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The role of human alkyladenine glycosylase in cellular resistance to the chloroethylnitrosoureas

dc.contributor.authorLi, Qiong
dc.contributor.authorWright, Steven E.
dc.contributor.authorMatijasevic, Zdenka
dc.contributor.authorChong, Wincha
dc.contributor.authorLudlum, David B.
dc.contributor.authorVolkert, Michael R.
dc.date2022-08-11T08:09:52.000
dc.date.accessioned2022-08-23T16:47:07Z
dc.date.available2022-08-23T16:47:07Z
dc.date.issued2003-03-29
dc.date.submitted2008-06-18
dc.identifier.citationCarcinogenesis. 2003 Mar;24(3):589-93.
dc.identifier.issn0143-3334 (Print)
dc.identifier.pmid12663522
dc.identifier.urihttp://hdl.handle.net/20.500.14038/41014
dc.description.abstractTo investigate the possible role of glycosylase action in causing tumor resistance, a full-length, histidine-tagged human alkyladenine glycosylase has been purified from the cloned human gene contained in a pTrc99A vector propagated in a tag alkA mutant Escherichia coli. This human enzyme releases both 3-methyladenine and 7-methylguanine from methylated DNA but in contrast to previous studies of the bacterial AlkA glycosylase, it does not release any adducts from [(3)H]chloroethylnitrosourea-modified DNA. This finding suggests that the alkyladenine DNA glycosylase-dependent resistance to the toxic effects of the chloroethylnitrosoureas reported previously in the literature may occur by a mechanism other than through direct glycosylase action.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12663522&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1093/carcin/24.3.589
dc.subjectBase Sequence
dc.subject*DNA Glycosylases
dc.subjectDNA Primers
dc.subjectHumans
dc.subjectN-Glycosyl Hydrolases
dc.subjectNitrosourea Compounds
dc.subjectSubstrate Specificity
dc.subjectCancer Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleThe role of human alkyladenine glycosylase in cellular resistance to the chloroethylnitrosoureas
dc.typeJournal Article
dc.source.journaltitleCarcinogenesis
dc.source.volume24
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/381
dc.identifier.contextkey533093
html.description.abstract<p>To investigate the possible role of glycosylase action in causing tumor resistance, a full-length, histidine-tagged human alkyladenine glycosylase has been purified from the cloned human gene contained in a pTrc99A vector propagated in a tag alkA mutant Escherichia coli. This human enzyme releases both 3-methyladenine and 7-methylguanine from methylated DNA but in contrast to previous studies of the bacterial AlkA glycosylase, it does not release any adducts from [(3)H]chloroethylnitrosourea-modified DNA. This finding suggests that the alkyladenine DNA glycosylase-dependent resistance to the toxic effects of the chloroethylnitrosoureas reported previously in the literature may occur by a mechanism other than through direct glycosylase action.</p>
dc.identifier.submissionpathoapubs/381
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages589-93


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