Recognition of DNA interstrand cross-links of cis-diamminedichloroplatinum(II) and its trans isomer by DNA-binding proteins
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
PubMed
7547982
DOI
10.1021/bi00038a035
Knihovny.cz E-zdroje
- MeSH
- adukty DNA metabolismus MeSH
- cisplatina metabolismus MeSH
- DNA footprinting MeSH
- DNA vazebné proteiny metabolismus MeSH
- endodeoxyribonukleasy metabolismus MeSH
- kompetitivní vazba MeSH
- konformace nukleové kyseliny MeSH
- molekulární sekvence - údaje MeSH
- poškození DNA MeSH
- proteiny s vysokou pohyblivostí metabolismus MeSH
- protinádorové látky metabolismus MeSH
- reagencia zkříženě vázaná metabolismus MeSH
- sekvence nukleotidů MeSH
- substrátová specifita MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- adukty DNA MeSH
- cisplatina MeSH
- DNA vazebné proteiny MeSH
- endodeoxyribonuclease VII MeSH Prohlížeč
- endodeoxyribonukleasy MeSH
- proteiny s vysokou pohyblivostí MeSH
- protinádorové látky MeSH
- reagencia zkříženě vázaná MeSH
- transplatin MeSH Prohlížeč
Recognition and processing by cellular proteins of DNA modified by platinum complexes have been suggested to be relevant to the mechanism of their antitumor activity. Platinum complexes form on DNA various mono- and bifunctional adducts. It has already been described by other authors that intrastrand cross-links formed on DNA by antitumor cis-diamminedichloroplatinum(II) (cisplatin) between neighboring purine residues are recognized by several DNA-binding proteins. In contrast, these proteins do not recognize the intrastrand cross-links formed on DNA by cisplatin or its clinically ineffective trans isomer (transplatin) between nonadjacent base residues. An eventuality heretofore not addressed is that DNA interstrand cross-links (ICLs) of platinum compounds may be recognized by and bound to DNA-binding proteins. DNA probes of 110 base pairs (bp) were constructed containing five equally spaced ICLs of cisplatin or transplatin. These ICLs were formed at specific sites at which these adducts are preferentially formed in natural DNA. Gel electrophoresis mobility shift and competition assays with these probes were used to investigate the specific recognition and binding of the calf thymus HMG1 protein to the DNA ICLs of both platinum isomers. The ICL of antitumor cisplatin was recognized by and bound to the HMG1 protein with a similar affinity as the 1,2-intrastrand d(GpG) cross-link of this drug. The protein binding to the ICL is selective for the DNA modification by cisplatin, but not by chemotherapeutically inactive transplatin.(ABSTRACT TRUNCATED AT 250 WORDS)
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