Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1967 Aug 1;126(2):331–346. doi: 10.1084/jem.126.2.331

THE SEROLOGIC SPECIFICITY OF TROPOCOLLAGEN TELOPEPTIDES

Peter F Davison 1, Lawrence Levine 1, Maurice P Drake 1, Albert Rubin 1, Susan Bump 1
PMCID: PMC2138319  PMID: 6028490

Abstract

Tropocollagen preparations from carp, buffalo fish, rats, calves, sheep, and humans have been studied by electron microscopy and serologic methods. Tropocollagens from each species appeared identical by electron microscopy but they were readily distinguished (except between sheep and calves) by C'-fixation tests with rabbit antisera against the various tropocollagens. Tests with calf tropocollagen antiserum showed no distinction between tropocollagen isolated from different tissues nor between individuals of the same or different strains. The major immunogenic sites in native tropocollagen are the telopeptides, and these are present on both α1- and α2-chains. The C'-fixing activity was lost with heat denaturation of the tropocollagen, but could be recovered in a concentration-dependent process on cooling. The fact that pure and enzyme-treated collagen can provoke serologic reaction implies that collagenous sutures and prostheses used in surgery may lead to sensitization and rejection, a fact which may merit clinical concern.

Full Text

The Full Text of this article is available as a PDF (960.9 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ALTGELT K., HODGE A. J., SCHMITT F. O. Gamma tropocollagen: a reversibly denaturable collagen macromolecule. Proc Natl Acad Sci U S A. 1961 Dec 15;47:1914–1924. doi: 10.1073/pnas.47.12.1914. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BORNSTEIN P., PIEZ K. A. A BIOCHEMICAL STUDY OF HUMAN SKIN COLLAGEN AND THE RELATION BETWEEN INTRA- AND INTERMOLECULAR CROSS-LINKING. J Clin Invest. 1964 Sep;43:1813–1823. doi: 10.1172/JCI105055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Beier G., Engel J. The renaturation of soluble collagen. Products formed at different temperatures. Biochemistry. 1966 Aug;5(8):2744–2755. doi: 10.1021/bi00872a035. [DOI] [PubMed] [Google Scholar]
  4. Davison P. F., Drake M. P. The physical characterization of monomeric tropocollagen. Biochemistry. 1966 Jan;5(1):313–321. doi: 10.1021/bi00865a040. [DOI] [PubMed] [Google Scholar]
  5. Drake M. P., Davison P. F., Bump S., Schmitt F. O. Action of proteolytic enzymes on tropocollagen and insoluble collagen. Biochemistry. 1966 Jan;5(1):301–312. doi: 10.1021/bi00865a039. [DOI] [PubMed] [Google Scholar]
  6. Francois C. J., Glimcher M. J. The separation of the alpha-chains of collagen by free-flow electrophoresis. Biochem J. 1967 Jan;102(1):148–152. doi: 10.1042/bj1020148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HANNIG K. EINE NEUENTWICKLUNG DER TRAEGERFREIEN KONTINUIERLICHEN ELEKTROPHORESE. ZUR TRENNUNG HOCHMOLEKULARER UND GROBDISPERSER TEILCHEN. Hoppe Seylers Z Physiol Chem. 1964;338:211–227. doi: 10.1515/bchm2.1964.338.1-2.211. [DOI] [PubMed] [Google Scholar]
  8. PIEZ K. A., CARRILLO A. L. HELIX FORMATION BY SINGLE- AND DOUBLE-CHAIN GELATINS FROM RAT SKIN COLLAGEN. Biochemistry. 1964 Jul;3:908–914. doi: 10.1021/bi00895a009. [DOI] [PubMed] [Google Scholar]
  9. PIEZ K. A., LEWIS M. S., MARTIN G. R., GROSS J. Subunits of the collagen molecule. Biochim Biophys Acta. 1961 Nov 11;53:596–598. doi: 10.1016/0006-3002(61)90226-8. [DOI] [PubMed] [Google Scholar]
  10. ROTHBARD S., WATSON R. F. Antigenicity of rat collagen. Distribution of antibody to rat collagen injected into rats. J Exp Med. 1962 Sep 1;116:337–346. doi: 10.1084/jem.116.3.337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. ROTHBARD S., WATSON R. F. Antigenicity of rat collagen; reverse anaphylaxis induced in rats by anti-rat collagen serum. J Exp Med. 1956 Jan 1;103(1):57–72. doi: 10.1084/jem.103.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. RUBIN A. L., PFAHL D., SPEAKMAN P. T., DAVISON P. F., SCHMITT F. O. Tropocollagen: significance of protease-induced alterations. Science. 1963 Jan 4;139(3549):37–39. doi: 10.1126/science.139.3549.37. [DOI] [PubMed] [Google Scholar]
  13. Rothbard S., Watson R. F. Immunologic relations among various animal collagens. J Exp Med. 1965 Sep 1;122(3):441–454. doi: 10.1084/jem.122.3.441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. SCHMITT F. O., LEVINE L., DRAKE M. P., RUBIN A. L., PFAHL D., DAVISON P. F. THE ANTIGENICITY OF TROPOCOLLAGEN. Proc Natl Acad Sci U S A. 1964 Mar;51:493–497. doi: 10.1073/pnas.51.3.493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. SCHMITT F. O. TELOPEPTIDE CONTROL OF TROPOCOLLAGEN INTERACTION DYNAMICS. Fed Proc. 1964 May-Jun;23:618–622. [PubMed] [Google Scholar]
  16. STEFFEN C., TIMPL R., WOLFF I. IMMUNOGENICITY AND SPECIFICITY OF COLLAGEN. II. INVESTIGATIONS ABOUT SPECIFICITY OF COLLAGEN AND ITS DERIVATIVES BY HEMAGGLUTINATION AND HEMAGGLUTINATION-INHIBITION OF ANTI-COLLAGEN AND ANTI-PARENT GELATINE IMMUNE SERA. J Immunol. 1964 Oct;93:656–667. [PubMed] [Google Scholar]
  17. VEIS A., DRAKE M. P. The introduction of intramolecular cocalent cross-linkages into ichthyocol tropocollagen with monofunctional aldehydes. J Biol Chem. 1963 Jun;238:2003–2011. [PubMed] [Google Scholar]
  18. Veis A., Anesey J. Modes of intermolecular cross-linking in mature insoluble collagen. J Biol Chem. 1965 Oct;240(10):3899–3908. [PubMed] [Google Scholar]
  19. WATSON R. F., ROTHBARD S., VANAMEE P. The antigenicity of rat collagen. J Exp Med. 1954 Jun 1;99(6):535–550. doi: 10.1084/jem.99.6.535. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES