Skip to main content

Peptidases in Connective Tissue Degradation and Remodelling in Reproductive and Invasive Tissues

  • Chapter
Cells, Membranes, and Disease, Including Renal

Abstract

An outline is given of the properties and substrate specificities of three lysosomal peptidases, and of efforts to elucidate their potential role in the intracellular degradation of collagen. Use of specific fluorogenic substrates such as Gly-Phe-NNap*, Lys-Ala-NNap and Gly-Pro-Met-NMec allows direct assay of DPP I, DPP II and TPP I respectively. They may hydrolyze macromolecules as exemplified by insulin A and B chains and by poly(Gly-Pro-Ala) as a model collagen α-chain. These are extensively hydrolyzed at acidic pH by the coupled action of the three exopeptidases, which could explain the degradation of proline-rich, collagen-derived polypeptides within lysosomes lacking any known endopeptidases active at prolyl bonds.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Miller, E.J. (1985) Ann. N.Ү. Acad. Sci. 460, 1–13.

    Article  CAS  Google Scholar 

  2. Timpl, R., Wiedemann, H., van Delden, V., Furthmayr, H. & Kühn, K. (1981) Eur. J. Biochem. 120, 203–211.

    Article  PubMed  CAS  Google Scholar 

  3. Miller, E.J. (1984) in Extracellular Matrix Biochemistry (Piez, K.A. & Reddi, A.H., eds.), Elsevier, New York, pp. 41–81.

    Google Scholar 

  4. Sellers, A. & Murphy, G. (1981) Internal. Rev. Connect. Tiss. Res. 9, 151–190.

    CAS  Google Scholar 

  5. Liotta, L.A., Thorgeirsson, U.P. & Garbisa, S. (1982) Cancer Metastasis Rev. 1, 277–288.

    Article  PubMed  CAS  Google Scholar 

  6. Woolley, D.E., Tetlow, L.C., Mooney, C.J. & Evanson, J.M. (1980) in Proteinases and Tumor Invasion (Staüli, P., Barrett, A.J. & Baici, A., eds.), Raven Press, New York, pp. 97–115.

    Google Scholar 

  7. Ten Cate, A.R. (1972) J. Anat. 112, 401–414.

    PubMed  Google Scholar 

  8. Deporter, D.A. & Ten Cate, A.R. (1973) J. Anat. 114, 457–461.

    PubMed  CAS  Google Scholar 

  9. Ten Cate, A.R. & Freeman, E. (1974) Anat. Rec. 179, 543–546.

    Article  PubMed  Google Scholar 

  10. Welsh, R.A. & Meyer, A.T. (1967) Arch. Path. 84, 354–362.

    PubMed  CAS  Google Scholar 

  11. Levine, A.M., Reddick, R. & Triche, T. (1978) Lab. Invest. 39, 531–540.

    PubMed  CAS  Google Scholar 

  12. Dingle, J.T. (1976) in Proteolysis and Physiological Regulation (Ribbons, D.W. & Brew, K., eds.), Academic Press, New York, pp. 339–355.

    Google Scholar 

  13. Woessner, J.F., Jr. (1976) in as for 12., pp. 357–369.

    Google Scholar 

  14. Singh, H., Kuo, T. & Kalnitsky, G. (1978) in Protein Turnover and Lysosome Function (Segal, H.L. & Doyle, D.J., eds.), Academic Press, New York, pp. 315–331.

    Google Scholar 

  15. Etherington, D.J. (1980) in Protein Degradation in Health and Disease, Ciba Found. Symp. 75, 87–103.

    CAS  Google Scholar 

  16. Murphy, G. & Reynolds, J.J. (1985) BioEssays 2, 55–60.

    Article  Google Scholar 

  17. Barrett, A.J. & McDonald, J.K. (1980) Mammalian Proteases: A Glossary and Bibliography, Vol. 1: The Endopeptidases, Academic Press, New York, 357 pp.

    Google Scholar 

  18. Piez, K.A., Eigner, E.A. & Lewis, M.S. (1963) Biochemistry 2, 58–66.

    Article  CAS  Google Scholar 

  19. Fietzek, P.P. & Kühn, K. (1976) Internat. Rev. Connect. Tiss. Res. 7, 1–60.

    CAS  Google Scholar 

  20. Nomenclature Committee, Internat. Union of Biochem. (1984) in Enzyme Nomenclature 1984, Academic Press, New York, pp. 330–366.

    Google Scholar 

  21. McDonald, J.K. & Barrett, A.J. (1986) Mammalian Proteases: A Glossary and Bibliography, Vol. 2: The Exopeptidases, Academic Press, New York, 416 pp.

    Google Scholar 

  22. Nomenclature Committee, Internat. Union of Biochem. (1985) Biochem. J. 231, 808 (cf. 807).

    Google Scholar 

  23. Barrett, A.J. & McDonald, J.K. (1986) Biochem. J. 237, 935.

    PubMed  CAS  Google Scholar 

  24. Bergmann, M. & Ross, W.F. (1936) J. Biol. Chem. 114, 717–726.

    CAS  Google Scholar 

  25. McDonald, J.K. (1985) Histochem. J. 17, 773–785.

    Article  PubMed  CAS  Google Scholar 

  26. McDonald, J.K., Zeitman, B.B., Reilly, T.J. & Ellis, S. (1969) J. Biol. Chem. 244, 2693–2709.

    PubMed  CAS  Google Scholar 

  27. McDonald, J.K., Hoisington, A.R. & Eisenhauer, D.A. (1985) Biochem. Biophys. Res. Comm. 126, 63–71.

    Article  PubMed  CAS  Google Scholar 

  28. McDonald, J.K., Ellis, S. & Reilly, T.J. (1966) J. Biol. Chem. 241, 1494–1501.

    PubMed  CAS  Google Scholar 

  29. McDonald, J.K., Reilly, T.J., Zeitman, B.B. & Ellis, S. (1968) J. Biol. Chem. 243, 2028–2037.

    PubMed  CAS  Google Scholar 

  30. McDonald, J.K., Callahan, P.X., Ellis, S., & Smith, R.E. (1971) in Tissue Proteinases (Barrett, A.J. & Dingle, J.T., eds.), North-Holland, Amsterdam, pp. 69–107.

