Skip to main content
SpringerLink
Log in

Conformation and processing of cathepsin D

  • Published:
Bioscience Reports

Abstract

Cathepsin D occurs in two forms, a single polypeptide chain (Mr 44000) and a non-covalent complex of two peptides of Mr 14000 and 30000 that is derived by proteolytic processing of the 44000 polypeptide. The two forms from bovine spleen are closely similar in secondary structure content, in aromatic amino acid environment and in the two step denaturation behaviour. Enzyme activity is lost irreversibly on denaturation but conformation can be partially regained. The two separated chains will only refold partially and this is related to their positions in the overall structure of cathepsin D. It is suggested that the processing step is related to protein turnover.

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

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Andreeva NA & Gustchina AE (1979) Biochem. Biophys. Res. Commun.87, 32–42.

    PubMed  Google Scholar 

  • Barrett AJ (1979) Adv. Exp. Med. Biol.95, 291–300.

    Google Scholar 

  • Barrett AJ & McDonald JK (1980)Mammalian Proteases: A Glossary and Bibliography, vol. 1, pp 338–350, Academic Press, London.

    Google Scholar 

  • Blundell TL, Sewell BT & McLachlan A (1979) Biochim. Biophys. Acta580, 24–31.

    PubMed  Google Scholar 

  • Erickson AH & Blobel G (1979) J. Biol. Chem.254, 11771–11774.

    PubMed  Google Scholar 

  • Erickson AH, Conner GE & Blobel G (1981) J. Biol. Chem.256, 11224–11231.

    PubMed  Google Scholar 

  • James MNG, Sielecki A, Salituro F, Rich DH & Hofmann T (1982) Proc. Natl. Acad. Sci. U.S.A.79, 6137–6141.

    PubMed  Google Scholar 

  • Keilova H & Tomasek V (1976) in:Intracecullar Protein Catabolism (Hanson H & Bohley P, eds), pp 237–251, J. A. Barth, Leipzig.

    Google Scholar 

  • Kregar I, Urh I, Umezawa H & Turk V (1977) Croat. Chem. Acta49, 587–592.

    Google Scholar 

  • Laemmli UK (1970) Nature (London)227 680–685.

    Google Scholar 

  • Lah T & Turk V (1982) Hoppe-Seyler's Z. Physiol. Chem.363, 247–254.

    PubMed  Google Scholar 

  • Lah T, Turk V & Pain RH (1980) Vestn. Slov. Kem. Drus.27, 237–250.

    Google Scholar 

  • Lah T, Drobnic-Kosorok M, Turk V & Pain RH (1984) Biochem. J.218, 601–608.

    PubMed  Google Scholar 

  • Misono KS, Chang J-J & Inagami T (1982) Proc. Natl. Acad. Sci. U.S.A.79, 4863–4867.

    PubMed  Google Scholar 

  • Ogunro EA, Ferguson AG & Losch M (1980) Cardiovasc. Res.14, 254–260.

    PubMed  Google Scholar 

  • Pain RH, Lah T & Turk V (1985) Trans. Biochem. Soc. (in press).

  • Panthier JJ, Fook S, Chambraud B, Strosberg AD, Corvol P & Rougeon F (1982) Nature (London)298, 90–92.

    Google Scholar 

  • Press EM, Porter RR & Cebra J (1960) Biochem. J.74, 509–513.

    Google Scholar 

  • Privalov PL, Mateo PL, Khechinashvilli NN, Stepanov VM & Revina LP (1981) J. Mol. Biol.152, 445–464.

    PubMed  Google Scholar 

  • Puizdar V & Turk V (1981) FEBS Lett.132, 299–304.

    PubMed  Google Scholar 

  • Shewale JG & Tang J (1984) Proc. Natl. Acad. Sci. U.S.A.81, 3703–3707.

    PubMed  Google Scholar 

  • Takahashi T & Tang J (1981) Methods Enzymol.80, 565–581.

    PubMed  Google Scholar 

  • Turk V, Lah T, Puizdar V, Kregar I & Pain RH (1981) Acta Med. Ger.40, 1439–1450.

    Google Scholar 

  • Whitaker JN (1981) Comp. Biochem. Physiol. B68, 215–220.

    Google Scholar 

  • Yamamoto K, Katsuda N, Himeno M & Kato K (1979) Eur. J. Biochem.95, 459–467.

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, University of Newcastle upon Tyne, NE1 7RU, UK

    Roger H. Pain

  2. Department of Biochemistry, Jozef Stefan Institute and Faculty of Chemistry, E. Kardelj University, Ljubljana, Yugoslavia

    Tamara Lan & Vito Turk

Authors
  1. Roger H. Pain
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Tamara Lan
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Vito Turk
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Pain, R.H., Lan, T. & Turk, V. Conformation and processing of cathepsin D. Biosci Rep 5, 957–967 (1985). https://doi.org/10.1007/BF01119908

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01119908

Keywords

Search

Navigation