AJTR Copyright © 2009-All rights reserved. Published by e-Century Publishing Corporation, Madison, WI 53711
Am J Translational Res 2010;2(3):235-247

Review Article
Isopeptidases in anticancer therapy: looking for inhibitors

Andrea Sgorbissa, Harish Potu, Claudio Brancolini

Dipartimento di Scienze e Tecnologie Biomediche (DSTB), Università degli Studi di Udine, p.le Kolbe 4 3100
Udine ITALY.

Received April 29, 2010; accepted May 6, 2010, available online May 10, 2010

Abstract: Addition of polypeptides belonging to the ubiquitin family to selected lysines residues is a widespread
post-translation modification (PTM) that controls many fundamental aspects of cell’s life. Specific alterations in
the normal turnover of this PTM are frequently observed in tumors. The conjugation/deconjugation cycle of
ubiquitin (Ub) or ubiquitin-like (Ubl) proteins influences the activities of oncogenes and tumor suppressor genes.
Two families of enzymes work in antagonizing manner to add or remove Ub and Ubl-proteins on target proteins:
the E3 ligases and the isopeptidases. These enzymes are the subjects of fervent research with the ambition to
comprehend their regulation, their mechanisms of action, their involvement in human diseases, and to develop
specific inhibitors for therapeutic intervention. Here we will discuss of isopeptidases, the deconjugating enzymes,
with particular emphasis on the pro-apoptotic activities of the relative inhibitors identified so far. (AJTR1004006).

Key words: Apoptosis, cancer, proteasome, isopeptidase, DUBs, necrosis, caspase, proteasome, USP

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Address all correspondence to:
Claudio Brancolini, PhD
Dipartimento di Scienze e Tecnologie
Biomediche. P.le Kolbe 4 - 33100 Udine ITALY.
Tel: ++0432- 494382. Fax: ++0432- 494301
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