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Advanced glycation end-product
Proteins or lipids chemically altered by sugar exposure

Advanced glycation end-products (AGEs) form through the Maillard reaction between reducing sugars and amino compounds during digestion and food processing. In aging individuals, AGEs may trigger inflammatory substances that contribute to tissue damage and increased risk of chronic diseases such as diabetes, atherosclerosis, and Alzheimer's disease. While AGEs are being studied as potential biomarkers of aging, current evidence as of 2024 remains inconsistent, with no confirmed causal association between dietary AGEs and disease development.

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Dietary sources

Animal-derived foods that are high in fat and protein are generally AGE-rich and are prone to further AGE formation during cooking.910 However, only low molecular weight AGEs are absorbed through diet, and vegetarians have been found to have higher concentrations of overall AGEs compared to non-vegetarians.11

Effects

AGEs can be produced in the body and in manufactured foods.1213 The accumulation of AGEs may have causative roles in several age-related diseases by forming adducts with proteins and lipids.1415 In preliminary research, AGEs affect nearly every type of cell and molecule in the body and are thought to be one factor in aging16 and some age-related chronic diseases.171819 They are also believed to play a causative role in the vascular complications of diabetes mellitus.20

AGEs may arise under certain pathological conditions, such as oxidative stress due to hyperglycemia in patients with diabetes.212223 AGEs may have a role as proinflammatory mediators in gestational diabetes.24

In the context of cardiovascular disease, a possible AGE mechanism is to induce crosslinking of collagen, which can cause vascular stiffening and entrapment of low-density lipoprotein particles (LDL) in the artery walls.25 AGEs can also cause glycation of LDL which can promote its oxidation.26 Oxidized LDL is one of the major factors in the development of atherosclerosis.27 AGEs can bind to RAGE (receptor for advanced glycation end products) and cause oxidative stress as well as activation of inflammatory pathways in vascular endothelial cells.2829

In other diseases

AGEs have been implicated in Alzheimer's disease and cardiovascular diseases.3031

According to in vitro research, the mechanism by which AGEs may induce damage is through a process called cross-linking that causes intracellular damage and apoptosis.32

Pathology

In laboratory studies, AGEs have a range of pathological effects, such as:3334

  • Increased vascular permeability.
  • Increased arterial stiffness.
  • Inhibition of vascular dilation by interfering with nitric oxide.
  • Oxidizing LDL.
  • Binding cells—including macrophage, endothelial, and mesangial—to induce the secretion of a variety of cytokines.
  • Enhanced oxidative stress.
  • Hemoglobin-AGE levels are elevated in diabetic individuals.35 Therefore, substances that inhibit AGE formation may limit the progression of disease and may offer new tools for therapeutic interventions in the therapy of AGE-mediated disease.3637
  • AGEs have specific cellular receptors; the best-characterized are those called RAGE. The activation of cellular RAGE on endothelium, mononuclear phagocytes, and lymphocytes triggers the generation of free radicals and the expression of inflammatory gene mediators.38 Such increases in oxidative stress lead to the activation of the transcription factor NF-κB and promote the expression of NF-κB regulated genes that have been associated with atherosclerosis.39

As of 2024, there is no conclusive clinical evidence for AGEs having a pathological role in aging diseases, and no causality has been demonstrated between foods, AGEs, and onset of aging or age-related diseases.40

Reactivity

Proteins are usually glycated through their lysine residues.4142 In humans, histones in the cell nucleus are richest in lysine, and therefore form the glycated protein N(6)-Carboxymethyllysine.43

A receptor nicknamed RAGE, from receptor for advanced glycation end products, is found on many cells, including endothelial cells, smooth muscle, cells of the immune system [which?] from tissue such as lung, liver, and kidney.4445 This receptor, when binding AGEs, is under preliminary research to determine if it contributes to age- and diabetes-related chronic inflammatory diseases.46

