Induction of Apoptosis of β Cells of the Pancreas by Advanced Glycation End‐Products, Important Mediators of Chronic Complications of Diabetes Mellitus
Abstract
We herein report cytotoxicity of advanced glycation end‐products (AGEs) on pancreatic β cells. AGEs stimulated reactive oxygen species (ROS) generation but did not arrest proliferation of the INS‐1 cell line. Pancreatic β cell lines or primary cultured islets possess a receptor for AGE (RAGE), and its expression increased after AGE treatment. TUNEL staining and FACS analysis using annexin V/PI antibodies showed that apoptosis increased in INS‐1 cells or primary cultured islets when incubated with BSA conjugated with glyceraldehyde (AGE2) or glucoaldehyde (AGE3), compared with those conjugated with glucose (AGE1). Reaction of INS‐1 cells to Ki67, which is a cellular marker for proliferation, was also increased after AGE treatment. The ability of primary cultured islets to secrete insulin was retained even after AGE treatment under either low or high glucose conditions. The antiserum against RAGE partially prevented AGE‐induced cellular events. Treatment of β cells with the antioxidant metallothionein results in a significant reduction in pathologic changes. AGEs might be able to induce apoptosis as well as proliferation of pancreatic β cell lines or primary cultured islets. Moreover, antibody array showed that RAD51 and RAD52 were significantly decreased in AGE2‐treated INS‐1 cells. AGEs might inhibit homologous DNA recombination for repairing DNA of INS‐1 cells damaged by ROS generation. It might be suggested that treatment of AGEs resulted in ROS production and apoptosis through their receptor on pancreatic β cells. AGEs might deteriorate function of pancreatic β cells in patients with long‐term hyperglycemia.
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In blood vessels, accumulated AGEs interact with mononuclear, endothelial, and smooth muscle cells, resulting in cellular dysfunction, tissue damage, and atherosclerosis development.
“In blood vessels, accumulated AGEs also interact with mononuclear, endothelial, and smooth muscle cells, resulting in cellular dysfunction, tissue damage, and atherosclerosis development55–57,59.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [57]
Inhibition of RAGE by RAGE antiserum can prevent the toxicity induced by AGEs in diabetic microvascular complications.
“In contrast, the inhibition of RAGE by RAGE antiserum can prevent the toxicity induced by AGEs in diabetic microvascular complications57.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [57]
Accumulation and exposure to AGEs exacerbate oxidative stress and inflammation and initiate the oxidation of LDLs, which are harmful to cardiovascular function.
“The accumulation and exposure to AGEs exacerbate oxidative stress and inflammation and initiate the oxidation of low-density lipoproteins (LDLs), which are harmful to cardiovascular function.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [57]
Endogenous and exogenous AGEs provoke the initiation and progression of NAFLD, and dietary AGEs from fructose- or sucrose-enriched diets and/or soft drinks can worsen liver fibrosis faster than endogenous AGEs.
“Endogenous and exogenous AGEs provoke the initiation and progression of NAFLD.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [57]
Aggregation of AGEs decreases GSH, SIRT1, and TIMP3 and increases oxidative stress and inflammation, promoting inflammatory liver injury and fibrosis in experimental animal models and NAFLD patients.
“The aggregation of AGEs decreases the levels of the most important cellular antioxidant peptides, glutathione (GSH), SIRT1, and tissue inhibitor of metalloproteinase 3 (TIMP3), accompanied by increased oxidative stress and inflammation, promoting inflammatory liver injury and fibrosis in experimental animal models and NAFLD patients55–57,124–126.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [57]
Soluble RAGE, inhibitors of the RAGE signaling pathway, neutralizing antibodies against RAGE or AA-AGE adduct, and other AGE-degrading compounds have been reported to decrease AGE adduct formation.
“Furthermore, soluble RAGE119,200, inhibitors of the RAGE signaling pathway130,131, neutralizing antibodies against RAGE57 or AA-AGE adduct199, and other AGE-degrading compound(s), such as pyridoxamine and ALT-711200, lipoic acid291, synthetic compounds OPB-9195292, and nitrothiadiazolo[3,2-α]pyrimidines293, have been reported to decrease AGE adduct formation.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [57]
AGEs contribute to pancreatic β-cell dysfunction, a key component in the pathogenesis of T2DM.
“AGEs also contribute to pancreatic 𝛽-cell dysfunction, another key component in the pathogenesis of T2DM.”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [135]
Inhibition of RAGE or antioxidant treatment prevents AGE-induced cell toxicity in primary β-cells and cell lines.
“Studies using primary 𝛽-cells and cell lines demonstrate that inhibition of RAGE or antioxidant treatment prevents AGE-induced cell toxicity.[135]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [135]
AGEs exert a cytotoxic effect on β-cells and induce apoptosis, which may be dependent on ROS production.
“AGEs exert cytotoxic effect on 𝛽-cells and induce apoptosis, which may be dependent on ROS production.”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [135]
Chronically increased ROS production can induce β-cell death and result in gradual onset of diabetes.
“Chronically increased ROS production could also induce -cell death and result in gradual onset of diabetes (249 -253).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [250]
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- Authors
- Lim, M., Park, L., Shin, G., Hong, H., Kang, I., & Park, Y.
- Affiliations
- Hanyang University (KR)
- Corresponding author
- Park, Yongsoo
- ORCID
- Park, Yongsoo
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 2008-12
- Volume
- 1150
- Issue
- 1
- Pages
- 311-315
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- OpenAlex
- W2074417825
- Cited by
- 81
- References
- 10
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2 · 2023: 9 · 2022: 1 · 2021: 5 · 2020: 3 · 2019: 7 · 2018: 1 · 2017: 4 · 2016: 7 · 2015: 4 · 2014: 8 · 2013: 8 · 2012: 3
- FWCI
- 3.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Keywords
- advanced glycation end products, pancreatic beta cells, apoptosis, receptor for advanced glycation end products, reactive oxygen species, beta-cell proliferation, insulin secretion, metallothionein, RAD51, RAD52, DNA repair, homologous recombination, diabetes complications, hyperglycemia, INS-1 cells, pancreatic islets
- MeSH terms
- Receptor for Advanced Glycation End Products, Animals, Cells, Cultured, Chronic Disease, Receptors, Immunologic, Glycation End Products, Advanced, Rats, Sprague-Dawley, Apoptosis, Reactive Oxygen Species, Tissue Array Analysis, Diabetes Complications, Insulin-Secreting Cells, Rad51 Recombinase, Mice, Rats, Rad52 DNA Repair and Recombination Protein
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