Recognition of major DNA adducts of enantiomeric cisplatin analogs by HMG box proteins and nucleotide excision repair of these adducts
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12031669
DOI
10.1016/s1074-5521(02)00134-5
PII: S1074552102001345
Knihovny.cz E-zdroje
- MeSH
- adukty DNA metabolismus MeSH
- antitumorózní látky metabolismus farmakologie MeSH
- CHO buňky MeSH
- cisplatina analogy a deriváty metabolismus farmakologie MeSH
- HeLa buňky MeSH
- křečci praví MeSH
- krysa rodu Rattus MeSH
- lidé MeSH
- oligonukleotidové sondy chemická syntéza MeSH
- oprava DNA fyziologie MeSH
- protein HMGB1 metabolismus MeSH
- rekombinantní proteiny genetika metabolismus MeSH
- retardační test MeSH
- sekvence nukleotidů MeSH
- stereoizomerie MeSH
- substrátová specifita MeSH
- terciární struktura proteinů MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- křečci praví MeSH
- krysa rodu Rattus MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- adukty DNA MeSH
- antitumorózní látky MeSH
- cisplatin-DNA adduct MeSH Prohlížeč
- cisplatina MeSH
- oligonukleotidové sondy MeSH
- protein HMGB1 MeSH
- rekombinantní proteiny MeSH
We examined HMG domain protein recognition of major 1,2-GG intrastrand DNA crosslinks, formed by two bifunctional enantiomeric analogs of antitumor cis-diamminedichloroplatinum(II) (cisplatin), and removal of these crosslinks during in vitro nucleotide excision repair (NER) reactions. Electrophoretic mobility shift assays show that domains A and B of HMGB1 protein bind to (2R,3R)-diaminobutanedichloroplatinum(II)-generated crosslinks with a higher affinity than to those generated by (2S,3S)-diaminobutanedichloroplatinum(II). The crosslinks of both enantiomers are removed by NER with a similar efficiency; however, HMG1B protein significantly inhibits removal of the (2R,3R)-diaminobutaneplatinum(II) adduct, but not that of the (2S,3S) enantiomer. Thus, HMG domain proteins discriminate among different conformations of the 1,2-GG intrastrand crosslinks of the two enantiomeric analogs of cisplatin, which results in different NER of these crosslinks. This observation may provide insight into the mechanisms underlying antitumor activity of cisplatin and its analogs.
Citace poskytuje Crossref.org
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Mechanism of the formation of DNA-protein cross-links by antitumor cisplatin
