Molecular models in nickel carcinogenesis

被引：87

作者：

Bal, W ^{[1
]}

Kozlowski, H

Kasprzak, KS

机构：

[1] Univ Wroclaw, Fac Chem, PL-50138 Wroclaw, Poland

[2] NCI, Comparat Carcinogenesis Lab, FCRDC, Frederick, MD 21702 USA

来源：

JOURNAL OF INORGANIC BIOCHEMISTRY | 2000年 / 79卷 / 1-4期

关键词：

nickel(II); nickel(II)-peptide interactions; histone H1; histone H2A; histone H3; histone H4; core histone tetramer; peptide bond hydrolysis; 2'-deoxyguanosine oxidation; speciation;

D O I：

10.1016/S0162-0134(99)00169-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Nickel compounds are known human carcinogens, but the exact molecular mechanisms of nickel carcinogenesis are not known. Due to their abundance, histones are likely targets for Ni(II) ions among nuclear macromolecules. This paper reviews our recent studies of peptide and protein models of Ni(II) binding to histones. The results allowed us to propose several mechanisms of Ni(II)-inflicted damage, including nucleobase oxidation and sequence-specific histone hydrolysis. Quantitative estimations of Ni(II) speciation, based on these studies, support the likelihood of Ni(II) binding to histones in vivo, and the protective role of high levels of glutathione. These calculations indicate the importance of histidine in the intracellular Ni(II) speciation. (C) 2000 Elsevier Science Inc. All rights reserved.

引用

页码：213 / 218

页数：6

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