Recognition of major DNA adducts of enantiomeric cisplatin analogs by HMG box proteins and nucleotide excision repair of these adducts
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12031669
DOI
10.1016/s1074-5521(02)00134-5
PII: S1074552102001345
Knihovny.cz E-resources
- MeSH
- DNA Adducts metabolism MeSH
- CHO Cells MeSH
- Cisplatin analogs & derivatives metabolism pharmacology MeSH
- HeLa Cells MeSH
- Cricetinae MeSH
- Rats MeSH
- Humans MeSH
- Oligonucleotide Probes chemical synthesis MeSH
- DNA Repair physiology MeSH
- HMGB1 Protein metabolism MeSH
- Antineoplastic Agents metabolism pharmacology MeSH
- Recombinant Proteins genetics metabolism MeSH
- Electrophoretic Mobility Shift Assay MeSH
- Base Sequence MeSH
- Stereoisomerism MeSH
- Substrate Specificity MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Rats MeSH
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- DNA Adducts MeSH
- cisplatin-DNA adduct MeSH Browser
- Cisplatin MeSH
- Oligonucleotide Probes MeSH
- HMGB1 Protein MeSH
- Antineoplastic Agents MeSH
- Recombinant Proteins 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.
References provided by Crossref.org
Conformation of DNA GG intrastrand cross-link of antitumor oxaliplatin and its enantiomeric analog
Mechanism of the formation of DNA-protein cross-links by antitumor cisplatin
