Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Cathepsin-D

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_891-2

Definition

Cathepsin-D (E.C. 3.4.23.5) is a ubiquitous lysosomal aspartic endo-proteinase cleaving preferentially -Phe-Phe-, -Leu-Tyr-, -Tyr-Leu-, and -Phe-Tyr- bonds in peptide chains containing at least five amino acids at an acidic pH.

Characteristics

Cathepsin-D is ubiquitously distributed in lysosomes. It was considered for a long time that the main function of cathepsin-D was to degrade proteins in lysosomes at an acidic pH. Apart from its function in general protein turnover, cathepsin-D can also activate precursors of biologically active proteins in pre-lysosomal compartments of specialized cells. Knock-outof cathepsin-D gene induces death shortly after birth with severe apoptotic and necrotic phenotypes. Its pH optimum depends on the enzyme source and on the substrate used for the determination of the activity and ranges between 2.8 and 5. No endogenous cathepsin-D tissue inhibitor is known in mammals. Pepstatin, a natural inhibitor of aspartic proteases isolated from...

Keywords

Human Immunodeficiency Virus Protease Estrogen Receptor Positive Breast Cancer Negative Breast Cancer Cell Line Estrogen Receptor Negative Breast Cancer Receptor Positive Breast Cancer Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access

References

  1. Chwieralski CE, Welte T, Buhling F (2006) Cathepsin-regulated apoptosis. Apoptosis 11:143–149CrossRefPubMedGoogle Scholar
  2. Liaudet-Coopman E, Beaujouin M, Derocq D et al (2006) Cathepsin D: newly discovered functions of a long-standing aspartic protease in cancer and apoptosis. Cancer Lett 237:167–179CrossRefPubMedGoogle Scholar
  3. Rochefort H (1992) Cathepsin D in breast cancer: a tissue marker associated with metastasis. Eur J Cancer 28A:1780–1783CrossRefPubMedGoogle Scholar
  4. Westley BR, May FE (1999) Prognostic value of cathepsin D in breast cancer. Br J Cancer 79:189–190CrossRefPubMedPubMedCentralGoogle Scholar

See Also

  1. (2012) Epithelial cell. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, pp 1291–1292. doi:10.1007/978-3-642-16483-5_1958Google Scholar
  2. (2012) Estrogens. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1333. doi:10.1007/978-3-642-16483-5_2019Google Scholar
  3. (2012) Knock-out. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1957. doi:10.1007/978-3-642-16483-5_3237Google Scholar
  4. (2012) Lysosome. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 2128. doi:10.1007/978-3-642-16483-5_3472Google Scholar
  5. (2012) Promoter. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 3004. doi:10.1007/978-3-642-16483-5_4768Google Scholar
  6. (2012) Proteinase. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 3092. doi:10.1007/978-3-642-16483-5_4805Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.IRCM, INSERM, UMICRLC Val d’AurelleMontpellierFrance