Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1990 Jun 1;268(2):267–274. doi: 10.1042/bj2680267

Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP).

R A Williamson 1, F A Marston 1, S Angal 1, P Koklitis 1, M Panico 1, H R Morris 1, A F Carne 1, B J Smith 1, T J Harris 1, R B Freedman 1
PMCID: PMC1131427  PMID: 2163605

Abstract

Disulphide bonds in human recombinant tissue inhibitor of metalloproteinases (TIMP) were assigned by resolving proteolytic digests of TIMP on reverse-phase h.p.l.c. and sequencing those peaks judged to contain disulphide bonds by virtue of a change in retention time on reduction. This procedure allowed the direct assignment of Cys-145-Cys-166 and the isolation of two other peptides containing two disulphide bonds each. Further peptide cleavage in conjunction with fast-atom-bombardment m.s. analysis permitted the assignments Cys-1-Cys-70, Cys-3-Cys-99, Cys-13-Cys-124 and Cys-127-Cys-174 from these peptides. The sixth bond Cys-132-Cys-137 was assigned by inference, as the native protein has no detectable free thiol groups.

Full text

PDF
267

Images in this article

269Fig. 1.
on p.269

Selected References

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

  1. Bunning R. A., Murphy G., Kumar S., Phillips P., Reynolds J. J. Metalloproteinase inhibitors from bovine cartilage and body fluids. Eur J Biochem. 1984 Feb 15;139(1):75–80. doi: 10.1111/j.1432-1033.1984.tb07978.x. [DOI] [PubMed] [Google Scholar]
  2. Cawston T. E., Galloway W. A., Mercer E., Murphy G., Reynolds J. J. Purification of rabbit bone inhibitor of collagenase. Biochem J. 1981 Apr 1;195(1):159–165. doi: 10.1042/bj1950159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dean D. D., Woessner J. F., Jr Extracts of human articular cartilage contain an inhibitor of tissue metalloproteinases. Biochem J. 1984 Feb 15;218(1):277–280. doi: 10.1042/bj2180277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Docherty A. J., Lyons A., Smith B. J., Wright E. M., Stephens P. E., Harris T. J., Murphy G., Reynolds J. J. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature. 1985 Nov 7;318(6041):66–69. doi: 10.1038/318066a0. [DOI] [PubMed] [Google Scholar]
  5. Galfre G., Howe S. C., Milstein C., Butcher G. W., Howard J. C. Antibodies to major histocompatibility antigens produced by hybrid cell lines. Nature. 1977 Apr 7;266(5602):550–552. doi: 10.1038/266550a0. [DOI] [PubMed] [Google Scholar]
  6. Gavrilovic J., Hembry R. M., Reynolds J. J., Murphy G. Tissue inhibitor of metalloproteinases (TIMP) regulates extracellular type I collagen degradation by chondrocytes and endothelial cells. J Cell Sci. 1987 Mar;87(Pt 2):357–362. doi: 10.1242/jcs.87.2.357. [DOI] [PubMed] [Google Scholar]
  7. Hembry R. M., Murphy G., Reynolds J. J. Immunolocalization of tissue inhibitor of metalloproteinases (TIMP) in human cells. Characterization and use of a specific antiserum. J Cell Sci. 1985 Feb;73:105–119. doi: 10.1242/jcs.73.1.105. [DOI] [PubMed] [Google Scholar]
  8. Herron G. S., Banda M. J., Clark E. J., Gavrilovic J., Werb Z. Secretion of metalloproteinases by stimulated capillary endothelial cells. II. Expression of collagenase and stromelysin activities is regulated by endogenous inhibitors. J Biol Chem. 1986 Feb 25;261(6):2814–2818. [PubMed] [Google Scholar]
  9. Kishi J., Hayakawa T. Purification and characterization of bovine dental pulp collagenase inhibitor. J Biochem. 1984 Aug;96(2):395–404. doi: 10.1093/oxfordjournals.jbchem.a134850. [DOI] [PubMed] [Google Scholar]
  10. Klapper M. H., Klapper I. Z. The 'knotting' problem in proteins. Loop penetration. Biochim Biophys Acta. 1980 Nov 20;626(1):97–105. doi: 10.1016/0005-2795(80)90201-9. [DOI] [PubMed] [Google Scholar]
  11. Morris H. R., Panico M., Taylor G. W. FAB-mapping of recombinant-DNA protein products. Biochem Biophys Res Commun. 1983 Nov 30;117(1):299–305. doi: 10.1016/0006-291x(83)91575-9. [DOI] [PubMed] [Google Scholar]
  12. Morris H. R., Pucci P. A new method for rapid assignment of S-S bridges in proteins. Biochem Biophys Res Commun. 1985 Feb 15;126(3):1122–1128. doi: 10.1016/0006-291x(85)90302-x. [DOI] [PubMed] [Google Scholar]
  13. Murphy G., Cawston T. E., Reynolds J. J. An inhibitor of collagenase from human amniotic fluid. Purification, characterization and action on metalloproteinases. Biochem J. 1981 Apr 1;195(1):167–170. doi: 10.1042/bj1950167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Murphy G., Reynolds J. J., Werb Z. Biosynthesis of tissue inhibitor of metalloproteinases by human fibroblasts in culture. Stimulation by 12-O-tetradecanoylphorbol 13-acetate and interleukin 1 in parallel with collagenase. J Biol Chem. 1985 Mar 10;260(5):3079–3083. [PubMed] [Google Scholar]
  15. Murphy G., Werb Z. Tissue inhibitor of metalloproteinases. Identification of precursor forms synthesized by human fibroblasts in culture. Biochim Biophys Acta. 1985 Apr 17;839(2):214–218. doi: 10.1016/0304-4165(85)90039-x. [DOI] [PubMed] [Google Scholar]
  16. Okada Y., Watanabe S., Nakanishi I., Kishi J., Hayakawa T., Watorek W., Travis J., Nagase H. Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases. FEBS Lett. 1988 Feb 29;229(1):157–160. doi: 10.1016/0014-5793(88)80817-2. [DOI] [PubMed] [Google Scholar]
  17. Stetler-Stevenson W. G., Krutzsch H. C., Liotta L. A. Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family. J Biol Chem. 1989 Oct 15;264(29):17374–17378. [PubMed] [Google Scholar]
  18. Stricklin G. P., Welgus H. G. Human skin fibroblast collagenase inhibitor. Purification and biochemical characterization. J Biol Chem. 1983 Oct 25;258(20):12252–12258. [PubMed] [Google Scholar]
  19. Wootton J. C., Baron A. J., Fincham J. R. The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptides from digestion with a staphylococcal proteinase. Biochem J. 1975 Sep;149(3):749–755. doi: 10.1042/bj1490749. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES