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Advanced glycation end products mediated cellular and molecular events in the pathology of diabetic nephropathy
Open accessAbstract
Diabetic nephropathy (DN) is a major cause of morbidity and mortality in diabetic patients and a leading cause of end-stage renal disease (ESRD). Degenerative changes such as glomerular hypertrophy, hyperfiltration, widening of basement membranes, tubulointerstitial fibrosis, glomerulosclerosis and podocytopathy manifest in various degrees of proteinuria in DN. One of the key mechanisms implicated in the pathogenesis of DN is non-enzymatic glycation (NEG). NEG is the irreversible attachment of reducing sugars onto free amino groups of proteins by a series of events, which include the formation of Schiff’s base and an Amadori product to yield advanced glycation end products (AGEs). AGE modification of client proteins from the extracellular matrix induces crosslinking, which is often associated with thickening of the basement membrane. AGEs activate several intracellular signaling cascades upon interaction with receptor for AGEs (RAGE), which manifest in aberrant cellular responses such as inflammation, apoptosis and autophagy, whereas other receptors such as AGE-R1, AGE-R3 and scavenger receptors also bind to AGEs and ensue endocytosis and degradation of AGEs. Elevated levels of both serum and tissue AGEs are associated with adverse renal outcome. Increased evidence supports that attenuation of AGE formation and/or inhibition of RAGE activation manifest(s) in improving renal function. This review provides insights of NEG, discusses the cellular and molecular events triggered by AGEs, which manifest in the pathogenesis of DN including renal fibrosis, podocyte epithelial-mesenchymal transition and activation of renin-angiotensin system. Therapies designed to target AGEs, such as inhibitors of AGEs formation and crosslink breakers, are discussed.
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“AGEs also activate NF-κB, MAPK, and protein kinase C (PKC) to promote mesangial proliferative inhibition, hypertrophy, and apoptosis70,71.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [71]
In the citing paper
“In addition, AGEs can be produced in renal mesangial cells and induce the expression of monocyte chemoattractant protein-1 (MCP-1).”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [71]
Citations
Cites
Advanced Glycation End Products: Sparking the Development of Diabetic Vascular Injury
Goldin, A., Beckman, J. A., Schmidt, A. M., & Creager, M. A. (2006) · Circulation · doi:10.1161/circulationaha.106.621854 · Cited by 2,261
Dehydrated Foods, Chemistry of Browning Reactions in Model Systems
Hodge, J. E. (1953) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60015a004 · Cited by 1,979
Neeper, M. P., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y., Elliston, K. O., Stern, D., & SHAW, A. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42138-2 · Cited by 1,545
Understanding RAGE, the receptor for advanced glycation end products
Bierhaus, A., Humpert, P. M., Morcos, M., Wendt, T., Chavakis, T., Arnold, B., Stern, D. M., & Nawroth, P. P. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0688-7 · Cited by 1,297
Advanced glycation end products in foods and a practical guide to their reduction in the diet
Uribarri, J., Woodruff, S., Goodman, S., Cai, W., Chen, X., Pyzik, R., Yong, A., Striker, G. E., & Vlassara, H. (2010) · Journal of the American Dietetic Association · doi:10.1016/j.jada.2010.03.018 · Cited by 1,289
Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
Thornalley, P. J., LANGBORG, A., & Minhas, H. S. (1999) · Biochemical Journal · doi:10.1042/bj3440109 · Cited by 1,209
Role of advanced glycation end products in cellular signaling
Ott, C., Jacobs, K., Haucke, E., Navarrete Santos, A., Grune, T., & Simm, A. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.016 · Cited by 1,150
Aminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-Linking
Brownlee, M., Vlassara, H., Kooney, A., Ulrich, P. C., & Cerami, A. (1986) · Science · doi:10.1126/science.3487117 · Cited by 1,146
Ahmed, M. U., Thorpe, S. R., & Baynes, J. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89188-3 · Cited by 864
Nonenzymatic Browning in Vivo: Possible Process for Aging of Long-Lived Proteins
Monnier, V. M., & Cerami, A. (1981) · Science · doi:10.1126/science.6779377 · Cited by 773
Research works printed but not linked: 1
- Alam S, Ahsan A, Alam S. Newer insights in drugs inhibiting formation and accumulation of advanced glycation end products. J Biochem Tech 2013; 5: 666–72.
