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. 1969 Mar;62(3):920–927. doi: 10.1073/pnas.62.3.920

REVERSIBLE TRANSFORMATION OF FIBROUS COLLAGEN TO A SOLUBLE STATE in vivo*

LeRoy Klein 1,2
PMCID: PMC223686  PMID: 5257013

Abstract

Metabolic pathways of pre-existing and newly synthesized collagen fractions from skin and induced connective tissue were studied in rats that had been labeled with 3H-L-proline 6 and 20 weeks previously. The distribution of specific radioactivity was determined for soluble and insoluble collagens. Multiple extractions of neutral salt-soluble and citrate-soluble collagen demonstrated constant specific radioactivities which indicated the achievement of an isotopic steady state. Citrate-soluble collagen was four times more radioactive than neutral salt-soluble collagen, which indicated a large difference in biological age (months) between fractions.

Different levels of specific radioactivity in collagen fractions from implanted sponge indicated that both pre-existing (citrate-soluble) and newly synthesized collagen (salt-soluble) contributed to the insoluble collagen of induced connective tissue in normal and hypophysectomized rats. The isotopic data indicated that pre-existing fibrous collagen could be solubilized in vivo and translocated from skin to sponge via citrate-soluble collagen.

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Selected References

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

  1. BALLOU J. E., THOMPSON R. C. Studies of metabolic turnover with tritium as a tracer. V. The predominantly non-dynamic state of body constituents in the rat. J Biol Chem. 1956 Dec;223(2):795–809. [PubMed] [Google Scholar]
  2. Bailey A. J. Intermediate labile intermolecular crosslinks in collagen fibres. Biochim Biophys Acta. 1968 Aug 13;160(3):447–453. doi: 10.1016/0005-2795(68)90216-x. [DOI] [PubMed] [Google Scholar]
  3. Chulkova T. M., Orekhovich V. N. Vliianie somatotropnogo gormona na vkliuchenie radioaktivnogo prolina v prokollagen. Vopr Med Khim. 1965 Nov-Dec;11(6):76–77. [PubMed] [Google Scholar]
  4. DAVISON A. N., DOBBING J. Metabolic stability of body constituents. Nature. 1961 Aug 26;191:844–848. doi: 10.1038/191844a0. [DOI] [PubMed] [Google Scholar]
  5. GONZALEZ CADAVID N., DENDUCHIS B., MANCINI R. E. Soluble collagens in normal rat skin, from embryo to adulthood. Lab Invest. 1963 Jun;12:598–605. [PubMed] [Google Scholar]
  6. GROSS J. Studies on the formation of collagen. II. The influence of growth rate on neutral salt extracts of guinea pig dermis. J Exp Med. 1958 Feb 1;107(2):265–277. doi: 10.1084/jem.107.2.265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HARKNESS R. D., MARKO A. M., MUIR H. M., NEUBERGER A. The metabolism of collagen and other proteins of the skin of rabbits. Biochem J. 1954 Apr;56(4):558–569. doi: 10.1042/bj0560558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HENRIQUES O. B., HENRIQUES S. B., NEUBERGER A. Quantitative aspects of glycine metabolism in the rabbit. Biochem J. 1955 Jul;60(3):409–424. doi: 10.1042/bj0600409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. JACKSON D. S., BENTLEY J. P. On the significance of the extractable collagens. J Biophys Biochem Cytol. 1960 Feb;7:37–42. doi: 10.1083/jcb.7.1.37. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. JACKSON D. S. Connective tissue growth stimulated by carrageenin. I. The formation and removal of collagen. Biochem J. 1957 Feb;65(2):277–284. doi: 10.1042/bj0650277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KULONEN E., MATHEWS M. B., DORFMAN A. Studies in procollagen. I. Solubility. Proc Soc Exp Biol Med. 1953 Nov;84(2):424–428. doi: 10.3181/00379727-84-20668. [DOI] [PubMed] [Google Scholar]
  12. Klein L. R., Weiss P. H. Induced connective tissue metabolism in vivo: reutilization of pre-existing collagen. Proc Natl Acad Sci U S A. 1966 Jul;56(1):277–284. doi: 10.1073/pnas.56.1.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Klein L., Garg B. D., Nowacek C. J. Evidence for an isotopic steady state in soluble collagens. Biochem Biophys Res Commun. 1969 Jan 6;34(1):8–13. [PubMed] [Google Scholar]
  14. Klein L. Use of chronically labeled animals in the study of a "metabolically inert" protein. Adv Tracer Methodol. 1968;4:215–226. doi: 10.1007/978-1-4684-7532-6_16. [DOI] [PubMed] [Google Scholar]
  15. Klein L., Weiss P. H. Reutilization of mature collagen in vivo. Biochem Biophys Res Commun. 1965 Nov 22;21(4):311–317. doi: 10.1016/0006-291x(65)90194-4. [DOI] [PubMed] [Google Scholar]
  16. Meselson M., Stahl F. W. THE REPLICATION OF DNA IN ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1958 Jul 15;44(7):671–682. doi: 10.1073/pnas.44.7.671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. NEUBERGER A., SLACK H. G. B. The metabolism of collagen from liver, bone, skin and tendon in the normal rat. Biochem J. 1953 Jan;53(1):47–52. doi: 10.1042/bj0530047. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. NIKKARI T., KULONEN E. Studies in experimental lathyrism. II. On the properties of collagen. Biochem Pharmacol. 1962 Oct;11:931–936. doi: 10.1016/0006-2952(62)90142-9. [DOI] [PubMed] [Google Scholar]
  19. OREKHOVITCH V. N., SHPIKITER V. O. Procollagens. Science. 1958 Jun 13;127(3311):1371–1376. doi: 10.1126/science.127.3311.1371. [DOI] [PubMed] [Google Scholar]
  20. POPENOE E. A., VAN SLYKE D. D. The formation of collagen hydroxylysine. J Biol Chem. 1962 Nov;237:3491–3494. [PubMed] [Google Scholar]
  21. REITHEL F. J. THE DISSOCIATION AND ASSOCIATION OF PROTEIN STRUCTURES. Adv Protein Chem. 1963;18:123–226. doi: 10.1016/s0065-3233(08)60269-7. [DOI] [PubMed] [Google Scholar]
  22. STETTEN M. R. Some aspects of the metabolism of hydroxyproline, studied with the aid of isotopic nitrogen. J Biol Chem. 1949 Nov;181(1):31–37. [PubMed] [Google Scholar]
  23. Valavaara M., Heikkinen E., Kulonen E. Effect of hypophysectomy on the incorporation of proline in the collagen fractions. Experientia. 1968 Aug 15;24(8):779–780. doi: 10.1007/BF02144862. [DOI] [PubMed] [Google Scholar]
  24. Weiss P. H., Klein L. The quantitative relationship of urinary peptide hydroxyproline excretion to collagen degradation. J Clin Invest. 1969 Jan;48(1):1–10. doi: 10.1172/JCI105957. [DOI] [PMC free article] [PubMed] [Google Scholar]

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