HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease.

JC Huang, DB Zamble, JT Reardon… - Proceedings of the …, 1994 - National Acad Sciences
JC Huang, DB Zamble, JT Reardon, SJ Lippard, A Sancar
Proceedings of the National Academy of Sciences, 1994National Acad Sciences
The most frequent DNA adduct made by the anticancer drug cisplatin, the 1, 2-intrastrand d
(GpG) cross-link, as well as the minor 1, 3-intrastrand d (GpTpG) adduct, were both repaired
by an in vitro human excision repair system. Fragments of 27-29 nt containing the platinum
damage were excised. The high mobility group (HMG)-domain proteins HMG1 and human
mitochondrial transcription factor specifically inhibited repair of the 1, 2-intrastrand cross-link
by the human excision nuclease. These results suggest that the types and levels of HMG …
The most frequent DNA adduct made by the anticancer drug cisplatin, the 1,2-intrastrand d(GpG) cross-link, as well as the minor 1,3-intrastrand d(GpTpG) adduct, were both repaired by an in vitro human excision repair system. Fragments of 27-29 nt containing the platinum damage were excised. The high mobility group (HMG)-domain proteins HMG1 and human mitochondrial transcription factor specifically inhibited repair of the 1,2-intrastrand cross-link by the human excision nuclease. These results suggest that the types and levels of HMG-domain proteins in a given tumor may influence the responsiveness of that cancer to cisplatin chemotherapy and they provide a rational basis for the synthesis of new platinum anticancer drug candidates.
National Acad Sciences