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Current Status of Endoplasmic Reticulum Stress in Type II Diabetes.
- Source :
-
Molecules (Basel, Switzerland) [Molecules] 2021 Jul 19; Vol. 26 (14). Date of Electronic Publication: 2021 Jul 19. - Publication Year :
- 2021
-
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.
- Subjects :
- Animals
Diabetes Mellitus, Type 2 drug therapy
Diabetes Mellitus, Type 2 pathology
Humans
Hyperglycemia drug therapy
Hyperglycemia metabolism
Hyperglycemia pathology
Hyperlipidemias drug therapy
Hyperlipidemias metabolism
Hyperlipidemias pathology
Neoplasms drug therapy
Neoplasms metabolism
Neoplasms pathology
Obesity drug therapy
Obesity metabolism
Obesity pathology
Diabetes Mellitus, Type 2 metabolism
Endoplasmic Reticulum Stress
Oxidative Stress
Signal Transduction
Subjects
Details
- Language :
- English
- ISSN :
- 1420-3049
- Volume :
- 26
- Issue :
- 14
- Database :
- MEDLINE
- Journal :
- Molecules (Basel, Switzerland)
- Publication Type :
- Academic Journal
- Accession number :
- 34299638
- Full Text :
- https://doi.org/10.3390/molecules26144362