Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1984 Apr 15;219(2):625–634. doi: 10.1042/bj2190625

Complete amino acid sequence of the N-terminal extension of calf skin type III procollagen.

A Brandt, R W Glanville, D Hörlein, P Bruckner, R Timpl, P P Fietzek, K Kühn
PMCID: PMC1153521  PMID: 6331392

Abstract

The N-terminal extension peptide of type III procollagen, isolated from foetal-calf skin, contains 130 amino acid residues. To determine its amino acid sequence, the peptide was reduced and carboxymethylated or aminoethylated and fragmented with trypsin, Staphylococcus aureus V8 proteinase and bacterial collagenase. Pyroglutamate aminopeptidase was used to deblock the N-terminal collagenase fragment to enable amino acid sequencing. The type III collagen extension peptide is homologous to that of the alpha 1 chain of type I procollagen with respect to a three-domain structure. The N-terminal 79 amino acids, which contain ten of the 12 cysteine residues, form a compact globular domain. The next 39 amino acids are in a collagenase triplet sequence (Gly- Xaa - Yaa )n with a high hydroxyproline content. Finally, another short non-collagenous domain of 12 amino acids ends at the cleavage site for procollagen aminopeptidase, which cleaves a proline-glutamine bond. In contrast with type I procollagen, the type III procollagen extension peptides contain interchain disulphide bridges located at the C-terminus of the triple-helical domain.

