Literature DB >> 9925755

Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein.

E Winstall1, E B Affar, R Shah, S Bourassa, A I Scovassi, G G Poirier.   

Abstract

Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins. Purification of PARG from many tissues revealed heterogeneity in activity and structure of this enzyme. To investigate PARG structure and localization, we developed a highly sensitive one-dimensional zymogram allowing us to analyze PARG activity in crude extracts of Cos-7, Jurkat, HL-60, and Molt-3 cells. In all extracts, a single PARG activity band corresponding to a protein of about 110 kDa was detected. This 110-kDa PARG activity was found mainly in cytoplasmic rather than in nuclear extracts of Cos-7 cells. Copyright 1999 Academic Press.

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Year:  1999        PMID： 9925755     DOI： 10.1006/excr.1998.4321

Source DB:  PubMed          Journal:  Exp Cell Res        ISSN： 0014-4827            Impact factor:   3.905


  13 in total

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Authors:  Amos A Fatokun; Valina L Dawson; Ted M Dawson
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2.  Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles.

Authors:  Jean-Philippe Gagné; Marie-Eve Bonicalzi; Pierre Gagné; Marie-Eve Ouellet; Michael J Hendzel; Guy G Poirier
Journal:  Biochem J       Date:  2005-12-15       Impact factor: 3.857

3.  Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death.

Authors:  Seong-Woon Yu; Shaida A Andrabi; Hongmin Wang; No Soo Kim; Guy G Poirier; Ted M Dawson; Valina L Dawson
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-20       Impact factor: 11.205

4.  Poly(ADP-ribose) (PAR) polymer is a death signal.

Authors:  Shaida A Andrabi; No Soo Kim; Seong-Woon Yu; Hongmin Wang; David W Koh; Masayuki Sasaki; Judith A Klaus; Takashi Otsuka; Zhizheng Zhang; Raymond C Koehler; Patricia D Hurn; Guy G Poirier; Valina L Dawson; Ted M Dawson
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-20       Impact factor: 11.205

5.  The macro domain is an ADP-ribose binding module.

Authors:  Georgios I Karras; Georg Kustatscher; Heeran R Buhecha; Mark D Allen; Céline Pugieux; Fiona Sait; Mark Bycroft; Andreas G Ladurner
Journal:  EMBO J       Date:  2005-05-19       Impact factor: 11.598

Review 6.  Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions.

Authors:  D D'Amours; S Desnoyers; I D'Silva; G G Poirier
Journal:  Biochem J       Date:  1999-09-01       Impact factor: 3.857

7.  Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death.

Authors:  W Ying; M B Sevigny; Y Chen; R A Swanson
Journal:  Proc Natl Acad Sci U S A       Date:  2001-10-09       Impact factor: 11.205

Review 8.  Structure and function of the ARH family of ADP-ribosyl-acceptor hydrolases.

Authors:  Masato Mashimo; Jiro Kato; Joel Moss
Journal:  DNA Repair (Amst)       Date:  2014-04-18

9.  Poly(ADPR) polymerase-1 and poly(ADPR) glycohydrolase level and distribution in differentiating rat germinal cells.

Authors:  Silvia Di Meglio; Marco Denegri; Salvatore Vallefuoco; Filomena Tramontano; A Ivana Scovassi; Piera Quesada
Journal:  Mol Cell Biochem       Date:  2003-06       Impact factor: 3.396

10.  Depletion of the 110-kilodalton isoform of poly(ADP-ribose) glycohydrolase increases sensitivity to genotoxic and endotoxic stress in mice.

Authors:  Ulrich Cortes; Wei-Min Tong; Donna L Coyle; Mirella L Meyer-Ficca; Ralph G Meyer; Virginie Petrilli; Zdenko Herceg; Elaine L Jacobson; Myron K Jacobson; Zhao-Qi Wang
Journal:  Mol Cell Biol       Date:  2004-08       Impact factor: 4.272
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