Carcinogenic metals and the epigenome: understanding the effect of nickel, arsenic, and chromium (original) (raw)

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New York University School of Medicine, Nelson Institute of Environmental Medicine

, 57 Old Forge Road, NY 10987,

USA

. Fax: +1 845 731-2118; Tel: +1 845 731-3515

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New York University School of Medicine, Nelson Institute of Environmental Medicine

, 57 Old Forge Road, NY 10987,

USA

. Fax: +1 845 731-2118; Tel: +1 845 731-3515

Search for other works by this author on:

New York University School of Medicine, Nelson Institute of Environmental Medicine

, 57 Old Forge Road, NY 10987,

USA

. Fax: +1 845 731-2118; Tel: +1 845 731-3515

Search for other works by this author on:

Received:

03 February 2012

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Yana Chervona, Adriana Arita, Max Costa, Carcinogenic metals and the epigenome: understanding the effect of nickel, arsenic, and chromium, Metallomics, Volume 4, Issue 7, July 2012, Pages 619–627, https://doi.org/10.1039/c2mt20033c
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Abstract

Carcinogenic metals, such as nickel, arsenic, and chromium, are widespread environmental and occupational pollutants. Chronic exposure to these metals has been connected with increased risks of numerous cancers and as well as non-carcinogenic health outcomes, including cardiovascular disease, neurologic deficits, neuro-developmental deficits in childhood, and hypertension. However, currently the specific molecular targets for metal toxicity and carcinogenicity are not fully understood. Here, we propose that the iron- and 2-oxoglutarate-dependent dioxygenase family enzymes, as well as, other histone modifying enzymes are important intracellular targets that mediate the toxicity and carcinogenicity of nickel, and maybe potential targets in chromium and arsenic induced carcinogenesis. Our data demonstrate that all three metals are capable of inducing post-translational histone modifications and affecting the enzymes that modulate them (i.e. the iron- and 2-oxoglutarate-dependent dioxygenase family, including HIF-prolyl hydroxylase PHD2, histone demethylase JHDM2A/JMJD1A, and DNA repair enzymes ABH3 and ABH2, and histone methyltransferases, G9a). Given the effects that these metals can exert on the epigenome, future studies of their involvement in histone modifying enzymes dynamics would deepen our understanding on their respective toxicities and carcinogenicities.

Graphical Abstract

This articles discusses the role of iron- and 2-oxoglutarate-dependent dioxygenase family enzymes, as well as other histone modifying enzymes in influencing translational histone modifications, and gene expression, thereby mediating the toxicity and carcinogenicity of metals.

© The Royal Society of Chemistry 2012

This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open\_access/funder\_policies/chorus/standard\_publication\_model)

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