Full text

PDF
625

Selected References

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

  1. Becker U., Helle O., Timpl R. Characterization of the amino-terminal segment in procollagen palpha2 chain from dermatosparactic sheep. FEBS Lett. 1977 Feb 1;73(2):197–200. doi: 10.1016/0014-5793(77)80979-4. [DOI] [PubMed] [Google Scholar]
  2. Bruckner P., Bächinger H. P., Timpl R., Engel J. Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transition. Eur J Biochem. 1978 Oct 16;90(3):595–603. doi: 10.1111/j.1432-1033.1978.tb12640.x. [DOI] [PubMed] [Google Scholar]
  3. Byers P. H., McKenney K. H., Lichtenstein J. R., Martin G. R. Preparation of type III procollagen and collagen from rat skin. Biochemistry. 1974 Dec 3;13(25):5243–5248. doi: 10.1021/bi00722a030. [DOI] [PubMed] [Google Scholar]
  4. Curran S., Prockop D. J. Isolation and partial characterization of the amino-terminal propeptide of type II procollagen from chick embryos. Biochemistry. 1982 Mar 30;21(7):1482–1487. doi: 10.1021/bi00536a003. [DOI] [PubMed] [Google Scholar]
  5. Engel J., Bruckner P., Becker U., Timpl R., Rutschmann B. Physical properties of the amino-terminal precursor-specific portion of type I procollagen. Biochemistry. 1977 Sep 6;16(18):4026–4033. doi: 10.1021/bi00637a014. [DOI] [PubMed] [Google Scholar]
  6. Fietzek P. P., Rexrodt F. W. The covalent structure of collagen. The amino-acid sequence of alpha2-CB4 from calf-skin collagen. Eur J Biochem. 1975 Nov 1;59(1):113–118. doi: 10.1111/j.1432-1033.1975.tb02431.x. [DOI] [PubMed] [Google Scholar]
  7. Fleischmajer R., Timpl R., Tuderman L., Raisher L., Wiestner M., Perlish J. S., Graves P. N. Ultrastructural identification of extension aminopropeptides of type I and III collagens in human skin. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7360–7364. doi: 10.1073/pnas.78.12.7360. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Glanville R. W., Fietzek P. P. Amino acid sequence to the N-terminal non-triple helical cross link region of type III collagen. FEBS Lett. 1976 Nov 15;72(1):99–102. doi: 10.1016/0014-5793(76)80907-6. [DOI] [PubMed] [Google Scholar]
  9. Glanville R. W., Rauter A. Pepsin fragments of human placental basement-membrane collagens showing interrupted triple-helical amino acid sequences. Hoppe Seylers Z Physiol Chem. 1981 Jul;362(7):943–951. doi: 10.1515/bchm2.1981.362.2.943. [DOI] [PubMed] [Google Scholar]
  10. Gollwitzer R., Becker U., Timpl R. Isolation and chemical characterization of reduced and aminoethylated polypeptide chains of bovine fibrinogen. FEBS Lett. 1974 Oct 1;47(1):177–180. doi: 10.1016/0014-5793(74)80453-9. [DOI] [PubMed] [Google Scholar]
  11. Gollwitzer R., Timpl R., Becker U., Furthmayr H. Chemical and immunological properties of reduced and alkylated polypeptide chains of bovine fibrinogen. Eur J Biochem. 1972 Aug 4;28(4):497–506. doi: 10.1111/j.1432-1033.1972.tb01937.x. [DOI] [PubMed] [Google Scholar]
  12. Henkel W., Glanville R. W. Covalent crosslinking between molecules of type I and type III collagen. The involvement of the N-terminal, nonhelical regions of the alpha 1 (I) and alpha 1 (III) chains in the formation of intermolecular crosslinks. Eur J Biochem. 1982 Feb;122(1):205–213. doi: 10.1111/j.1432-1033.1982.tb05868.x. [DOI] [PubMed] [Google Scholar]
  13. Hörlein D., Fietzek P. P., Wachter E., Lapière C. M., Kühn K. Amino acid sequence of the aminoterminal segment of dermatosparactic calf-skin procollagen type I. Eur J Biochem. 1979 Aug 15;99(1):31–38. doi: 10.1111/j.1432-1033.1979.tb13227.x. [DOI] [PubMed] [Google Scholar]
  14. Inglis A. S. Cleavage at aspartic acid. Methods Enzymol. 1983;91:324–332. doi: 10.1016/s0076-6879(83)91030-3. [DOI] [PubMed] [Google Scholar]
  15. Klapper D. G., Wilde C. E., 3rd, Capra J. D. Automated amino acid sequence of small peptides utilizing Polybrene. Anal Biochem. 1978 Mar;85(1):126–131. doi: 10.1016/0003-2697(78)90282-8. [DOI] [PubMed] [Google Scholar]
  16. Krieg T., Hörlein D., Wiestner M., Müller P. K. Aminoterminal extension peptides from type I procollagen normalize excessive collagen synthesis of scleroderma fibroblasts. Arch Dermatol Res. 1978 Nov 10;263(2):171–180. doi: 10.1007/BF00446438. [DOI] [PubMed] [Google Scholar]
  17. Lenaers A., Lapiere C. M. Type III procollagen and collagen in skin. Biochim Biophys Acta. 1975 Jul 21;400(1):121–131. doi: 10.1016/0005-2795(75)90132-4. [DOI] [PubMed] [Google Scholar]