The pathogenesis of this process is hypothesized to activation of the nuclear factor kappa B (NF-κB) following AGE binding.47 NF-κB controls several genes involved in inflammation.48 AGEs can be detected and quantified using bioanalytical and immunological methods.49

Clearance

In clearance, or the rate at which a substance is removed or cleared from the body, it has been found that the cellular proteolysis of AGEs—the breakdown of proteins—produces AGE peptides and "AGE free adducts" (AGE adducts bound to single amino acids). These latter, after being released into the plasma, can be excreted in the urine.50

Nevertheless, the resistance of extracellular matrix proteins to proteolysis renders their advanced glycation end products less conducive to being eliminated.51 While the AGE free adducts are released directly into the urine, AGE peptides are endocytosed by the epithelial cells of the proximal tubule and then degraded by the endolysosomal system to produce AGE amino acids. It is thought that these acids are then returned to the kidney's inside space, or lumen, for excretion. 52 AGE free adducts are the major form through which AGEs are excreted in urine, with AGE-peptides occurring to a lesser extent53 but accumulating in the plasma of patients with chronic kidney failure.54

Larger, extracellularly derived AGE proteins cannot pass through the basement membrane of the renal corpuscle and must first be degraded into AGE peptides and AGE free adducts. Peripheral macrophage55 as well as liver sinusoidal endothelial cells and Kupffer cells 56 have been implicated in this process, although the real-life involvement of the liver has been disputed. 57

Large AGE proteins unable to enter the Bowman's capsule are capable of binding to receptors on endothelial and mesangial cells and to the mesangial matrix.58 Activation of RAGE induces production of a variety of cytokines, including TNFβ, which mediates an inhibition of metalloproteinase and increases production of mesangial matrix, leading to glomerulosclerosis59 and decreasing kidney function in patients with unusually high AGE levels.

Although the only form suitable for urinary excretion, the breakdown products of AGE — peptides and free adducts — are more aggressive than the AGE proteins from which they are derived, and they can perpetuate related pathology in diabetic patients, even after hyperglycemia has been brought under control.60

See also

References

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  2. Hellwig M, Diel P, Eisenbrand G, et al. (September 2024). "Dietary glycation compounds - implications for human health". Critical Reviews in Toxicology. 54 (8): 485–617. doi:10.1080/10408444.2024.2362985. PMID 39150724. https://www.tandfonline.com/doi/full/10.1080/10408444.2024.2362985 ↩

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  4. Rungratanawanich W, Qu Y, Wang X, et al. (February 2021). "Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury". Experimental and Molecular Medicine. 53 (2): 168–188. doi:10.1038/s12276-021-00561-7. PMC 8080618. PMID 33568752. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8080618 ↩

  5. Hellwig M, Diel P, Eisenbrand G, et al. (September 2024). "Dietary glycation compounds - implications for human health". Critical Reviews in Toxicology. 54 (8): 485–617. doi:10.1080/10408444.2024.2362985. PMID 39150724. https://www.tandfonline.com/doi/full/10.1080/10408444.2024.2362985 ↩

  6. Rungratanawanich W, Qu Y, Wang X, et al. (February 2021). "Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury". Experimental and Molecular Medicine. 53 (2): 168–188. doi:10.1038/s12276-021-00561-7. PMC 8080618. PMID 33568752. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8080618 ↩

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  59. Yan Hd, Li Xz, Xie Jm, et al. (May 2007). "Effects of advanced glycation end products on renal fibrosis and oxidative stress in cultured NRK-49F cells". Chinese Medical Journal. 120 (9): 787–793. doi:10.1097/00029330-200705010-00010. PMID 17531120. https://doi.org/10.1097%2F00029330-200705010-00010 ↩

  60. Gugliucci A, Bendayan M (1996). "Renal fate of circulating advanced glycated end products (AGE): evidence for reabsorption and catabolism of AGE peptides by renal proximal tubular cells". Diabetologia. 39 (2): 149–60. doi:10.1007/BF00403957. PMID 8635666. https://doi.org/10.1007%2FBF00403957 ↩