Restriction of Advanced Glycation End Products Improves Insulin Resistance in Human Type 2 Diabetes
Open accessAbstract
OBJECTIVE: Increased oxidative stress (OS) and impaired anti-OS defenses are important in the development and persistence of insulin resistance (IR). Several anti-inflammatory and cell-protective mechanisms, including advanced glycation end product (AGE) receptor-1 (AGER1) and sirtuin (silent mating-type information regulation 2 homolog) 1 (SIRT1) are suppressed in diabetes. Because basal OS in type 2 diabetic patients is influenced by the consumption of AGEs, we examined whether AGE consumption also affects IR and whether AGER1 and SIRT1 are involved. RESEARCH DESIGN AND METHODS: The study randomly assigned 36 subjects, 18 type 2 diabetic patients (age 61 ± 4 years) and 18 healthy subjects (age 67 ± 1.4 years), to a standard diet (>20 AGE equivalents [Eq]/day) or an isocaloric AGE-restricted diet (<10 AGE Eq/day) for 4 months. Circulating metabolic and inflammatory markers were assessed. Expression and activities of AGER1 and SIRT1 were examined in patients’ peripheral blood mononuclear cells (PMNC) and in AGE-stimulated, AGER1-transduced (AGER1+), or AGER1-silenced human monocyte-like THP-1 cells. RESULTS: Insulin and homeostasis model assessment, leptin, tumor necrosis factor-α and nuclear factor-κB p65 acetylation, serum AGEs, and 8-isoprostanes decreased in AGE-restricted type 2 diabetic patients, whereas PMNC AGER1 and SIRT1 mRNA, and protein levels normalized and adiponectin markedly increased. AGEs suppressed AGER1, SIRT-1, and NAD+ levels in THP-1 cells. These effects were inhibited in AGER1+ but were enhanced in AGER1-silenced cells. CONCLUSIONS: Food-derived pro-oxidant AGEs may contribute to IR in clinical type 2 diabetes and suppress protective mechanisms, AGER1 and SIRT1. AGE restriction may preserve native defenses and insulin sensitivity by maintaining lower basal OS.
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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 [55]
Restriction of dietary AGEs can reduce and/or reverse these effects by enhancing insulin sensitivity and upregulating AGE-R1 and SIRT1 while suppressing NF-κB, TNF-α, leptin, and serum AGEs in type 2 DM.
“Restriction of dietary AGEs can reduce and/or reverse these effects by enhancing insulin sensitivity and upregulating AGE-R1 and SIRT1 expression while suppressing NF-κB, tumor necrosis factor-alpha (TNF-α), leptin, and serum AGEs in type 2 DM55.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [55]
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 [55]
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 [55]
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 [55]
AGER1 can counteract AGE-induced oxidative stress and inhibit activation of NF-kB by promoting sirtuin1-dependent deacetylation and suppression of NF-kB.
“AGER1 can counteract AGE-induced oxidative stress [61,62] as well as inhibit the activation of NF-𝜅B by promoting a sirtuin1-dependent deacetylation and suppression of NF-𝜅B.[63,64]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [63]
An AGE-restricted diet improves insulin sensitivity in T2DM with normalization of AGER1 and sirtuin1 expression and a decrease in NF-kB acetylation, circulating TNFα, serum AGEs, and leptin.
“with an AGE-restricted diet improving insulin sensitivity in T2DM with a normalization of the expression of AGER1 and sir-tuin1 as well as a decrease in NF-𝜅B acetylation circulating TNF𝛼, serum AGEs, and leptin.[63]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [63]
Insulin resistance may be a mechanism underpinning the ability of AGEs to disrupt hypothalamic control of energy balance.
“In light of the central role of insulin in regulating energy balance, insulin resistance may be a mechanism underpinning the ability of AGEs to disrupt hypothalamic control of energy balance.[63,131,133]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [63]
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- Authors
- Uribarri, J., Cai, W., Ramdas, M., Goodman, S., Pyzik, R., Chen, X., Zhu, L., Striker, G. E., & Vlassara, H.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Vlassara, Helen
- Venue
- Diabetes Care
- Publisher
- American Diabetes Association
- Published
- 2011-06-17
- Volume
- 34
- Issue
- 7
- Pages
- 1610-1616
- ISSN
- 0149-5992 (ISSN-L)
- 1935-5548
- PMC
- PMC3120204
- OpenAlex
- W2061906058
- Cited by
- 320
- References
- 26
- Citations by year
- 2026: 2 · 2025: 14 · 2024: 19 · 2023: 20 · 2022: 24 · 2021: 25 · 2020: 25 · 2019: 16 · 2018: 26 · 2017: 30 · 2016: 26 · 2015: 32 · 2014: 10 · 2013: 31 · 2012: 13
- FWCI
- 11.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Diabetes Care (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R37AG023188, R01AG009453)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK091231)
- National Center for Research Resources (M01RR000071)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Keywords
- advanced glycation end products, insulin resistance, type 2 diabetes, SIRT1, oxidative stress, inflammation, NAD+, adiponectin, TNF-α, NF-κB p65 acetylation, 8-isoprostane, peripheral blood mononuclear cells, THP-1 cells
- MeSH terms
- Receptor for Advanced Glycation End Products, Aged, Cells, Cultured, Diabetes Mellitus, Type 2, Female, Humans, Hypoglycemic Agents, Inflammation, Insulin Resistance, Leukocytes, Mononuclear, Male, Middle Aged, Receptors, Immunologic, Glycation End Products, Advanced, Oxidative Stress, Sirtuin 1
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