Oncotarget

Reviews:

Poly(adenosine diphosphate-ribose) polymerase as therapeutic target: lessons learned from its inhibitors

Anna Mária Cseh _, Zsolt Fábián, Balázs Sümegi and Luca Scorrano

PDF  |  HTML  |  Supplementary Files  |  How to cite  |  Order a Reprint

Oncotarget. 2017; 8:50221-50239. https://doi.org/10.18632/oncotarget.16859

Metrics: PDF 1328 views  |   HTML 2082 views  |   ?  


Abstract

Anna Mária Cseh1,2, Zsolt Fábián3, Balázs Sümegi1 and Luca Scorrano2

1Department of Biochemistry and Medical Chemistry, University of Pécs Medical School, Pécs, Hungary

2Department of Biology, University of Padova, Padova, Italy

3Conway Institute, University College Dublin, Belfield, Dublin, Ireland

Correspondence to:

Anna Mária Cseh, email: anna.cseh@aok.pte.hu

Keywords: PARP, mitochondria, cancer, signaling, targeted therapy

Received: February 10, 2017     Accepted: March 28, 2017     Published: April 05, 2017

ABSTRACT

Poly(ADP-ribose) polymerases are a family of DNA-dependent nuclear enzymes catalyzing the transfer of ADP-ribose moieties from cellular nicotinamide-adenine-dinucleotide to a variety of target proteins. Although they have been considered as resident nuclear elements of the DNA repair machinery, recent works revealed a more intricate physiologic role of poly(ADP-ribose) polymerases with numerous extranuclear activities. Indeed, poly(ADP-ribose) polymerases participate in fundamental cellular processes like chromatin remodelling, transcription or regulation of the cell-cycle. These new insight into the physiologic roles of poly(ADP-ribose) polymerases widens the range of human pathologies in which pharmacologic inhibition of these enzymes might have a therapeutic potential. Here, we overview our current knowledge on extranuclear functions of poly(ADP-ribose) polymerases with a particular focus on the mitochondrial ones and discuss potential fields of future clinical applications.


Creative Commons License All site content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 License.
PII: 16859