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Profilin 1 as a target for cathepsin X activity in tumor cells
Pečar Fonović, Urša (Author), Jevnikar, Zala (Author), Rojnik, Matija (Author), Doljak, Bojan (Author), Fonović, Marko (Author), Jamnik, Polona (Author), Kos, Janko (Author)

URLURL - Presentation file, Visit http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0053918 This link opens in a new window

Abstract
Cathepsin X has been reported to be a tumor promotion factor in various types of cancer; however, the molecular mechanisms linking its activity with malignant processes are not understood. Here we present profilin 1, a known tumor suppressor, as a target for cathepsin X carboxypeptidase activity in prostate cancer PC-3 cells. Profilin 1 co-localizes strongly with cathepsin X intracellularly in the perinuclear area as well as at the plasma membrane. Selective cleavage of C-terminal amino acids was demonstrated on a synthetic octapeptide representing the profilin C-terminal region, and on recombinant profilin 1. Further, intact profilin 1 binds its poly-L-proline ligand clathrin significantly better than it does the truncated one, as shown using cathepsin X specific inhibitor AMS-36 and immunoprecipitation of the profilin 1/clathrin complex. Moreover, the polymerization of actin, which depends also on the binding of poly-L-proline ligands to profilin 1, was promoted by AMS-36 treatment of cells and by siRNA cathepsin X silencing. Our results demonstrate that increased adhesion, migration and invasiveness of tumor cells depend on the inactivation of the tumor suppressive function of profilin 1 by cathepsin X. The latter is thus designated as a target for development of new antitumor strategies

Language:English
Keywords:katepsin X, tumorji, profilin 1, rak prostate, celice raka
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Year:2013
Number of pages:str. 1-9, e53918
Numbering:Vol. 8, iss. 1
UDC:616.64-006-08
ISSN on article:1932-6203
DOI:10.1371/journal.pone.0053918 Link is opened in a new window
COBISS.SI-ID:3375217 Link is opened in a new window
Views:615
Downloads:152
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Record is a part of a journal

Title:PloS one
Publisher:Public Library of Science
ISSN:1932-6203
COBISS.SI-ID:2005896 This link opens in a new window

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