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. 1970 Nov;67(3):1307–1314. doi: 10.1073/pnas.67.3.1307

Relationship between the Intra and Intermolecular Cross-links of Collagen*

Andrew H Kang 1,†, Jerome Gross 1
PMCID: PMC283353  PMID: 5274460

Abstract

Spontaneous cross-linking in vitro, during incubation of purified collagen in nonstriated and native type fibrils, was studied to elucidate the relationship between intra and intermolecular cross-links. In nonbanded fibrils, the aldol condensation products of two allysyl residues, previously shown to constitute the intramolecular cross-link, formed spontaneously and could be isolated as such, whereas in native type fibrils, these compounds were found to be incorporated into an intermolecular cross-link; after chemical reduction they could not be isolated. Similar results were obtained from studies on a native collagenous tissue, rat tail tendon. It is suggested that the intramolecular cross-link is not a separate entity but only an intermediate of an intermolecular cross-link and that its existence in solubilized collagen is a result of the extraction procedure. The quantitative formation of intramolecular cross-links in vitro and identification of the cross-link compound are also reported.

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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. 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]
  2. Bornstein P., Piez K. A. The nature of the intramolecular cross-links in collagen. The separation and characterization of peptides from the cross-link region of rat skin collagen. Biochemistry. 1966 Nov;5(11):3460–3473. doi: 10.1021/bi00875a012. [DOI] [PubMed] [Google Scholar]
  3. Deshmukh A. D., Nimni M. E. In vitro formation of intramolecular crosslinks in tropocollagen. Biochem Biophys Res Commun. 1969 Jun 27;35(6):845–853. doi: 10.1016/0006-291x(69)90701-3. [DOI] [PubMed] [Google Scholar]
  4. Franzblau C., Kang A. H., Faris B. In vitro formation of intermolecular crosslinks in chick skin collagen. II. Kinetics. Biochem Biophys Res Commun. 1970 Jul 27;40(2):437–444. doi: 10.1016/0006-291x(70)91028-4. [DOI] [PubMed] [Google Scholar]
  5. GROSS J., KIRK D. The heat precipitation of collagen from neutral salt solutions: some rate-regulating factors. J Biol Chem. 1958 Aug;233(2):355–360. [PubMed] [Google Scholar]
  6. Kang A. H., Faris B., Franzblau C. Intramolecular cross-link of chick skin collagen. Biochem Biophys Res Commun. 1969 Aug 7;36(3):345–349. doi: 10.1016/0006-291x(69)90570-1. [DOI] [PubMed] [Google Scholar]
  7. Kang A. H., Faris B., Franzblau C. The in vitro formation of intermolecular cross-links in chick skin collagen. Biochem Biophys Res Commun. 1970 Apr 8;39(1):175–182. doi: 10.1016/0006-291x(70)90774-6. [DOI] [PubMed] [Google Scholar]
  8. Kang A. H., Gross J. Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen. Biochemistry. 1970 Feb 17;9(4):796–804. doi: 10.1021/bi00806a012. [DOI] [PubMed] [Google Scholar]
  9. Kang A. H., Piez K. A., Gross J. Characterization of the alpha-chains of chick skin collagen and the nature of the NH2-terminal cross-link region. Biochemistry. 1969 Sep;8(9):3648–3655. doi: 10.1021/bi00837a023. [DOI] [PubMed] [Google Scholar]
  10. Kang A. H., Piez K. A., Gross J. Characterization of the cyanogen bromide peptides from the alpha 1 chain of chick skin collagen. Biochemistry. 1969 Apr;8(4):1506–1514. doi: 10.1021/bi00832a029. [DOI] [PubMed] [Google Scholar]
  11. Piez K. A. Cross-linking of collagen and elastin. Annu Rev Biochem. 1968;37:547–570. doi: 10.1146/annurev.bi.37.070168.002555. [DOI] [PubMed] [Google Scholar]
  12. Pinnell S. R., Martin G. R. The cross-linking of collagen and elastin: enzymatic conversion of lysine in peptide linkage to alpha-aminoadipic-delta-semialdehyde (allysine) by an extract from bone. Proc Natl Acad Sci U S A. 1968 Oct;61(2):708–716. doi: 10.1073/pnas.61.2.708. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rojkind M., Gutierrez A. M., Zeichner M., Lent R. W. The nature of the intramolecular cross-link in collagen. Biochem Biophys Res Commun. 1969 Aug 7;36(3):350–356. doi: 10.1016/0006-291x(69)90571-3. [DOI] [PubMed] [Google Scholar]
  14. Schiffmann E., Martin G. R. Spontaneous generation of cross-links in aldehyde-containing collagen. Arch Biochem Biophys. 1970 May;138(1):226–232. doi: 10.1016/0003-9861(70)90302-4. [DOI] [PubMed] [Google Scholar]
  15. Tanzer M. L. Collagen reduction by sodium borohydride: effects of reconstitution, maturation and lathyrism. Biochem Biophys Res Commun. 1968 Sep 6;32(5):885–892. doi: 10.1016/0006-291x(68)90324-0. [DOI] [PubMed] [Google Scholar]
  16. Tanzer M. L. Intermolecular cross-links in reconstituted collagen fibrils. Evidence for the nature of the covalent bonds. J Biol Chem. 1968 Aug 10;243(15):4045–4054. [PubMed] [Google Scholar]

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