Nitrosated glycine derivatives as a potential source of O6-methylguanine in DNA.
dc.contributor.author | Shuker, D E | |
dc.contributor.author | Margison, Geoffrey P | |
dc.date.accessioned | 2010-03-29T15:09:58Z | |
dc.date.available | 2010-03-29T15:09:58Z | |
dc.date.issued | 1997-02-01 | |
dc.identifier.citation | Nitrosated glycine derivatives as a potential source of O6-methylguanine in DNA. 1997, 57 (3):366-9 Cancer Res. | en |
dc.identifier.issn | 0008-5472 | |
dc.identifier.pmid | 9012456 | |
dc.identifier.uri | http://hdl.handle.net/10541/95196 | |
dc.description.abstract | The nitrosated bile acid conjugate N-nitrosoglycocholic acid reacts with DNA to give, rise to several adducts including O6-carboxymethylguanine and, unexpectedly, O6-methylguanine (O6-MG). O6-MG is well established as a toxic and promutagenic lesion and is a substrate for the DNA repair protein O6-alkylguanine-DNA-alkyltransferase. In contrast, O6-carboxymethylguanine is not repaired by this protein. Similar results have been obtained for other nitrosated glycine derivatives, which suggests that O6-MG, which has been observed in DNA from human gastrointestinal tissues, may be derived from intragastric nitrosation of glycine or related compounds. | |
dc.language.iso | en | en |
dc.subject.mesh | DNA | |
dc.subject.mesh | Glycine | |
dc.subject.mesh | Guanine | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Nitrosamines | |
dc.title | Nitrosated glycine derivatives as a potential source of O6-methylguanine in DNA. | en |
dc.type | Article | en |
dc.contributor.department | MRC Toxicology Unit, Hodgkin Building, University of Leicester, United Kingdom. | en |
dc.identifier.journal | Cancer Research | en |
html.description.abstract | The nitrosated bile acid conjugate N-nitrosoglycocholic acid reacts with DNA to give, rise to several adducts including O6-carboxymethylguanine and, unexpectedly, O6-methylguanine (O6-MG). O6-MG is well established as a toxic and promutagenic lesion and is a substrate for the DNA repair protein O6-alkylguanine-DNA-alkyltransferase. In contrast, O6-carboxymethylguanine is not repaired by this protein. Similar results have been obtained for other nitrosated glycine derivatives, which suggests that O6-MG, which has been observed in DNA from human gastrointestinal tissues, may be derived from intragastric nitrosation of glycine or related compounds. |