The presence of a truncated base excision repair pathway in human spermatozoa that is mediated by OGG1

DNA repair has long been considered impossible in human spermatozoa due to the high level of DNA compaction observed in these cells. However, detailed examination of the base excision repair pathway in human spermatozoa has revealed the presence of an enzyme critical to this pathway, 8-oxoguanine DN...

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Veröffentlicht in:Journal of cell science 2013-03, Vol.126 (Pt 6), p.1488-1497
Hauptverfasser: Smith, Tegan B, Dun, Matthew D, Smith, Nathan D, Curry, Ben J, Connaughton, Haley S, Aitken, Robert J
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Sprache:eng
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Zusammenfassung:DNA repair has long been considered impossible in human spermatozoa due to the high level of DNA compaction observed in these cells. However, detailed examination of the base excision repair pathway in human spermatozoa has revealed the presence of an enzyme critical to this pathway, 8-oxoguanine DNA glycosylase 1 (OGG1). This glycosylase was associated with the sperm nucleus and mitochondria and could actively excise 8-hydroxy-2'-deoxyguanosine (8OHdG), releasing this adduct into the extracellular space. This activity was significantly reduced in the presence of cadmium (II), a recognized inhibitor of OGG1, in a time- and dose-dependent manner (P
ISSN:1477-9137
DOI:10.1242/jcs.121657