Cited by 163Advanced Glycation End Products researchChronic Kidney Disease and DiabetesRenal Diseases and Glomerulopathies

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Advanced glycation end products mediated cellular and molecular events in the pathology of diabetic nephropathy

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Kumar Pasupulati, Anil, Chitra, P. Swathi, Reddy, G. Bhanuprakash·2016·Biomolecular Concepts

DOI 10.1515/bmc-2016-0021

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Abstract

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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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
ORCID: 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
DOI: 10.1515/bmc-2016-0021
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: cc-by-nc-nd
creativecommons.org/licenses/by-nc-nd/3.0/ (unspecified)
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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Advanced glycation end products mediated cellular and molecular events in the pathology of diabetic nephropathy

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