alexa (PARP)-1 N-Terminal Fragment Down Regulates Endogenous PARP-1 Expression and Activity and Sensitises Cells to Oxidative Stress | OMICS International | Abstract
ISSN: 2157-7013

Journal of Cell Science & Therapy
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Research Article

(PARP)-1 N-Terminal Fragment Down Regulates Endogenous PARP-1 Expression and Activity and Sensitises Cells to Oxidative Stress

Ida Rachel Rajiah*
Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK
Corresponding Author : Dr Ida Rachel Rajiah
Department of Pathology
University of Cambridge, Tennis Court Road
Cambridge CB2 1QP, UK
Tel: +44(0)1223761654
Fax: +44-(0)1223-333346
E-mail: [email protected], [email protected]
Received Febrauary 19, 2013; Accepted March 20, 2013; Published March 22, 2013
Citation: Rajiah IR (2013) (PARP)-1 N-Terminal Fragment Down Regulates Endogenous PARP-1 Expression and Activity and Sensitises Cells to Oxidative Stress. J Cell Sci Ther 4:138. doi: 10.4172/2157-7013.1000138
Copyright: © 2013 Rajiah IR, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Poly (ADP-ribose) polymerase-1 (PARP-1) is a nuclear enzyme that plays a vital role in DNA repair. This makes it an attractive anticancer therapeutic target. It is activated by DNA breaks and catalyses the synthesis of homopolymers of ADP-ribose from NAD+. Competitive inhibitors as well as the non-catalytic, DNA-binding domain of PARP-1 abolish its polymer synthesising function. Such inhibitors of PARP-1 have been used in clinical trials and are known to cause nausea, fatigue and haematological events and with chronic use the risk of drug-induced DNA damage and tumorigenesis. In this study, I have investigated the effect of PARP-1-N-terminal fragment on endogenous PARP-1 activity and expression in mammalian cells. To elicit DNA damage response, different concentrations of H2O2 were used. For visualisation of the effects by live imaging, 750 bp PARP-1-N-terminal fragment was tagged to EGFPN1 vector. My data shows an inverse correlation between the expression of this fragment and poly (ADP-ribose) synthesis at lower concentrations of H2O2 and induction of apoptosis at higher concentrations. My experimental evidence also supports regulation of endogenous PARP-1 expression by the fragment in the absence of DNA damage. This construct has allowed for the visualisation of its functional ability to sensitise cells to oxidative damage and induce apoptosis as observed by the formation of apoptotic precursors and caspase cleavage products in live cells. The data also provides direct evidence for its therapeutic potential in chemotherapy or radiotherapy to avert necrosis induced inflammatory response.

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