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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]
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Self-citation
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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