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. 1980 Nov;77(11):6434–6438. doi: 10.1073/pnas.77.11.6434

Biosynthesis of A,B procollagen.

C A Kumamoto, J H Fessler
PMCID: PMC350299  PMID: 6779280

Abstract

Interest in cell-associated collagens led others to isolate A and B collagen chains, also known as type V collagen, from many tissues, but only after pepsin cleavage. Soluble precursors of these chains are synthesized in vitro by crop, a chicken embryo muscle tissue, and are converted by at least two processing steps from procollagens via intermediates to final forms which are large than the pepsin-derived A and B chains. Heterotrimeric, disulfide-bridged procollagen molecules corresponding to B2A exist. Components were separated by ion exchange chromatography, velocity sedimentation, and electrophoresis, and the relationships between them were established by sequential radioactive labeling and comparison of peptides generated by protease cleavage.

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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., Shellswell G. B., Duance V. C. Identification and change of collagen types in differentiating myoblasts and developing chick muscle. Nature. 1979 Mar 1;278(5699):67–69. doi: 10.1038/278067a0. [DOI] [PubMed] [Google Scholar]
  2. Bentz H., Bächinger H. P., Glanville R., Kühn K. Physical evidence for the assembly of A and B chains of human placental collagen in a single triple helix. Eur J Biochem. 1978 Dec;92(2):563–567. doi: 10.1111/j.1432-1033.1978.tb12778.x. [DOI] [PubMed] [Google Scholar]
  3. Benya P., Berger K., Golditch M., Schneir M. Recommendations concerning the use of bacterial collagenase for isolating collagen-associated molecules from tissues. Anal Biochem. 1973 May;53(1):313–316. doi: 10.1016/0003-2697(73)90438-7. [DOI] [PubMed] [Google Scholar]
  4. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  5. Burgeson R. E., El Adli F. A., Kaitila I. I., Hollister D. W. Fetal membrane collagens: identification of two new collagen alpha chains. Proc Natl Acad Sci U S A. 1976 Aug;73(8):2579–2583. doi: 10.1073/pnas.73.8.2579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chung E., Rhodes K., Miller E. J. Isolation of three collagenous components of probable basement membrane origin from several tissues. Biochem Biophys Res Commun. 1976 Aug 23;71(4):1167–1174. doi: 10.1016/0006-291x(76)90776-2. [DOI] [PubMed] [Google Scholar]
  7. Cleveland D. W., Fischer S. G., Kirschner M. W., Laemmli U. K. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem. 1977 Feb 10;252(3):1102–1106. [PubMed] [Google Scholar]
  8. Fessler L. I., Fessler J. H. Protein assembly of procollagen and effects of hydroxylation. J Biol Chem. 1974 Dec 10;249(23):7637–7646. [PubMed] [Google Scholar]
  9. Hong B. S., Davison P. F., Cannon D. J. Isolation and characterization of a distinct type of collagen from bovine fetal membranes and other tissues. Biochemistry. 1979 Oct 2;18(20):4278–4282. doi: 10.1021/bi00587a003. [DOI] [PubMed] [Google Scholar]
  10. Jimenez S. A., Yankowski R., Bashey R. I. Identification of two new collagen alpha-chains in extracts of lathyritic chick embryo tendons. Biochem Biophys Res Commun. 1978 Apr 28;81(4):1298–1306. doi: 10.1016/0006-291x(78)91277-9. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
  13. Linsenmayer T. F., Little C. D. Embryonic neural retina collagen: in vitro synthesis of high molecular weight forms of type II plus a new genetic type. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3235–3239. doi: 10.1073/pnas.75.7.3235. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mayne R., Vail M. S., Miller E. J. Characterization of the collagen chains synthesized by cultured smooth muscle cells derived from rhesus monkey thoracic aorta. Biochemistry. 1978 Feb 7;17(3):446–452. doi: 10.1021/bi00596a011. [DOI] [PubMed] [Google Scholar]
  15. Morris N. P., Fessler L. I., Fessler J. H. Procollagen propeptide release by procollagen peptidases and bacterial collagenase. J Biol Chem. 1979 Nov 10;254(21):11024–11032. [PubMed] [Google Scholar]
  16. Peterkofsky B., Diegelmann R. Use of a mixture of proteinase-free collagenases for the specific assay of radioactive collagen in the presence of other proteins. Biochemistry. 1971 Mar 16;10(6):988–994. doi: 10.1021/bi00782a009. [DOI] [PubMed] [Google Scholar]
  17. Rhodes R. K., Miller E. J. Physicochemical characterization and molecular organization of the collagen A and B chains. Biochemistry. 1978 Aug 22;17(17):3442–3448. doi: 10.1021/bi00610a003. [DOI] [PubMed] [Google Scholar]
  18. Trelstad R. L., Lawley K. R. Isolation and initial characterization of human basement membrane collagens. Biochem Biophys Res Commun. 1976 May 23;76(2):376–384. doi: 10.1016/0006-291x(77)90735-5. [DOI] [PubMed] [Google Scholar]
  19. von der Mark H., von der Mark H. Isolation and characterization of collagen A and B chains from chick embryos. FEBS Lett. 1979 Mar 1;99(1):101–105. doi: 10.1016/0014-5793(79)80258-6. [DOI] [PubMed] [Google Scholar]

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