  18. Morikawa T., Tuderman L., Prockop D. J. Inhibitors of procollagen N-protease. Synthetic peptides with sequences similar to the cleavage site in the pro alpha 1(I) chain. Biochemistry. 1980 Jun 10;19(12):2646–2650. doi: 10.1021/bi00553a017. [DOI] [PubMed] [Google Scholar]
  19. Nowack H., Olsen B. R., Timpl R. Characterization of the amino-terminal segment in type III procollagen. Eur J Biochem. 1976 Nov 1;70(1):205–216. doi: 10.1111/j.1432-1033.1976.tb10971.x. [DOI] [PubMed] [Google Scholar]
  20. Nusgens B. V., Goebels Y., Shinkai H., Lapière C. M. Procollagen type III N-terminal endopeptidase in fibroblast culture. Biochem J. 1980 Dec 1;191(3):699–706. doi: 10.1042/bj1910699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nusgens B., Lapiere C. M. A simplified procedure for measuring amino-procollagen peptidase type I. Anal Biochem. 1979 Jun;95(2):406–412. doi: 10.1016/0003-2697(79)90747-4. [DOI] [PubMed] [Google Scholar]
  22. Paglia L. M., Wiestner M., Duchene M., Ouellette L. A., Hörlein D., Martin G. R., Müller P. K. Effects of procollagen peptides on the translation of type II collagen messenger ribonucleic acid and on collagen biosynthesis in chondrocytes. Biochemistry. 1981 Jun 9;20(12):3523–3527. doi: 10.1021/bi00515a034. [DOI] [PubMed] [Google Scholar]
  23. Paglia L., Wilczek J., de Leon L. D., Martin G. R., Hörlein D., Müller P. Inhibition of procollagen cell-free synthesis by amino-terminal extension peptides. Biochemistry. 1979 Oct 30;18(22):5030–5034. doi: 10.1021/bi00589a034. [DOI] [PubMed] [Google Scholar]
  24. Pesciotta D. M., Silkowitz M. H., Fietzek P. P., Graves P. N., Berg R. A., Olsen B. R. Purification and characterization of the amino-terminal propeptide of Pro alpha 1(I) chains from embryonic chick tendon procollagen. Biochemistry. 1980 May 27;19(11):2447–2454. doi: 10.1021/bi00552a024. [DOI] [PubMed] [Google Scholar]
  25. Rohde H., Becker U., Nowack H., Timpl R. Antigenic structure of the aminoterminal region in type I procollagen. Characterization of sequential and conformational determinants. Immunochemistry. 1976 Dec;13(12):967–974. doi: 10.1016/0019-2791(76)90266-4. [DOI] [PubMed] [Google Scholar]
  26. Rohde H., Bruckner P., Timpl R. Immunochemical properties of the aminopropeptide of procollagen type III. Eur J Biochem. 1983 Sep 15;135(2):197–202. doi: 10.1111/j.1432-1033.1983.tb07637.x. [DOI] [PubMed] [Google Scholar]
  27. Rohde H., Langer I., Krieg T., Timpl R. Serum and urine analysis of the aminoterminal procollagen peptide type III by radioimmunoassay with antibody Fab fragments. Coll Relat Res. 1983 Sep;3(5):371–379. doi: 10.1016/s0174-173x(83)80018-1. [DOI] [PubMed] [Google Scholar]
  28. Rohde H., Vargas L., Hahn E., Kalbfleisch H., Bruguera M., Timpl R. Radioimmunoassay for type III procollagen peptide and its application to human liver disease. Eur J Clin Invest. 1979 Dec;9(6):451–459. doi: 10.1111/j.1365-2362.1979.tb00912.x. [DOI] [PubMed] [Google Scholar]
  29. Rohde H., Wachter E., Richter W. J., Bruckner P., Helles O., Timpl R. Amino acid sequence of the N-terminal non-collagenous segment of dermatosparactic sheep procollagen type I. Biochem J. 1979 Jun 1;179(3):631–642. doi: 10.1042/bj1790631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Shinkai H., Lapiere C. M. Characterization of oligosaccharide units of p-N-collagen type III from dermatosparactic bovine skin. Biochim Biophys Acta. 1983 Jul 5;758(1):30–36. doi: 10.1016/0304-4165(83)90006-5. [DOI] [PubMed] [Google Scholar]
  31. Tate V. E., Finer M. H., Boedtker H., Doty P. Chick pro alpha 2 (I) collagen gene: exon location and coding potential for the prepropeptide. Nucleic Acids Res. 1983 Jan 11;11(1):91–104. doi: 10.1093/nar/11.1.91. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Timpl R., Glanville R. W., Nowack H., Wiedemann H., Fietzek P. P., Kühn K. Isolation, chemical and electron microscopical characterization of neutral-salt-soluble type III collagen and procollagen from fetal bovine skin. Hoppe Seylers Z Physiol Chem. 1975 Nov;356(11):1783–1792. doi: 10.1515/bchm2.1975.356.2.1783. [DOI] [PubMed] [Google Scholar]
  33. Tuderman L., Kivirikko K. I., Prockop D. J. Partial purification and characterization of a neutral protease which cleaves the N-terminal propeptides from procollagen. Biochemistry. 1978 Jul 25;17(15):2948–2954. doi: 10.1021/bi00608a002. [DOI] [PubMed] [Google Scholar]
  34. Wiestner M., Krieg T., Hörlein D., Glanville R. W., Fietzek P., Müller P. K. Inhibiting effect of procollagen peptides on collagen biosynthesis in fibroblast cultures. J Biol Chem. 1979 Aug 10;254(15):7016–7023. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES