Naringin Protects Pancreatic β-Cells Against Oxidative Stress-Induced Apoptosis by Inhibiting Both Intrinsic and Extrinsic Pathways in Insulin-Deficient Diabetic Mice

2018 ◽  
Vol 62 (5) ◽  
pp. 1700810 ◽  
Author(s):  
Ye Jin Lim ◽  
Jung Ho Kim ◽  
Jeong Hoon Pan ◽  
Jae Kyeom Kim ◽  
Tae-Sik Park ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Diabetic Mice ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Induced Apoptosis

Bach1 deficiency protects pancreatic β-cells from oxidative stress injury

2013 ◽  
Vol 305 (5) ◽  
pp. E641-E648 ◽  
Author(s):  
Keiichi Kondo ◽  
Yasushi Ishigaki ◽  
Junhong Gao ◽  
Tetsuya Yamada ◽  
Junta Imai ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Insulin Resistance ◽  
Pancreatic Islets ◽  
Antioxidative Enzymes ◽  
Heme Oxygenase 1 ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Stress Injury ◽  
Induced Apoptosis ◽  
Deficient Mice

BTB and CNC homology 1 (Bach1) is a transcriptional repressor of antioxidative enzymes, such as heme oxygenase-1 (HO-1). Oxidative stress is reportedly involved in insulin secretion impairment and obesity-associated insulin resistance. However, the role of Bach1 in the development of diabetes is unclear. HO-1 expression in the liver, white adipose tissue, and pancreatic islets was markedly upregulated in Bach1-deficient mice. Unexpectedly, glucose and insulin tolerance tests showed no differences in obese wild-type (WT) and obese Bach1-deficient mice after high-fat diet loading for 6 wk, suggesting minimal roles of Bach1 in the development of insulin resistance. In contrast, Bach1 deficiency significantly suppressed alloxan-induced pancreatic insulin content reduction and the resultant glucose elevation. Furthermore, TUNEL-positive cells in pancreatic islets of Bach1-deficient mice were markedly decreased, by 60%, compared with those in WT mice. HO-1 expression in islets was significantly upregulated in alloxan-injected Bach1-deficient mice, whereas expression of other antioxidative enzymes, e.g., catalase, superoxide dismutase, and glutathione peroxidase, was not changed by either alloxan administration or Bach1 deficiency. Our results suggest that Bach1 deficiency protects pancreatic β-cells from oxidative stress-induced apoptosis and that the enhancement of HO-1 expression plays an important role in this protection.

scholarly journals Cyanidin-3-glucoside isolated from mulberry fruit protects pancreatic β-cells against oxidative stress-induced apoptosis

2014 ◽  
Vol 35 (2) ◽  
pp. 405-412 ◽  
Author(s):  
JONG SEOK LEE ◽  
YOUNG RAE KIM ◽  
IN GYU SONG ◽  
SUK-JIN HA ◽  
YOUNG EON KIM ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Mulberry Fruit ◽  
Induced Apoptosis

scholarly journals Cyanidin Attenuates Methylglyoxal-Induced Oxidative Stress and Apoptosis in INS-1 Pancreatic β-Cells by Increasing Glyoxalase-1 Activity

Nutrients ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 1319 ◽  
Author(s):  
Tanyawan Suantawee ◽  
Thavaree Thilavech ◽  
Henrique Cheng ◽  
Sirichai Adisakwattana
Keyword(s):  
Oxidative Stress ◽  
Protective Effect ◽  
Oxidative Dna Damage ◽  
Inhibitory Effect ◽  
Protein Glycation ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Glyoxalase 1 ◽  
Its Gene ◽  
Induced Apoptosis

Recently, the mechanisms responsible for anti-glycation activity of cyanidin and its derivatives on the inhibition of methylglyoxal (MG)-induced protein glycation and advanced glycation-end products (AGEs) as well as oxidative DNA damage were reported. In this study, we investigated the protective effect of cyanidin against MG-induced oxidative stress and apoptosis in rat INS-1 pancreatic β-cells. Exposure of cells to cytotoxic levels of MG (500 µM) for 12 h caused a significant reduction in cell viability. However, the pretreatment of cells with cyanidin alone (6.25–100 μM) for 12 h, or cotreatment of cells with cyanidin (3.13–100 μM) and MG, protected against cell cytotoxicity. In the cotreatment condition, cyanidin (33.3 and 100 μM) also decreased MG-induced apoptosis as determined by caspase-3 activity. Furthermore, INS-1 cells treated with MG increased the generation of reactive oxygen species (ROS) during a 6 h exposure. The MG-induced increase in ROS production was inhibited by cyanidin (33.3 and 100 μM) after 3 h stimulation. Furthermore, MG diminished the activity of glyoxalase 1 (Glo-1) and its gene expression as well as the level of total glutathione. In contrast, cyanidin reversed the inhibitory effect of MG on Glo-1 activity and glutathione levels. Interestingly, cyanidin alone was capable of increasing Glo-1 activity and glutathione levels without affecting Glo-1 mRNA expression. These findings suggest that cyanidin exerts a protective effect against MG-induced oxidative stress and apoptosis in pancreatic β-cells by increasing the activity of Glo-1.

Cinnamtannin D-1 Protects Pancreatic β-Cells from Palmitic Acid-Induced Apoptosis by Attenuating Oxidative Stress

2014 ◽  
Vol 62 (22) ◽  
pp. 5038-5045 ◽  
Author(s):  
Ting Wang ◽  
Peng Sun ◽  
Liang Chen ◽  
Qi Huang ◽  
Kaixian Chen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Palmitic Acid ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Induced Apoptosis

Carbonyl reductase 1 protects pancreatic β-cells against oxidative stress-induced apoptosis in glucotoxicity and glucolipotoxicity

2010 ◽  
Vol 49 (10) ◽  
pp. 1522-1533 ◽  
Author(s):  
M.A. Rashid ◽  
Seonmin Lee ◽  
Eunyoung Tak ◽  
Jisun Lee ◽  
Tae Gyu Choi ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Carbonyl Reductase ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Induced Apoptosis

scholarly journals Synergistic Effects of Milk-Derived Exosomes and Galactose on α-Synuclein Pathology in Parkinson’s Disease and Type 2 Diabetes Mellitus

2021 ◽  
Vol 22 (3) ◽  
pp. 1059
Author(s):  
Bodo C. Melnik
Keyword(s):  
Oxidative Stress ◽  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Dopaminergic Neurons ◽  
Vagal Nerve ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
The Brain

Epidemiological studies associate milk consumption with an increased risk of Parkinson’s disease (PD) and type 2 diabetes mellitus (T2D). PD is an α-synucleinopathy associated with mitochondrial dysfunction, oxidative stress, deficient lysosomal clearance of α-synuclein (α-syn) and aggregation of misfolded α-syn. In T2D, α-syn promotes co-aggregation with islet amyloid polypeptide in pancreatic β-cells. Prion-like vagal nerve-mediated propagation of exosomal α-syn from the gut to the brain and pancreatic islets apparently link both pathologies. Exosomes are critical transmitters of α-syn from cell to cell especially under conditions of compromised autophagy. This review provides translational evidence that milk exosomes (MEX) disturb α-syn homeostasis. MEX are taken up by intestinal epithelial cells and accumulate in the brain after oral administration to mice. The potential uptake of MEX miRNA-148a and miRNA-21 by enteroendocrine cells in the gut, dopaminergic neurons in substantia nigra and pancreatic β-cells may enhance miRNA-148a/DNMT1-dependent overexpression of α-syn and impair miRNA-148a/PPARGC1A- and miRNA-21/LAMP2A-dependent autophagy driving both diseases. MiRNA-148a- and galactose-induced mitochondrial oxidative stress activate c-Abl-mediated aggregation of α-syn which is exported by exosome release. Via the vagal nerve and/or systemic exosomes, toxic α-syn may spread to dopaminergic neurons and pancreatic β-cells linking the pathogenesis of PD and T2D.

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