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Article: ATP modulates poly(ADP-ribose) polymerase-1-facilitated topoisomerase I-linked DNA religation in the presence of camptothecin

TitleATP modulates poly(ADP-ribose) polymerase-1-facilitated topoisomerase I-linked DNA religation in the presence of camptothecin
Authors
Issue Date2008
PublisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.molpharm.org
Citation
Molecular Pharmacology, 2008, v. 73 n. 6, p. 1829-1837 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/69788
ISSN
2014 Impact Factor: 4.128
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPark, SYen_HK
dc.contributor.authorLeung, CHen_HK
dc.contributor.authorCheng, YCen_HK
dc.date.accessioned2010-09-06T06:16:51Z-
dc.date.available2010-09-06T06:16:51Z-
dc.date.issued2008en_HK
dc.identifier.citationMolecular Pharmacology, 2008, v. 73 n. 6, p. 1829-1837en_HK
dc.identifier.issn0026-895Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/69788-
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.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.molpharm.orgen_HK
dc.relation.ispartofMolecular Pharmacologyen_HK
dc.titleATP modulates poly(ADP-ribose) polymerase-1-facilitated topoisomerase I-linked DNA religation in the presence of camptothecinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0026-895X&volume=&spage=1829&epage=1837&date=2008&atitle=ATP+Modulates+Poly(ADP-Ribose)+Polymerase-1-Facilitated+Topoisomerase+I-Linked+DNA+Religation+in+the+Presence+of+Camptothecin+en_HK
dc.identifier.emailLeung, CH:duncanl@hkucc.hku.hken_HK
dc.identifier.authorityLeung, CH=rp00730en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1124/mol.107.044438en_HK
dc.identifier.pmid18349103en_HK
dc.identifier.scopuseid_2-s2.0-44249121712en_HK
dc.identifier.hkuros143573en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-44249121712&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume73en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1829en_HK
dc.identifier.epage1837en_HK
dc.identifier.isiWOS:000255982500024-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridPark, SY=13404645500en_HK
dc.identifier.scopusauthoridLeung, CH=7402612570en_HK
dc.identifier.scopusauthoridCheng, YC=36041844200en_HK
dc.identifier.citeulike2941208-

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