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Endoplasmic Reticulum Stress Induced by Toxic Elements—a Review of Recent Developments

  • S. V. S. RanaEmail author
Article
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Abstract

Endoplasmic reticulum of all eukaryotic cells is a membrane-bound organelle. Under electron microscope it appears as parallel arrays of “rough membranes” and a maze of “smooth vesicles” respectively. It performs various functions in cell, i.e., synthesis of proteins to degradation of xenobiotics. Bioaccumulation of drugs/chemicals/xenobiotics in the cytosol can trigger ER stress. It is recognized by the accumulation of unfolded or misfolded proteins in the lumen of ER. Present review summarizes the present status of knowledge on ER stress caused by toxic elements, viz arsenic, cadmium, lead, mercury, copper, chromium, and nickel. While inorganic arsenic may induce various glucose-related proteins, i.e., GRP78, GRP94 and CHOP, XBP1, and calpains, cadmium upregulates GRP78. Antioxidants like ascorbic acid, NAC, and Se inhibit the expression of UPR. Exposure to lead also changes ER stress related genes, i.e., GRP 78, GRP 94, ATF4, and ATF6. Mercury too upregulates these genes. Nickel, a carcinogenic element upregulates the expression of Bak, cytochrome C, caspase-3, caspase-9, caspase-12, and GADD 153. Much is not known on ER stress caused by nanoparticles. The review describes inter-organelle association between mitochondria and ER. It also discusses the interdependence between oxidative stress and ER stress. A cross talk amongst different cellular components appears essential to disturb pathways leading to cell death. However, these molecular switches within the signaling network used by toxic elements need to be identified. Nevertheless, ER stress especially caused by toxic elements still remains to be an engaging issue.

Keywords

Toxic elements Endoplasmic reticulum stress Oxidative stress Unfolded protein response Biomarkers of endoplasmic reticulum stress Cell death 

Abbreviations

ER

Endoplasmic reticulum

ER stress

Endoplasmic reticulum stress

UPR

Unfolded protein response

IRE1

Inositol requiring kinase 1

elf2alpha

Initiation factor 2 alpha

PERK

PKR-like kinase

ATF

Activating transcription factor

Bip

Binding protein

GRP78

Glucose-regulated protein 78

ERAD

ER-associated degradation

PDI

Protein disulfide isomerise

ROS

Reactive oxygen species

FAD

Flavin adenine nucleotide

ERO1

Endoplasmic reticulum oxidoreduction 1

ATO

Arsenic trioxide

GRP94

Glucose-related protein 94

CHOP

C/EBP homologous protein

XBP1

X-box binding protein

GSIS

Glucose-stimulated insulin secretion

GJIC

Gap junctional intercellular communication

NOX4

NADPH oxidase 4

MFO

Mixed function oxidase

NAC

N-acetyl cysteine

Se

Selenium

Notes

Acknowledgments

Financial support from Indian Science Congress Association, Kolkata (India), in the form of Ashutosh Mookerjee Fellowship to the author is gratefully acknowledged. The author is also thankful to the Head of the Department of Toxicology, Ch. Charan Singh University, Meerut (India), for extending the technical and administrative support.

Compliance with Ethical Standards

Conflict of Interest

The author declares that there is no conflict of interest.

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Authors and Affiliations

  1. 1.Department of ToxicologyCh. Charan Singh UniversityMeerutIndia

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