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Oxidative Stress-Induced Mitochondrial Dysfunction and Asthma

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Oxidative Stress in Lung Diseases

Abstract

Asthma is a well-recognized global concern with ever-increasing prevalence and economic burden worldwide. Genetic susceptibility and exposure to environmental triggers such as allergens, pollutants, infectious agents and even lifestyle choices are well-established modulators of the disease. Recent studies show that irrespective of the nature of causal trigger (allergic or nonallergic), mitochondria and its dysfunction is a central player in asthma pathogenesis. This chapter discusses the studies and mechanisms through which mitochondria plays its role in causing asthma pathogenesis. Under allergic asthma conditions, immune response and epithelial barrier functions are the key players modulating the function of mitochondria. Other mechanism that leads to the development of obese-asthma phenotype involves disruption of cellular bioenergetics via modulating nitric oxide levels, calcium homeostasis, etc. Repair, reprogramming and/or replacement of the dysfunctional mitochondria are some of the possible therapeutic strategies for better management of asthma.

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Abbreviations

12/15-LOX:

12/15-lipoxygenase

12-S-HETE:

12-S-hydroxyeicosatetraenoic acid

13-S-HODE:

13-S-hydroxyoctadecadienoic acid

ADMA:

Asymmetric dimethylarginine

AMP:

Adenosine monophosphate

ATP:

Adenosine triphosphate

CaMKII:

Ca2+/calmodulin-dependent protein kinase II

CLR:

C-type lectin receptors

DAMP:

Damage-associated molecular pattern

DC :

Dendritic cell

DRP1:

Dynamin-related protein 1

eNOS:

Endothelial nitric oxide synthase

ETC:

Electron transport chain

FADH2:

2-Dihydro flavin adenine dinucleotide

HDM:

House dust mite

IgE:

Immunoglobulin E

IL :

Interleukins

LPS:

Lipopolysaccharide

MCU:

Mitochondrial calcium uniporter

MetS:

Metabolic syndrome

MHC II:

Major histocompatibility complex class II

MSC:

Mesenchymal stem cell

mtDNA:

Mitochondrial DNA

NADH:

Nicotinamide adenine dinucleotide (reduced)

NADPH:

Nicotinamide adenine dinucleotide phosphate (reduced)

nDNA:

Nuclear DNA

NF-kβ:

Nuclear factor kappa-light-chain-enhancer of activated B cells

NFP:

N-Formyl peptides

NLR:

Nucleotide-binding domain/leucine-rich repeat receptor

NLRP3:

Nod-like receptor family pyrin domain containing 3

NO:

Nitric oxide

NRF-1:

Nuclear respiratory factor-1

OONO−:

Peroxynitrite

OPA1:

Optic atrophy protein 1

OVA:

Ovalbumin

PAMP:

Pathogen-associated molecular pattern

PBMCs:

Peripheral blood mononuclear cells

PC :

Phosphatidylcholine

PGC-1α:

Peroxisome proliferator-activated receptor-gamma coactivator

PKC-δ:

Protein kinase C delta type

PQQ:

Pyrroloquinoline quinone

PRR:

Pathogen recognition receptor

RLR:

Retinoic acid-inducible gene (RIG-1)-like receptors

ROS:

Reactive oxygen species

siRNA:

Small interfering RNA

TCR:

T-cell receptor

TFAM:

Mitochondrial transcription factor A

Th2:

Type 2 T helper cells

TLR:

Toll-like receptor

TNF-α:

Tumour necrosis factor alpha

TRPV1:

Transient receptor potential cation channel subfamily V member 1

UQCRC2:

Ubiquinol-cytochrome c reductase core protein II

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Author notes

  1. Authors Samarpana Chakraborty and Kritika Khanna have equally contributed to this chapter.

Authors and Affiliations

  1. CSIR Institute of Genomics and Integrative Biology, Delhi, India

    Samarpana Chakraborty, Kritika Khanna & Anurag Agrawal

  2. Academy of Scientific and Innovative Research, Delhi, India

    Anurag Agrawal

  3. Baylor College of Medicine, Houston, TX, USA

    Anurag Agrawal

Authors
  1. Samarpana Chakraborty
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  2. Kritika Khanna
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  3. Anurag Agrawal
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Corresponding author

Correspondence to Anurag Agrawal .

Editor information

Editors and Affiliations

  1. Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India

    Sajal Chakraborti

  2. Department of Internal Medicine, The Ohio State University, Columbus, OH, USA

    Narasimham L. Parinandi

  3. Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India

    Rita Ghosh

  4. Apollo Hospitals Educational & Research Foundation (AHERF), Indraprastha Apollo Hospitals, New Delhi, Delhi, India

    Nirmal K. Ganguly

  5. Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India

    Tapati Chakraborti

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Chakraborty, S., Khanna, K., Agrawal, A. (2020). Oxidative Stress-Induced Mitochondrial Dysfunction and Asthma. In: Chakraborti, S., Parinandi, N., Ghosh, R., Ganguly, N., Chakraborti, T. (eds) Oxidative Stress in Lung Diseases. Springer, Singapore. https://doi.org/10.1007/978-981-32-9366-3_6

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