    Google Scholar 

  31. Barrett, A.J. (1975) in Proteases and Biological Control (Reich, E., Rifkin, D.B. & Shaw, E., eds.), Cold Spring Harbor Laboratory, New York, pp. 476–477.

    Google Scholar 

  32. McDonald, J.K., Callahan, P.X. & Ellis, S. (1972) Meths. Enzymol. 25, 272–281.

    Article  CAS  Google Scholar 

  33. McDonald, J.K. & Schwabe, C. (1977) in Proteinases in Mammalian Cells and Tissues (Barrett, A.J., ed.), North-Holland, Amsterdam, pp. 311–391.

    Google Scholar 

  34. Barrett, A.J. & Heath, M.F. (1977) in Lysosomes: A Laboratory Handbook, 2nd edn. (Dingle, J.T., ed.), Elsevier/North-Holland, Amsterdam, pp. 19–145.

    Google Scholar 

  35. Dolbeare, F.A. & Smith, R.E. (1977) Clin. Chem. 23, 1485–1491.

    PubMed  CAS  Google Scholar 

  36. McDonald, J.K. & Schwabe, C. (1980) Biochim. Biophys. Acta 616, 68–81.

    PubMed  CAS  Google Scholar 

  37. Green, G.D. & Shaw, E. (1981) J. Biol. Chem. 256, 1923–1928.

    PubMed  CAS  Google Scholar 

  38. McDonald, J.K. & Schwabe, C. (1982) Ann. N.Y. Acad. Sci. 380, 178–186.

    Article  PubMed  CAS  Google Scholar 

  39. Stauber, W.T. & Ong, S-H. (1982) J. Histochem. Cytochem. 30, 162–164.

    Article  PubMed  CAS  Google Scholar 

  40. Timpl, R. (1982) Meths. Enzymol. 82, 472–498.

    Article  CAS  Google Scholar 

  41. McDonald, J.K., Leibach, F.H., Grindeland, R.E. & Ellis, S. (1968) J. Biol. Chem. 243, 4143–4150.

    PubMed  CAS  Google Scholar 

  42. Eisenhauer, D.A. & McDonald, J.K. (1986) J. Biol. Chem. 262, 8859–8865.

    Google Scholar 

  43. Fukasawa, K., Fukasawa, K.M., Hiraoka, B.Y. & Harada, M. (1983) Biochim. Biophys. Acta 745, 6–11.

    Article  PubMed  CAS  Google Scholar 

  44. Nachlas, M.M., Monis, B., Rosenblatt. D. & Seligman, A.M. (1960) J. Biophys. Biochem. Cytol. 7, 261–264.

    Article  PubMed  CAS  Google Scholar 

  45. Barrett, A.J. (1973) Biochem. J. 131, 809–822.

    PubMed  CAS  Google Scholar 

  46. Smith, R.E. & Van Frank, R.M. (1975) in Lysosomes in Biology and Pathology (Dingle, J.T. & Dean, R.T., eds.), North-Holland, Amsterdam, pp. 193–249.

    Google Scholar 

  47. Hartree, E.F. (1975) J. Reprod. Fert. 44, 125–126.

    Article  CAS  Google Scholar 

  48. Sannes, P.L., Schofield, B.H. & McDonald, J.K. (1986) J. Histochem. Cytochem. 34, 983–988.

    Article  PubMed  CAS  Google Scholar 

  49. Sannes, P.L., McDonald, J.K. & Spicer, S.S. (1977) Lab. Invest. 37, 243–253.

    Article  PubMed  CAS  Google Scholar 

  50. Sannes, P.L. (1983) J. Histochem. Cytochem. 31, 684–690.

    Article  PubMed  CAS  Google Scholar 

  51. Doebber, T.W., Divor, A.R. & Ellis, S. (1978) Endocrinology 103, 1794–1804.

    Article  PubMed  CAS  Google Scholar 

  52. Curry, T.E., Jr., Dean, D.D., Woessner, J.F. Jr. & LeMaire, W.J. (1985) Biol. Reprod. 33, 981–991.

    Article  PubMed  CAS  Google Scholar 

  53. McDonald, J.K., Hoisington, A.R. & Eisenhauer, D.A. (1985) Biochem. Biophys. Res. Comm. 126, 63–71.

    Article  PubMed  CAS  Google Scholar 

  54. Ehrenreich, B.A. & Cohn, Z.A. (1969) J. Exp. Med. 129, 227–243.

    Article  PubMed  CAS  Google Scholar 

  55. Welgus, H.G., Grant, G.A., Sacchettini, J.C., Roswit, W.T. & Jeffrey, J.J. (1985) J. Biol. Chem. 260, 13601–13606.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1987 Plenum Press, New York

About this chapter

Cite this chapter

McDonald, J.K., Schwabe, C., Owers, N.O. (1987). Peptidases in Connective Tissue Degradation and Remodelling in Reproductive and Invasive Tissues. In: Reid, E., Cook, G.M.W., Luzio, J.P. (eds) Cells, Membranes, and Disease, Including Renal. Methodological Surveys in Biochemistry and Analysis, vol 17. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1283-3_35

Download citation

  • DOI: https://doi.org/10.1007/978-1-4684-1283-3_35

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-1285-7

  • Online ISBN: 978-1-4684-1283-3

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics