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Epigenetic Phenomena of Arsenic and Histone Tail Modifications: Implications for Diet and Nutrition

  • Qiao Yi Chen
  • Max CostaEmail author
Reference work entry

Abstract

Naturally occurring inorganic arsenic has been identified as the causal agent in human skin, lung, bladder, liver, and prostate cancers. Furthermore, arsenic exposure has also been associated with noncarcinogenic health outcomes, including cardiovascular disease, neurologic deficits, neurodevelopmental deficits in childhood, and hypertension. According to the Agency for Toxic Substances and Disease Registry, arsenic is considered number one on the substance priority list. However, the overall risks on human health may exceed the documented levels due to lack of a comprehensive consideration of exposure through diet and anthropogenic factors. Arsenic permeates through water and soil, and related health issues elicit global concerns for the mass public. The exact mechanism of arsenic toxicity is still not fully understood, although convincing evidence and recent advance in epigenetic research such as DNA methylation and histone posttranslational modifications have broadened our scope in understanding the mechanism of arsenic toxicity and carcinogenicity. This chapter will present the most recent literatures on the effect of arsenic on histone tail modifications as well as implications on food and diet.

Keywords

Inorganic arsenic Histone tail modifications Methylation Acetylation H3.1 Stem-loop binding protein Nutrition 

List of Abbreviations

AcCOA

Acetyl coenzyme A

As

Arsenic

As (III)

Trivalent As

As (V)

Pentavalent As

As3MT1

Arsenic methyltransferase 1

BL-41

Human lung carcinoma cells

DMA5+

Dimethylarsinic acid

HACAT

Male-derived human keratinocytes

HAT

Histone acetyltransferase

HEK293

Female-derived human embryonic kidney cells

H(X)K(X)

Histone (X) Lysine (X)

iAs

Inorganic arsenic

K

Lysine

MMA5+

Monomethylarsonic acid

PBMC

Peripheral blood mononuclear cells

Ppb

Parts per billion

PTMs

Histone posttranslational modifications

R

Arginine

SAM

Cofactor S-Adenosyl methionine

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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  1. 1.Department of Environmental MedicineNew York University School of MedicineTuxedoUSA

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