Cu(Ⅱ)-histones interaction related to toxicity-carcinogenesis

G. Malandrinos; N. Hadjiliadis

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Cu(Ⅱ)-histones interaction related to toxicity-carcinogenesis

机译：Cu（Ⅱ）-组蛋白相互作用与毒性-致癌作用的关系

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In this review, we summarize the research work performed in the last years to elucidate the Cu(Ⅱ) induced toxicity-carcinogenesis mechanisms based on studies of Cu(Ⅱ) interactions with histone model peptides the most abundant protein part of cell nucleus. Oligopeptide models of histones, synthesized and used in most cases, helped us to determine stoichiometry, binding sites, conformations adopted and DNA damage caused by the metal. They are all reviewed and discussed, in an attempt to better understand the mechanisms of carcinogenesis caused by Cu(Ⅱ) ions. The metal-histones interaction affecting both DNA oxidative damage pathways and possibly the cause of epigenetic effects have also been considered. Strong Cu(Ⅱ) binding especially at physiological pH values provided by a 3N (N_(im), 2N~-} donor set could promote genotoxicity (DNA single/double strand scission) while induction of epigenetic changes might be the result of severe histone conformational changes affecting post-translational machinery ("histone code").

机译：在这篇综述中，我们基于对Cu（Ⅱ）与细胞核中蛋白质含量最高的组蛋白模型肽相互作用的研究，总结了近年来为阐明Cu（Ⅱ）诱导的毒性致癌机制所做的研究工作。在大多数情况下合成并使用的组蛋白的寡肽模型可帮助我们确定化学计量，结合位点，采用的构象以及金属引起的DNA损伤。他们都进行了审查和讨论，以更好地了解由Cu（Ⅱ）离子引起的致癌机理。还考虑了金属-组蛋白的相互作用会影响DNA氧化损伤途径，也可能影响表观遗传作用的原因。强大的Cu（Ⅱ）结合力，特别是在3N（N_（im），2N〜-}供体集提供的生理pH值下）可以促进遗传毒性（DNA单链/双链断裂），而表观遗传变化的诱导可能是严重组蛋白的结果影响翻译后机器的构象变化（“组蛋白代码”）。

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来源
《Coordination chemistry reviews》 |2014年第3期|55-71|共17页
作者
G. Malandrinos; N. Hadjiliadis;
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作者单位

University of Ioannina, Department of Chemistry, 45110 Ioannina, Greece;

University of Ioannina, Department of Chemistry, 45110 Ioannina, Greece;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);
原文格式 PDF
正文语种 eng
中图分类
关键词
Histones; Cu; Toxicity; Carcinogenesis;

机译：组蛋白;铜毒性;致癌作用;

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机译：Cu（II）和Ni（II）与组蛋白H2B的末端封闭的六肽Ac-Leu-Ala-His-Tyr-Asn-Lys-酰胺模型相互作用（80-85）
2. Interactions of Ni(II) and Cu(II) ions with the hydrolysis products of the C-terminal -ESHH- motif of histone H2A model peptides.Association of the stability of the complexes formed with the cleavage of the -E-S- bond [J] . Marios Mylonas, John C.Plakatouras, Nick Hadjiliadis Dalton transactions: An international journal of inorganic chemistry . 2004,第24期

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3. Interactions of Nickel(II) with histones: interactions of Nickel(II) with CH3CO-Thr-Glu-Ser-His-His-Lys-NH2, a peptide modeling the potential metal binding site in the "C-Tail" region of histone H2A. [J] . Bal W, Lukszo J, Bialkowski K, Chemical research in toxicology . 1998,第9期

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4. Picosecond laser cross: linking histones to DNA in chromatin: implication in studying histone/DNA interactions [C] . Author(s): D.Angelov Institute of Solid State Physics Sofia Bulgaria, S.Dimitrov Institute of Molecular Biology Sofia Bulgaria, E.Keskinova Institute of Solid State Physics Sofia Bulgaria, Intermational conference on laser applications in life sciences . 1994

机译：PicoSecond激光十字：将组蛋白联系在染色质中DNA：在研究组蛋白/ DNA相互作用时意味着
5. Dynamics and Interactions of Organic Molecules Bound to the Cu(111) Surface. [D] . Wyrick, Jonathan Eugene. 2013

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6. Cu(II) and Ni(II) Interactions with the Terminally Blocked Hexapeptide Ac-Leu-Ala-His-Tyr-Asn-Lys-amide Model of Histone H2B (80–85) [O] . Katerina Panagiotou, Maria Panagopoulou, Tilemachos Karavelas, 2008

机译：Cu（II）和Ni（II）与组蛋白H2B末端封闭的六肽Ac-Leu-Ala-His-Tyr-Asn-Lys-酰胺模型的相互作用（80-85）
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机译：Cu（II）和Ni（II）与组蛋白H2B的末端封闭六肽Ac-Leu-Ala-His-Tyr-Asn-Lys-酰胺模型的相互作用（80-85）

Cu(Ⅱ)-histones interaction related to toxicity-carcinogenesis

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