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

URLURL - Predstavitvena datoteka, za dostop obiščite http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0053918 Povezava se odpre v novem oknu

Izvleček
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

Jezik:Angleški jezik
Ključne besede:katepsin X, tumorji, profilin 1, rak prostate, celice raka
Vrsta gradiva:Delo ni kategorizirano (r6)
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:FFA - Fakulteta za farmacijo
Leto izida:2013
Št. strani:str. 1-9, e53918
Številčenje:Vol. 8, iss. 1
UDK:616.64-006-08
ISSN pri članku:1932-6203
DOI:10.1371/journal.pone.0053918 Povezava se odpre v novem oknu
COBISS.SI-ID:3375217 Povezava se odpre v novem oknu
Število ogledov:596
Število prenosov:145
Metapodatki:XML RDF-CHPDL DC-XML DC-RDF
 
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Naslov:PloS one
Založnik:Public Library of Science
COBISS.SI-ID:2005896 Povezava se odpre v novem oknu

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