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Article: ATP modulates poly(ADP-ribose) polymerase-1-facilitated topoisomerase I-linked DNA religation in the presence of camptothecin
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TitleATP modulates poly(ADP-ribose) polymerase-1-facilitated topoisomerase I-linked DNA religation in the presence of camptothecin
 
AuthorsPark, SY2 3
Leung, CH1 3
Cheng, YC3
 
Issue Date2008
 
PublisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.molpharm.org
 
CitationMolecular Pharmacology, 2008, v. 73 n. 6, p. 1829-1837 [How to Cite?]
DOI: http://dx.doi.org/10.1124/mol.107.044438
 
AbstractPoly(ADP-ribose) polymerase (PARP)-1 was reported to promote the religation activity of topoisomerase I in the presence of camptothecin by itself through the direct interaction with topoisomerase I or by the formation of poly(ADP-ribosyl)ated topoisomerase I. We have demonstrated previously that ATP inhibited PARP-1/NAD-facilitated religation of topoisomerase I-linked DNA (TLD) in the presence of camptothecin. The mechanism of action was further studied in the present work. ATP as well as other nucleotides, including CTP, UTP, and GTP, had no effect on topoisomerase I cleavage and religation activities in the absence of camptothecin. In the presence of camptothecin or its derivative topotecan, ATP (at up to 2 mM) inhibited PARP-1/NAD-facilitated TLD religation in a dose-dependent manner. This could be due to the suppression of topoisomerase I poly(ADP-ribosyl)ation through the competition with NAD for the binding site(s) on PARP-1. The interaction between ATP and PARP-1 was independent of ATP hydrolysis. Study of different nucleotide analogs revealed that the structure could determine the dose response of nucleotides. In addition, it was noted that higher concentrations of ATP and CTP (at 2.5 mM or higher) promoted DNA religation by a PARP-1-independent mechanism. Our study implies the possible role of ATP and other nucleotides in the regulation of topoisomerase I activity in the presence of camptothecin analogs. Copyright © 2008 The American Society for Pharmacology and Experimental Therapeutics.
 
ISSN0026-895X
2012 Impact Factor: 4.411
2012 SCImago Journal Rankings: 2.000
 
DOIhttp://dx.doi.org/10.1124/mol.107.044438
 
ISI Accession Number IDWOS:000255982500024
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorPark, SY
 
dc.contributor.authorLeung, CH
 
dc.contributor.authorCheng, YC
 
dc.date.accessioned2010-09-06T06:16:51Z
 
dc.date.available2010-09-06T06:16:51Z
 
dc.date.issued2008
 
dc.description.abstractPoly(ADP-ribose) polymerase (PARP)-1 was reported to promote the religation activity of topoisomerase I in the presence of camptothecin by itself through the direct interaction with topoisomerase I or by the formation of poly(ADP-ribosyl)ated topoisomerase I. We have demonstrated previously that ATP inhibited PARP-1/NAD-facilitated religation of topoisomerase I-linked DNA (TLD) in the presence of camptothecin. The mechanism of action was further studied in the present work. ATP as well as other nucleotides, including CTP, UTP, and GTP, had no effect on topoisomerase I cleavage and religation activities in the absence of camptothecin. In the presence of camptothecin or its derivative topotecan, ATP (at up to 2 mM) inhibited PARP-1/NAD-facilitated TLD religation in a dose-dependent manner. This could be due to the suppression of topoisomerase I poly(ADP-ribosyl)ation through the competition with NAD for the binding site(s) on PARP-1. The interaction between ATP and PARP-1 was independent of ATP hydrolysis. Study of different nucleotide analogs revealed that the structure could determine the dose response of nucleotides. In addition, it was noted that higher concentrations of ATP and CTP (at 2.5 mM or higher) promoted DNA religation by a PARP-1-independent mechanism. Our study implies the possible role of ATP and other nucleotides in the regulation of topoisomerase I activity in the presence of camptothecin analogs. Copyright © 2008 The American Society for Pharmacology and Experimental Therapeutics.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationMolecular Pharmacology, 2008, v. 73 n. 6, p. 1829-1837 [How to Cite?]
DOI: http://dx.doi.org/10.1124/mol.107.044438
 
dc.identifier.citeulike2941208
 
dc.identifier.doihttp://dx.doi.org/10.1124/mol.107.044438
 
dc.identifier.epage1837
 
dc.identifier.hkuros143573
 
dc.identifier.isiWOS:000255982500024
 
dc.identifier.issn0026-895X
2012 Impact Factor: 4.411
2012 SCImago Journal Rankings: 2.000
 
dc.identifier.issue6
 
dc.identifier.openurl
 
dc.identifier.pmid18349103
 
dc.identifier.scopuseid_2-s2.0-44249121712
 
dc.identifier.spage1829
 
dc.identifier.urihttp://hdl.handle.net/10722/69788
 
dc.identifier.volume73
 
dc.languageeng
 
dc.publisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.molpharm.org
 
dc.publisher.placeUnited States
 
dc.relation.ispartofMolecular Pharmacology
 
dc.relation.referencesReferences in Scopus
 
dc.titleATP modulates poly(ADP-ribose) polymerase-1-facilitated topoisomerase I-linked DNA religation in the presence of camptothecin
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. Korea Institute of Toxicology
  3. Yale University School of Medicine