Chapter title |
Detecting and Quantifying pADPr In Vivo
|
---|---|
Chapter number | 3 |
Book title |
Poly(ADP-Ribose) Polymerase
|
Published in |
Methods in molecular biology, July 2017
|
DOI | 10.1007/978-1-4939-6993-7_3 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6992-0, 978-1-4939-6993-7
|
Authors |
Yi-Chen Lai, Rajesh K. Aneja, Margaret A. Satchell, Robert S. B. Clark |
Abstract |
Poly(ADP-ribose) polymerases (PARP) participate in diverse biological processes contributing to cellular homeostasis or exacerbating injury. PARP catalyzes the addition of ADP-ribose molecules (pADPr) to the target proteins, a process termed poly-ADP-ribosylation. Overactivation of PARP, as reflected by increased poly-ADP-ribosylation, accumulation of pADPr-modified proteins or free pADPr, contributes to depletion of NAD(+) and mitochondrial dysfunction, potentially leading to cell death. Since PARP overactivation and increases in free pADPr have been identified as key contributors to the pathobiology of many diseases, monitoring PARP-1 activation by detecting and quantifying pADPr may provide valuable mechanistic insights as well as facilitating therapeutic drug monitoring for PARP inhibitors.Several non-isotopic immunodetection methods for quantifying pADPr are discussed: western blotting of poly-ADP-ribosylated proteins, cellular localization of pADPr by immunohistochemistry, quantification of pADPr by enzyme-linked immunoassay and small scale two-dimensional gel electrophoresis. |
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