stability of collagen: its significance in biology and physiology. In Chemical Dynamics: Papers in Honor of Henry Eyring (Ed. J. Hirschfelder), pp. 537–555. Wiley, New York.Google Scholar
  22. RIGBY, B.J. (1977b): Thermal transitions in the collagenous tissues of Poikilothermic animals. J. Thermal Biology. 2: 89–93.CrossRefGoogle Scholar
  23. RIGBY, B.J., HIRAI, N., SPIKES, J.D. and EYRING, H. (1959): The mechanical properties of rat tail tendon. J. Gen. Physiology. 43: 265–283.CrossRefGoogle Scholar
  24. RIGBY, B.J. and MITCHELL, T.W. (1978): In vitro studies of the interaction between ascorbic acid and rat tail tendon. Biochem. Biophys. Acta. 544: 62–68.CrossRefGoogle Scholar
  25. RIGBY, B.J., MITCHELL, T.W. and ROBINSON, M. (1977a): Oxygen participation in the in vivo and in vitro ageing of collagen fibrils. Biochem. Biophys. Res. Commun. 79: 400–405.CrossRefGoogle Scholar
  26. RIGBY, B.J. and ROBINSON, M. (1975): Thermal transitions in collagen and the preferred temperature range of animals. Nature 253: 277–279.CrossRefGoogle Scholar
  27. SINEX, F.M. (1968): The role of collagen in ageing. In Treatise on Collagen (Ed. B.S. Gould), Vol. 2, Part B, pp. 409–448. Academic Press, New York.Google Scholar
  28. VEIS, A. (1967): Inact collagen. In Treatise on Collagen (Ed. G.N. Ramachandran), Vol. 1, pp. 367–439. Academic Press, New York.Google Scholar
  29. VON HIPPEL, P.H. (1967): Structure and stabilization of the collagen molecule in solution. In Treatise on Collagen (Ed. G.N. Ramachandran), Vol. 1, pp. 253–338. Academic Press, New York.Google Scholar
  30. WAINWRIGHT, S.A., BIGGS, W.D., CURREY, J.D. and GOSLINE, J.M. (1976): “Mechanical Design in Organisms”, pp. 88–93. Edward Arnold, London.Google Scholar
  31. WEISS, J.B., SEDOWOFIA, K., and JONES, C. (1980): Collagen degradation: a defended multi-enzyme system. In Biology of Collagen. (Eds. A. Viidik and J. Vuust), pp. 113–134. Academic Press, London.Google Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • B. J. Rigby
    • 1
  1. 1.CSIRO Division of Textile PhysicsRydeAustralia

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