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The Journal of Biophysical and Biochemical Cytology logoLink to The Journal of Biophysical and Biochemical Cytology
. 1960 Feb 1;7(1):37–42. doi: 10.1083/jcb.7.1.37

On the Significance of the Extractable Collagens

David S Jackson 1, John P Bentley 1
PMCID: PMC2224869  PMID: 14406281

Abstract

This investigation has sought to determine the significance of the wide range of extractable collagen fractions which appear to exist in growing connective tissues and to determine their position in the process of fibrogenesis. Carrageenin granulomata were induced in guinea pigs and, after injection of 14C-glycine, this tissue and skin from the same animal were subjected to successive extractions with neutral salt solutions of increasing ionic strength, citrate buffer pH 3.6, and to gelatinization. The specific activity of these fractions was determined at various time intervals. At 8 hours it was found that the specific activity decreased with increasing ionic strength of the neutral salts and was still lower in the citrate extracts and gelatin. At 36 hours the situation was almost completely reversed except that the citrate extract and gelatin still had the lowest activities. The data from skin were more clear cut than that from the granuloma and the reasons for this are discussed. It is concluded that at any given time in developing connective tissue, there is a continuous spectrum of collagen aggregates of varying degrees of strength of cross-linkage, dependent upon the time that has elapsed since their constituent molecules were synthesized. The various extraction media used remove a particular cross-section of these aggregates depending upon their disaggregating power. These extracts will thus be biologically heterogeneous. The fraction extracted with 0.14 M NaCl will contain the collagen molecules most recently synthesized and in this respect can be considered the earliest form of extracellular 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. Bowes J. H., Kenten R. H. The swelling of collagen in alkaline solutions. 1. Swelling in solutions of sodium hydroxide. Biochem J. 1950 Jan;46(1):1–8. doi: 10.1042/bj0460001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. GREEN N. M., LOWTHER D. A. Formation of collagen hydroxyproline in vitro. Biochem J. 1959 Jan;71(1):55–66. doi: 10.1042/bj0710055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. GROSS J. Influence of time on the reversible association between large molecules: the collagen system. Nature. 1958 Feb 22;181(4608):556–556. doi: 10.1038/181556a0. [DOI] [PubMed] [Google Scholar]
  4. GROSS J. Studies on the formation of collagen. I. Properties and fractionation of neutral salt extracts of normal guinea pig connective tissue. J Exp Med. 1958 Feb 1;107(2):247–263. doi: 10.1084/jem.107.2.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. GROSS J. The behavior of collagen units as a model in morphogenesis. J Biophys Biochem Cytol. 1956 Jul 25;2(4 Suppl):261–274. doi: 10.1083/jcb.2.4.261. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gross J., Highberger J. H., Schmitt F. O. EXTRACTION OF COLLAGEN FROM CONNECTIVE TISSUE BY NEUTRAL SALT SOLUTIONS. Proc Natl Acad Sci U S A. 1955 Jan 15;41(1):1–7. doi: 10.1073/pnas.41.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. HIGHBERGER J. H., GROSS J., SCHMITT F. O. The interaction of mucoprotein with soluble collagen; an electron microscope study. Proc Natl Acad Sci U S A. 1951 May;37(5):286–291. doi: 10.1073/pnas.37.5.286. [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. JACKSON D. S., LEACH A. A., JACOBS S. The amino acid composition of the collagen fractions of rabbit skin. Biochim Biophys Acta. 1958 Feb;27(2):418–420. doi: 10.1016/0006-3002(58)90356-1. [DOI] [PubMed] [Google Scholar]
  12. JACKSON D. S. Some biochemical aspects of fibrogenesis and wound healing. N Engl J Med. 1958 Oct 23;259(17):814–820. doi: 10.1056/NEJM195810232591705. [DOI] [PubMed] [Google Scholar]
  13. JACKSON S. F. The formation of connective and skeletal tissues. Proc R Soc Lond B Biol Sci. 1954 Sep 27;142(909):536–548. doi: 10.1098/rspb.1954.0042. [DOI] [PubMed] [Google Scholar]
  14. NEUBERGER A., PERRONE J. C., SLACK H. G. B. The relative metabolic inertia of tendon collagen in the rat. Biochem J. 1951 Jul;49(2):199–204. [PMC free article] [PubMed] [Google Scholar]
  15. NEUMAN R. E., LOGAN M. A. The determination of hydroxyproline. J Biol Chem. 1950 May;184(1):299–306. [PubMed] [Google Scholar]
  16. OREKHOVICH V. N., SHPIKITER V. O. Molekuliarnyi ves i stepen' asimmetrii prokollagena. Biokhimiia. 1955 May-Jun;20(3):438–443. [PubMed] [Google Scholar]

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