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Reactive Oxygen Species, Kinase Signaling, and Redox Regulation of Epigenetics

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Oxidative Stress and Redox Regulation

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Abstract

Reactive oxygen species (ROS) cause alterations in the cellular redox status (GSH/GSSG ratio) and hence activate various kinase signaling pathways, redox sensitive transcription factors (NF-κB and AP-1), and chromatin modification enzymes leading to increased pro-inflammatory and immunological responses. Chromatin modification enzymes include histone acetyltransferases (HATs), histone and non-histone deacetylases (HDACs, sirtuins), histone methyltransferases (HMTs) and histone demethylases (HDMs). Activation of these enzymes results in transcriptional gene activation/repression. Histone methyltransferases are enzymes that dynamically cause histone mono-, di- or tri-methylation at lysine residues, which either result in gene activation (H3K4, H3K36, and H3K79) or repression (H3K9, H3K27, and H3K20). Histone demethylases catalyze the removal of methyl groups from lysine or arginine residue of histones, hence regulating gene expression. Recent evidences have indicated that oxidative stress and environmental agents can alter nuclear histone acetylation/deacetylation/methylation, allowing access for transcription factor DNA binding and leading to enhanced pro-inflammatory gene expression. Cross-talks between histone modifications and DNA methylation also occur during inflammation. Understanding the mechanisms of ROS and redox epigenetic regulation via stress signaling kinases, redox sensitive transcription factors, the balance between histone acetylation/deacetylation and histone methylation/demethylation may lead to the development of novel therapies based on epigenetics against chronic inflammatory diseases, and cancer.

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Abbreviations

AP-1:

activator protein-1

CBP:

CREB-binding protein

COPD:

chronic obstructive pulmonary disease

CREB:

cAMP-response-element-binding protein

CS:

cigarette smoke

ECSOD:

extracellular superoxide dismutase

ERK:

extracellular signal-related kinase

FOXO:

forkhead box O

GR:

glucocorticoid receptor

GSH:

glutathione

GSSG:

glutathione disulfide

HAT:

histone acetyltransferase

HDAC:

histone deacetylase

HDM:

histone demethylase

HMT:

histone methytransferase

4-HNE:

4-hydroxy-2-nonenal

H2O2 :

hydrogen peroxide

•OH:

hydroxyl radical

IKK:

IkappaB kinase

IL-8:

interleukin-8

JNK:

c-Jun N-terminal protein kinase

LPS:

lipopolysaccharide

MMP-9:

matrix metalloproteinase-9

MnSOD:

manganese SOD

MSK1:

mitogen- and stress-activated kinase 1

NAD+ :

nicotinamide adenine dinucleotide

NF-κB:

nuclear factor κB

NIK:

NF-κB inducing kinase

NO:

nitric oxide

NSCLC:

non-small cell lung cancer

PCAF:

p300-CBP associated factor

ONOO− :

peroxynitrite anion

PGC-1α:

peroxisome-proliferator-activated receptor (PPAR) gamma co-activator-1 alpha

PI3K:

phosphoinositide 3-kinase

PKC:

Protein kinase C

RNS:

reactive nitrogen species

ROS:

reactive oxygen species

SIRT1:

sirtuin 1

STAT3:

signal transducer and activator of transcription 3

O2 •− :

superoxide anion

SOD:

superoxide dismutase

TGF-β1:

transforming growth factor-beta 1

TNF-α:

tumor necrosis factor-alpha

TSA:

trichostatin A

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Acknowledgements

This study was supported by the NIH 1R01HL085613, 1R01HL097751, 1R01HL092842, and NIEHS Environmental Health Science Center grant P30-ES01247.

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  1. Department of Environmental Medicine, Lung Biology and Disease Program, University of Rochester Medical Center, 850, 601 Elmwood Avenue, Rochester, NY, 14642, USA

    Isaac K. Sundar & Irfan Rahman Ph.D.

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  1. Isaac K. Sundar
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  2. Irfan Rahman Ph.D.
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Correspondence to Irfan Rahman Ph.D. .

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  1. Mol.,Cel. and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA

    Ursula Jakob

  2. The Alexander Silberman Institute of Life Science, Department of Biological Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel

    Dana Reichmann

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Sundar, I.K., Rahman, I. (2013). Reactive Oxygen Species, Kinase Signaling, and Redox Regulation of Epigenetics. In: Jakob, U., Reichmann, D. (eds) Oxidative Stress and Redox Regulation. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5787-5_11

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