Advanced glycation end products in the pathogenesis of chronic kidney disease

Rabbani, Naila; Thornalley, Paul J.

doi:10.1016/j.kint.2017.11.034

Cited by 387Advanced Glycation End Products researchChronic Kidney Disease and DiabetesDialysis and Renal Disease Management

Advanced glycation end products in the pathogenesis of chronic kidney disease

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Rabbani, Naila, Thornalley, Paul J.·2018·Kidney International

DOI 10.1016/j.kint.2017.11.034

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Abstract

Advanced glycation end products (AGEs) are stable posttranslational modifications of proteins formed by the spontaneous reaction with glucose and related metabolites. Important AGEs quantitatively are methylglyoxal (MG)-derived hydroimidazolone MG-H1, N ε-carboxymethyl-lysine (CML), and glucosepane. They contribute to the development of chronic kidney disease (CKD). Cellular proteolysis of AGE-modified proteins forms AGE free adducts, glycated amino acids, which are cleared by the kidneys and excreted in urine. Dietary AGEs mainly supplement the endogenous flux of AGE free adduct formation. AGE free adducts accumulate markedly in plasma with decline in glomerular filtration rate. A key precursor of AGEs is the dicarbonyl metabolite MG, which is metabolized by glyoxalase 1 (Glo1) of the cytoplasmic glyoxalase system. Proteins susceptible to MG modification are collectively called the dicarbonyl proteome. Abnormal increase of MG dicarbonyl stress is a characteristic of CKD, driven by down-regulation of renal Glo1, increasing flux of MG-H1 formation. Protein inactivation and dysfunction linked to the dicarbonyl proteome contributes to CKD development. The receptor for AGEs, RAGE, is important in development of CKD, but its interaction with AGEs in vivo remains enigmatic; other ligands and ternary complexation may be influential. Prevention of diabetic kidney disease (DKD) by overexpression of Glo1 in transgenic animal models has stimulated the development of small-molecule inducers of Glo1 expression, Glo1 inducers, to prevent AGE formation. trans-Resveratrol-hesperetin combination therapy is a Glo1 inducer. In clinical trial it demonstrated a profound improvement in insulin resistance and vascular inflammation. It may find future therapeutic application for treatment of DKD.

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In humans, serum contains AGE peptides and free AGE adducts; AGE peptides are filtered by renal glomeruli and reabsorbed by proximal convoluted tubules and eliminated in urine as free AGE adducts.
“In humans, serum contains AGE peptides and free AGE adducts. AGE peptides are generally filtered by renal glomeruli and further reabsorbed by proximal convoluted tubules and eliminated from the body in the form of free AGE adducts in the urine66,67.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [66]
Increased circulating AGEs can accumulate in renal glomeruli and enhance collagen and laminin production in the extracellular matrix together with proximal tubular senescence, oxidative stress, and inflammatory processes.
“Increased circulating AGEs can accumulate in the renal glomeruli and enhance collagen and laminin production in the extracellular matrix together with proximal tubular senescence, oxidative stress, and inflammatory processes66.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [66]
The AGE-RAGE interaction in the kidney can increase oxidative stress, inflammation, and fibrosis by stimulating CTGF, TGF-β, MAPK, NF-κB and PKC pathways to develop podocyte damage, glomerular hypertrophy, proteinuria, and end-stage renal failure.
“Similarly, the AGE-RAGE interaction in the kidney can increase oxidative stress, inflammation, and fibrosis by stimulating connective tissue growth factor (CTGF), transforming growth factor-β (TGF-β), MAPK, NF-κB and PKC pathways to develop podocyte damage, glomerular hypertrophy, proteinuria, and ultimately end-stage renal failure66,72,73.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [66]

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Rabbani N, Sebekova K, Sebekova K, Jr., et al. Protein glycation, oxidation and nitration free adduct accumulation after bilateral nephrectomy and ureteral ligation. Kidney Internat 2007; 72: 1113-1121.
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Authors: Rabbani, N., & Thornalley, P. J.
Affiliations: University Hospital Coventry (GB)
Corresponding author: Thornalley, Paul J.
ORCID: Rabbani, Naila
Thornalley, Paul J.
Venue: Kidney International
Publisher: Elsevier BV
Published: 2018-04
Volume: 93
Issue: 4
Pages: 803-813
ISSN: 0085-2538 (ISSN-L)
DOI: 10.1016/j.kint.2017.11.034
OpenAlex: W2788736028
Cited by: 387
References: 112
Citations by year: 2026: 31 · 2025: 47 · 2024: 55 · 2023: 58 · 2022: 53 · 2021: 57 · 2020: 45 · 2019: 34 · 2018: 7
FWCI: 4.63
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1461 d)
Locations: Kidney International (publishedVersion)
PubMed (publishedVersion)
Warwick Research Archive Portal (University of Warwick) (acceptedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
Health Sciences › Medicine › Nephrology › Dialysis and Renal Disease Management
Keywords: advanced glycation end products, chronic kidney disease, methylglyoxal, glyoxalase I, receptor for advanced glycation end products, trans-resveratrol, hesperetin, diabetic nephropathy, glycation
MeSH terms: Receptor for Advanced Glycation End Products, Animals, Diabetic Nephropathies, Humans, Kidney, Lactoylglutathione Lyase, Prognosis, Risk Factors, Glycation End Products, Advanced, Disease Progression, Protein Carbonylation, Renal Insufficiency, Chronic, Renal Elimination

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Advanced glycation end products in the pathogenesis of chronic kidney disease

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