Search: onr:"swepub:oai:lup.lub.lu.se:63e52ee3-6350-4e67-a2f7-66231c4c491e" >
Proteolysis of cyst...
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Laurent-Matha, Valerie
(author)
Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment
- Article/chapterEnglish2012
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LIBRIS-ID:oai:lup.lub.lu.se:63e52ee3-6350-4e67-a2f7-66231c4c491e
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https://lup.lub.lu.se/record/3372683URI
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https://doi.org/10.1096/fj.12-205229DOI
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Language:English
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Summary in:English
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Subject category:art swepub-publicationtype
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Subject category:ref swepub-contenttype
Notes
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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
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Huesgen, Pitter F.
(author)
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Masson, Olivier
(author)
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Derocq, Danielle
(author)
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Prebois, Christine
(author)
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Gary-Bobo, Magali
(author)
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Lecaille, Fabien
(author)
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Rebiere, Bertrand
(author)
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Meurice, Guillaume
(author)
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Orear, Cedric
(author)
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Hollingsworth, Robert E.
(author)
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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)
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Lalmanach, Gilles
(author)
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Overall, Christopher M.
(author)
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Liaudet-Coopman, Emmanuelle
(author)
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Avdelningen för klinisk kemi och farmakologiInstitutionen för laboratoriemedicin
(creator_code:org_t)
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In:FASEB Journal: Wiley26:12, s. 5172-51811530-68600892-6638
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Laurent-Matha, V ...
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Huesgen, Pitter ...
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Masson, Olivier
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Derocq, Danielle
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Prebois, Christi ...
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Gary-Bobo, Magal ...
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Lecaille, Fabien
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Rebiere, Bertran ...
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Meurice, Guillau ...
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Orear, Cedric
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Hollingsworth, R ...
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Abrahamson, Magn ...
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Lalmanach, Gille ...
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Overall, Christo ...
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Liaudet-Coopman, ...
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FASEB Journal
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Lund University