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Current status of endoplasmic reticulum stress in type ii diabetes

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Mustapha, S, Mohammed, M, Azemi, AK, Jatau, AI, Shehu, A, Mustapha, L, Aliyu, IM, Danraka, RN, Amin, A, Bala, AA, Wan Ahmad, WAN, Rasool, AHG, Mustafa, MR and Mokhtar, SS 2021 , 'Current status of endoplasmic reticulum stress in type ii diabetes' , Molecules, vol. 26, no. 14 , pp. 1-16 , doi: 10.3390/molecules26144362.

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Abstract

The endoplasmic reticulum (ER) plays a multifunctional role in lipid biosynthesis, calcium storage, protein folding, and processing. Thus, maintaining ER homeostasis is essential for cellular functions. Several pathophysiological conditions and pharmacological agents are known to disrupt ER homeostasis, thereby, causing ER stress. The cells react to ER stress by initiating an adaptive signaling process called the unfolded protein response (UPR). However, the ER initiates death signaling pathways when ER stress persists. ER stress is linked to several diseases, such as cancer, obesity, and diabetes. Thus, its regulation can provide possible therapeutic targets for these. Current evidence suggests that chronic hyperglycemia and hyperlipidemia linked to type II diabetes disrupt ER homeostasis, thereby, resulting in irreversible UPR activation and cell death. Despite progress in understanding the pathophysiology of the UPR and ER stress, to date, the mechanisms of ER stress in relation to type II diabetes remain unclear. This review provides up-to-date information regarding the UPR, ER stress mechanisms, insulin dysfunction, oxidative stress, and the therapeutic potential of targeting specific ER stress pathways.

Item Type: Article
Authors/Creators:Mustapha, S and Mohammed, M and Azemi, AK and Jatau, AI and Shehu, A and Mustapha, L and Aliyu, IM and Danraka, RN and Amin, A and Bala, AA and Wan Ahmad, WAN and Rasool, AHG and Mustafa, MR and Mokhtar, SS
Keywords: endoplasmic reticulum, endoplasmic reticulum stress, apoptosis, homeostasis, unfolded protein response, type II diabetes
Journal or Publication Title: Molecules
Publisher: Molecular Diversity Preservation International
ISSN: 1420-3049
DOI / ID Number: 10.3390/molecules26144362
Copyright Information:

Copyright 2021 the authors. Licensed under Creative Commons Attribution 4.0 International (CC BY 4.0) https://creativecommons.org/licenses/by/4.0/

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