Journal Article

The discovery of a new family of mammalian enzymes for repair of oxidatively damaged DNA, and its physiological implications

Tapas K. Hazra, Tadahide Izumi, Y.Wah Kow and Sankar Mitra

in Carcinogenesis

Volume 24, issue 2, pages 155-157
Published in print February 2003 | ISSN: 0143-3334
Published online February 2003 | e-ISSN: 1460-2180 | DOI: http://dx.doi.org/10.1093/carcin/24.2.155
The discovery of a new family of mammalian enzymes for repair of oxidatively damaged DNA, and its physiological implications

More Like This

Show all results sharing this subject:

  • Clinical Cytogenetics and Molecular Genetics

GO

Show Summary Details

Preview

Oxidatively damaged bases in the genome are likely to be responsible for mutations leading to sporadic carcinogenesis. Two structurally similar DNA glycosylases, NTH1 and OGG1, which are able to excise most of these damaged bases, were identified previously in mammalian cells. A distinct family, consisting of two human DNA glycosylases orthologous to enzymes in Escherichia coli, has recently been characterized; they have overlapping substrate ranges with NTH1 and OGG1. The presence of multiple enzymes with potential back-up functions underscores the importance of removing both endogenously and exogenously generated oxidatively damaged bases from the genome, and may explain why no cancer or other disease phenotype has so far been linked to the deficiency of a single DNA glycosylase.

Keywords: DHU, 5,6 dihydro uracil; Fapy, formamidinopyrimidine; 5-OHC, 5-hydroxycytosine; 5-OHU, 5-hydroxyuracil; 8-oxoG, 7,8 dihydro 8-oxoguanine; ROS, reactive oxygen species; TCR, transcription-coupled repair; TG, thymine glycol.

Journal Article.  2678 words. 

Subjects: Clinical Cytogenetics and Molecular Genetics

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.