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Maithilikarpagaselvi, N., Kanwar, T., Rathore, M., Sreenivasulu, K., Bajpai, N. K., & Banerjee, M. (2024) · Human Gene · doi:10.1016/j.humgen.2024.201322 · Cited by 4
Wu, Y., Zhang, B., Ma, X., Yu, P., Zhou, S., & Wang, X. (2025) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-025-01591-1 · Cited by 5
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Kamel, W. A., Haghi, M., Khosroshahi, H. T., & Dehghan, G. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10846-z · Cited by 3
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Stop the “Vicious Cycle” induced by Glycative Stress.
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Hassan, A. A., Zbaar, S. A., & Khedhair, K. A. (2021) · Indian Journal of Forensic Medicine & Toxicology · doi:10.37506/ijfmt.v15i4.17257 · Cited by 1
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Liu, Z., Chen, J., Sun, L., Li, J., & Sun, H. Q. (2021) · Research Square · doi:10.21203/rs.3.rs-870754/v1
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Si, Y., Huang, Y., Chen, M., Wu, Z., Li, G., Li, H., Ge, P., Liu, H., Zhang, W., & Yan-li, X. (2022) · Current Pharmaceutical Analysis · doi:10.2174/1573412918666220427135241
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李, 燕. (2023) · Advances in Clinical Medicine · doi:10.12677/acm.2023.13102220
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Zahra, H. A. (2025) · Journal of Biological Research - Bollettino della Società Italiana di Biologia Sperimentale · doi:10.4081/jbr.2025.12656
Ahmadirad, H., Farhadnejad, H., Norouzzadeh, M., Jahromi, M. K., Mokhtari, E., Omrani, M., Teymoori, F., Sadeghi, R., Mirmiran, P., & Bagherian, M. (2025) · Cancer Epidemiology · doi:10.1016/j.canep.2025.102807
Li, Y., Zong, A., Xu, C., Liu, L., Zhang, Y., Li, B., Du, F., & Xu, T. (2025) · Food & Function · doi:10.1039/d5fo00867k
Yanardağ, R., Ertik, O., Bal‐Demirci, T., Ülküseven, B., & Tunalı, S. (2025) · Journal of the Turkish Chemical Society Section A Chemistry · doi:10.18596/jotcsa.1734840
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Vyas, K., Chhipa, A. S., Chauhan, A., & Patel, S. S. (2026) · Discover Molecules · doi:10.1007/s44345-026-00071-x
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Metadata
- Authors
- Kumar Pasupulati, A., Chitra, P. S., & Reddy, G. B.
- Affiliations
- Department of Biochemistry, University of Hyderabad, Hyderabad 500 046, India
- National Institute of Nutrition (IN)
- Corresponding author
- Reddy, G. Bhanuprakash
- Venue
- Biomolecular Concepts
- Publisher
- Walter de Gruyter GmbH
- Published
- 2016-11-07
- Volume
- 7
- Issue
- 5-6
- Pages
- 293-309
- ISSN
- 1868-5021 (ISSN-L)
- 1868-503X
- OpenAlex
- W2550737605
- Cited by
- 163
- References
- 110
- Citations by year
- 2026: 7 · 2025: 18 · 2024: 19 · 2023: 21 · 2022: 25 · 2021: 29 · 2020: 19 · 2019: 9 · 2018: 8 · 2017: 8
- FWCI
- 0.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- BioMolecular Concepts (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Defence Research and Development Organisation
- 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 › Renal Diseases and Glomerulopathies
- Keywords
- diabetic nephropathy, advanced glycation end products, glycation, receptor for advanced glycation end products, renal fibrosis, renin-angiotensin system, proteinuria, glomerulosclerosis, inflammation, apoptosis, autophagy
- MeSH terms
- Receptor for Advanced Glycation End Products, Diabetic Nephropathies, Humans, Protein Binding, Renin-Angiotensin System, Signal Transduction, Glycation End Products, Advanced, Podocytes, Epithelial-Mesenchymal Transition, Molecular Targeted Therapy
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