Abstract
Endoplasmic reticulum (ER) is an important organelle for the protein synthesis, modification, folding, assembly, and the transport of new peptide chains. When the folding ability of ER proteins is impaired, the accumulation of unfolded or misfolded proteins in ER leads to endoplasmic reticulum stress (ERS). The nucleotide-binding oligomerization domain-like receptor family, pyrin domain-containing 3 (NLRP3) inflammasome, can induce the maturation and secretion of interleukin-1beta (IL-1β) and IL-18 through activating caspase-1. It is associated with many diseases. Studies have shown that ERS can regulate NLRP3 inflammasome in many diseases including diabetes. However, the mechanism of the effects of ERS on NLRP3 inflammasome in diabetes has not been fully understood. This review summarizes the recent researches about the effects of ERS on NLRP3 inflammasome and the related mechanism in diabetes to provide ideas for the relevant basic research in the future.
Highlights
Diabetes is characterized by the destruction of glucose homeostasis and the deficiency of insulin effect on the liver, muscle, pancreas, and fat (Sarwar et al, 2010; Defronzo et al, 2015)
The studies showed that metformin and resveratrol, as well as TUDCA, inhibited reactive oxygen species (ROS) generation and endoplasmic reticulum stress (ERS) induced by high glucose (HG) and improved glucose homeostasis in the adipose tissue of diabetic mice, indicating that ERS was involved in the inhibitory effects of metformin and resveratrol on HG-induced oxidative stress (Li et al, 2016)
Previous studies have shown that ERS can activate NLRP3 inflammasome through ROS/ERK1 pathway, ROS/Thioredoxininteracting protein (TXNIP) pathway and NF-κB pathway (Figure 1; Ji et al, 2019)
Summary
Diabetes is characterized by the destruction of glucose homeostasis and the deficiency of insulin effect on the liver, muscle, pancreas, and fat (Sarwar et al, 2010; Defronzo et al, 2015). It can be inferred that Mangiferin inhibited HG-induced TXNIP/NLRP3 inflammasome activation through suppressing ERS by activating AMPK to improve endothelial dysfunction (Song et al, 2015).
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