Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1975 Aug;149(2):381–385. doi: 10.1042/bj1490381

The chemistry of the collagen cross-links. The mechanism of stabilization of the reducible intermediate cross-links.

S P Robins, A J Bailey
PMCID: PMC1165631  PMID: 1237296

Abstract

The periodate-degradation technique was used to demonstrate the mechanism by which the reducible cross-links of collagen are stabilized. In all the tissues examined, Smith degradations of the 3H-labelled cross-links indicated that dihydroxylysinonorleucine is derived solely from hydroxylysino-5-oxonorleucine, the Amadori-rearranged product of the original condensation reaction. Monohydroxylysinonorleucine exists in both keto and aldimine forms, the former being derived from hydroxyallysine and the latter from allysine. Their relative proportions are tissue-dependent and are related to the degree of hydroxylation of the specific lysine residues in both the telopeptides and the triple helix.

Full text

PDF
381

Selected References

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

  1. Bailey A. J., Peach C. M., Fowler L. J. Chemistry of the collagen cross-links. Isolation and characterization of two intermediate intermolecular cross-links in collagen. Biochem J. 1970 May;117(5):819–831. doi: 10.1042/bj1170819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bailey A. J., Peach C. M. Isolation and structural identification of a labile intermolecular crosslink in collagen. Biochem Biophys Res Commun. 1968 Dec 9;33(5):812–819. doi: 10.1016/0006-291x(68)90233-7. [DOI] [PubMed] [Google Scholar]
  3. Bailey A. J., Robins S. P., Balian G. Biological significance of the intermolecular crosslinks of collagen. Nature. 1974 Sep 13;251(5471):105–109. doi: 10.1038/251105a0. [DOI] [PubMed] [Google Scholar]
  4. Barnes M. J., Constable B. J., Morton L. F., Kodicek E. Hydroxylysine in the N-terminal regions of the 1 - and 2 -chains of various collagens. Biochem J. 1971 Nov;125(2):433–437. doi: 10.1042/bj1250433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Barnes M. J., Constable B. J., Morton L. F., Kodicek E. Hydroxylysine in the N-terminal telopeptides of skin collagen from chick embryo and newborn rat. Biochem J. 1971 Dec;125(3):925–928. doi: 10.1042/bj1250925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Barnes M. J., Constable B. J., Morton L. F., Royce P. M. Age-related variations in hydroxylation of lysine and proline in collagen. Biochem J. 1974 May;139(2):461–468. doi: 10.1042/bj1390461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Clamp J. R., Hough L. Some observations on the periodate oxidation of amino compounds. Biochem J. 1966 Oct;101(1):120–126. doi: 10.1042/bj1010120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Davis N. R. Stable crosslinks of collagen. Biochem Biophys Res Commun. 1973 Oct 1;54(3):914–922. doi: 10.1016/0006-291x(73)90781-x. [DOI] [PubMed] [Google Scholar]
  9. Deshmukh K., Nimni M. E. In vitro formation of crosslinks in mature rat skin collagen in the absence of N-terminal peptides. Biochem Biophys Res Commun. 1971 Apr 16;43(2):416–422. doi: 10.1016/0006-291x(71)90769-8. [DOI] [PubMed] [Google Scholar]
  10. Eyre D. R., Glimcher M. J. Analysis of a crosslinked peptide from calf bone collagen: evidence that hydroxylysyl glycoside participates in the crosslink. Biochem Biophys Res Commun. 1973 May 15;52(2):663–671. doi: 10.1016/0006-291x(73)90764-x. [DOI] [PubMed] [Google Scholar]
  11. Hulmes D. J., Miller A., Parry D. A., Piez K. A., Woodhead-Galloway J. Analysis of the primary structure of collagen for the origins of molecular packing. J Mol Biol. 1973 Sep 5;79(1):137–148. doi: 10.1016/0022-2836(73)90275-1. [DOI] [PubMed] [Google Scholar]
  12. Kang A. H. Studies on the location of intermolecular cross-links in collagen. Isolation of a CNBr peptide containing -hydroxylysinonorleucine. Biochemistry. 1972 May 9;11(10):1828–1835. doi: 10.1021/bi00760a015. [DOI] [PubMed] [Google Scholar]
  13. Kuboki Y., Tanzer M. L., Mechanic G. L. Isolation of polypeptides containing the intermolecular cross-link , '-dihydroxylysinonorleucine from dentin collagen. Arch Biochem Biophys. 1973 Sep;158(1):106–115. doi: 10.1016/0003-9861(73)90602-4. [DOI] [PubMed] [Google Scholar]
  14. Mechanic G. L. Collagen crosslinks: direct evidence of a reducible stable form of the Schiff base delta-6 dehydro-5,5-dihydroxylysinonorleucine as 5-keto-5'hydroxylysinonorleucine in bone collagen. Biochem Biophys Res Commun. 1974 Feb 27;56(4):923–927. doi: 10.1016/s0006-291x(74)80276-7. [DOI] [PubMed] [Google Scholar]
  15. Mechanic G. L., Kuboki Y., Shimokawa H., Nakamoto K., Sasaki S., Kawanishi Y. Collagen crosslinks: direct quantitative determination of stable structural crosslinks in bone and dentin collagens. Biochem Biophys Res Commun. 1974 Sep 23;60(2):756–763. doi: 10.1016/0006-291x(74)90305-2. [DOI] [PubMed] [Google Scholar]
  16. Miller E. J. Collagen cross-linking: identification of two cyanogen bromide peptides containing sites of intermolecular cross-link formation in cartilage collagen. Biochem Biophys Res Commun. 1971 Oct 15;45(2):444–451. doi: 10.1016/0006-291x(71)90839-4. [DOI] [PubMed] [Google Scholar]
  17. Miller E. J., Lane J. M., Piez K. A. Isolation and characterization of the peptides derived from the alpha-1 chain of chick bone collagen after cyanogen bromide cleavage. Biochemistry. 1969 Jan;8(1):30–39. doi: 10.1021/bi00829a006. [DOI] [PubMed] [Google Scholar]
  18. Miller E. J., Lunde L. G. Isolation and characterization of the cyanogen bromide peptides from the alpha 1(II) chain of bovine and human cartilage collagen. Biochemistry. 1973 Aug 14;12(17):3153–3159. doi: 10.1021/bi00741a003. [DOI] [PubMed] [Google Scholar]
  19. Miller E. J., Robertson P. B. The stability of collagen cross-links when derived from hydroxylsyl residues. Biochem Biophys Res Commun. 1973 Sep 5;54(1):432–439. doi: 10.1016/0006-291x(73)90940-6. [DOI] [PubMed] [Google Scholar]
  20. Robins S. P., Bailey A. J. Relative stabilities of the intermediate reducible crosslinks present in collagen fibres. FEBS Lett. 1973 Jul 1;33(2):167–174. doi: 10.1016/0014-5793(73)80184-x. [DOI] [PubMed] [Google Scholar]
  21. Robins S. P., Shimokomaki M., Bailey A. J. The chemistry of the collagen cross-links. Age-related changes in the reducible components of intact bovine collagen fibres. Biochem J. 1973 Apr;131(4):771–780. doi: 10.1042/bj1310771. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES