Original Article

Journal of Investigative Dermatology (1979) 73, 80–83; doi:10.1111/1523-1747.ep12532769

Aging of Collagen

J Peter Bentley

Department of Biochemistry, University of Oregon Health Sciences Center, Portland, Oregon, U.S.A.

Top

Abstract

Current knowledge of the structure and the mechanism of formation of the covalent cross-links that fuse individual collagen molecules into a stable fiber is reviewed. Some of the mechanical properties of dermal connective tissue and the way in which these change with age can be correlated with the types of cross-link present in the tissue.

Cross-links are routinely detected by treatment of a tissue sample with tritium-labeled borohydride and subsequent isolation and quantification of the cross-linked compound, which has been rendered radioactive by reaction with this reducing compound. After maturity, the number of detectable cross-links decreases even though the mechanical stability of the tissue increases. This anomaly is examined in the light of recent data suggesting that cross-links may be oxidized in vivo and thus become undetectable since they can no longer react with borohydride.

Top

References

  1. Hall, DA: The Ageing of Connective Tissue 1976 New York, Academic Press,
  2. Rollet, A: Handbuch der Lehre von den Geweben 1871 1: Edited by Stricker, p, 35
  3. Gustavson, KH: The Chemistry and Reactivity of Collagen 1956 New York, Academic Press,
  4. Verzar, F: Aging of the collagen fiber. Int Rev Connect Tissue Res 1964 2: 243–300,  | PubMed |
  5. Verzar, F: Veränderungen der thermoelastischen Kontraktion von Sehnenfasern im Alter. Helvetica Physiologica et Pharmacologica Acta 1955 13: C64–C67,  | PubMed |
  6. Verzar, F: Das Altern des Killagens. Helvetica Physiologica et Pharmacologica Acta 1956 14: 207–220,  | PubMed |
  7. Verzar, F: The aging of collagen fibers. Experientia [Suppl] 1956 4: 35–41,
  8. Bjorksten, J: A common molecular basis for the aging syndrome. J Am Geriatr Soc 1958 6: 740–748,
  9. Allain, JC, LeLous, M, Bazin, S, Bailey, AJ, Delaunay, A: Isometric tension developed during heating of collagenous tissues—relationships with collagen cross linking. Biochim Biophys Acta 1978 533: 147–155,  | PubMed |
  10. Tanzer, ML: Cross-linking, Biochemistry of Collagen 1976 Edited by GN Ramachandram, AH Reddi. New York, Plenum Press, pp 137–162
  11. Robins, SP, Bailey, AJ: Age-related changes in collagen: The identification of reducible lysine-carbohydrate condensation products. Biochem Biophys Res Commun 1972 48: 76–84,  | Article | PubMed | ChemPort |
  12. Robins, SP, Bailey, AJ: The chemistry of the collagen cross links: The mechanism of stabilization of the reducible intermediate cross-links. Biochem J 1975 149: 381–385,  | PubMed | ChemPort |
  13. Eyre, DR, Glimcher, MJ: Analysis of a crosslinked peptide from calf bone collagen: Evidence that hydroxylysyl glycoside participates in the crosslink. Biochem Biophys Res Commun 1973 52: 663–671,  | Article | PubMed |
  14. Miller, EJ, Robertson, PB: The stability of collagen cross-links when derived from hydroxylysyl residues. Biochem Biophys Res Commun 1973 54: 432–439,  | Article | PubMed | ISI | ChemPort |
  15. Mechanic, GL, 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 60: 756–763,  | Article | PubMed |
  16. Robins, SP, Shimokomaki, M, Bailey, AJ: The chemistry of the collagen cross-links. Age related changes in the reducible components of intact bovine collagen fibres. Biochem J 1973 131: 771–780,  | PubMed | ISI | ChemPort |
  17. Volpin, D, Giro, MG, Castellani, I, Peserico, A: Age related changes in the reducible cross-links of human dermis collagen. Dermatologica 1977 155: 335–339,  | PubMed |
  18. Bailey, AJ, Shimokomaki, MG: Age related changes in the reducible cross-links of collagen. FEBS Lett 1971 16: 86–88,  | Article | PubMed |
  19. Mechanic, GL, Gallop, PM, Tanzer, ML: The nature of crosslinking in collagens from mineralized sources. Biochem Biophys Res Commun 1971 45: 644–653,  | Article | PubMed | ChemPort |
  20. Bailey, AJ, Peach, CM: Chemistry of collagen cross-links: The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo. Biochem J 1971 121: 257–259,  | PubMed | ChemPort |
  21. Bailey, AJ, Ranta, MH, Nicholls, AC, Partridge, SM, Elsden, DF: Isolation of alpha-aminoadipic acid from mature dermal collagen and elastin. Evidence for an oxidative pathway in the maturation of collagen and elastin. Biochem Biophys Res Commun 1977 78: 1403–1410,  | Article | PubMed |
  22. Tanzer, ML, Housley, T, Berube, L, Fairweather, R, Franzblau, C, Gallop, PM: Structure of two histidine-containing cross-links from collagen. Biol Chem 1973 248: 393–402,
  23. Robins, SP, Bailey, AJ: Relative stabilities of the intermediate reducible crosslinks present in collagen fibres. FEBS Lett 1973 33: 167–174,  | Article | PubMed | ChemPort |
  24. Fitzgibbons, JF, Koler, RD, Jones, RT: Red cell age-related changes of hemoglobins A1a+b and A1c in normal and diabetic subjects. J Clin Invest 1976 58: 820–824,  | PubMed |
  25. Gabbay, KH, Hasty, K, Breslow, JL, Ellison, RC, Bunn, HF, Gallop, PM: Glycosylated hemoglobins and long-term blood glucose control in diabetes mellitus. J Clin Endocrinol Metab 1977 44: 859–864,  | PubMed |

Extra navigation

.
ADVERTISEMENT