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  • Laurent-Matha, Valerie (author)

Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment

  • Article/chapterEnglish2012

Publisher, publication year, extent ...

  • 2012-08-16
  • Wiley,2012

Numbers

  • LIBRIS-ID:oai:lup.lub.lu.se:63e52ee3-6350-4e67-a2f7-66231c4c491e
  • https://lup.lub.lu.se/record/3372683URI
  • https://doi.org/10.1096/fj.12-205229DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • The aspartic protease cathepsin D, a poor prognostic indicator of breast cancer, is abundantly secreted as procathepsin D by human breast cancer cells and self-activates at low pH in vitro, giving rise to catalytically active cathepsin D. Due to a lower extracellular pH in tumor microenvironments compared to normal tissues, cathepsin D may cleave pathophysiological substrates contributing to cancer progression. Here, we show by yeast 2-hybrid and degradomics analyses that cystatin C, the most potent natural secreted inhibitor of cysteine cathepsins, both binds to and is a substrate of extracellular procathepsin D. The amount of cystatin C in the extracellular environment is reduced in the secretome of mouse embryonic fibroblasts stably transfected with human cathepsin D. Cathepsin D extensively cleaved cystatin C in vitro at low pH. Cathepsin D secreted by breast cancer cells also processed cystatin C at the pericellular pH of tumors and so enhancing extracellular proteolytic activity of cysteine cathepsins. Thus, tumor derived cathepsin D assists breast cancer progression by reducing cystatin C activity, which, in turn, enhances cysteine cathepsin proteolytic activity, revealing a new link between protease classes in the protease web.-Laurent-Matha, V., Huesgen, P. F., Masson, O., Derocq, D., Prebois, C., Gary-Bobo, M., Lecaille, F., Rebiere, B., Meurice, G., Orear, C., Hollingsworth, R. E., Abrahamson, M., Lalmanach, G., Overall, C. M., Liaudet-Coopman, E. Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment. FASEB J. 26, 5172-5181 (2012). www.fasebj.org

Subject headings and genre

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  • Huesgen, Pitter F. (author)
  • Masson, Olivier (author)
  • Derocq, Danielle (author)
  • Prebois, Christine (author)
  • Gary-Bobo, Magali (author)
  • Lecaille, Fabien (author)
  • Rebiere, Bertrand (author)
  • Meurice, Guillaume (author)
  • Orear, Cedric (author)
  • Hollingsworth, Robert E. (author)
  • Abrahamson, MagnusLund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Proteasinhibitorforskning,Forskargrupper vid Lunds universitet,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine,Protease Inhibitor Research,Lund University Research Groups(Swepub:lu)kkem-mab (author)
  • Lalmanach, Gilles (author)
  • Overall, Christopher M. (author)
  • Liaudet-Coopman, Emmanuelle (author)
  • Avdelningen för klinisk kemi och farmakologiInstitutionen för laboratoriemedicin (creator_code:org_t)

Related titles

  • In:FASEB Journal: Wiley26:12, s. 5172-51811530-68600892-6638

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