The DOI matches its Crossref record; 226 of the 226 references it cites were found in a registry or an index.
The glycation of albumin: Structural and functional impacts
Abstract
Oxidative stress and protein modifications are frequently observed in numerous disease states. Glucose constitutes a vital nutrient necessary to cellular oxygen metabolism. However, hyperglycemia-associated damage is an important factor in diabetes disorders. Albumin, the major circulating protein in blood, can undergo increased glycation in diabetes. From recent studies, it has become evident that protein glycation has important implications for protein activity, unfolding, and degradation, as well as for cell functioning. After giving a brief overview of the key role of albumin in overall antioxidant defense, this review examines its role as a target of glycation reactions. A synthesis of state of the art methods for measuring and characterizing albumin glycation is detailed. In light of recent data, we then report the impact of glycation on the structure of albumin and its various activities, especially its antioxidant and binding capacities. The biological impact of glycated albumin on cell physiology is also discussed, specifically the role of the protein as a biological marker of diabetes.
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“In addition to long-lived proteins, AGEs can bind to proteins with short half-lives such as serum albumin, thereby activating RAGEs and inducing inflammatory responses followed by protein dysfunction and cell damage34.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [34]
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Advanced Glycation End Products and Diabetic Complications
Singh, V. P., Bali, A., Singh, N., & Jaggi, A. S. (2014) · The Korean Journal of Physiology & Pharmacology · doi:10.4196/kjpp.2014.18.1.1 · Cited by 1,518
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Metadata
- Authors
- Rondeau, P., & Bourdon, E.
- Affiliations
- University of Reunion Island (RE)
- Corresponding author
- Rondeau, Philippe
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 2011-04
- Volume
- 93
- Issue
- 4
- Pages
- 645-658
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- OpenAlex
- W2040634316
- Cited by
- 433
- References
- 226
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 28 · 2023: 24 · 2022: 39 · 2021: 29 · 2020: 37 · 2019: 23 · 2018: 35 · 2017: 34 · 2016: 36 · 2015: 34 · 2014: 38 · 2013: 23 · 2012: 21
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimie (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Ministère de l'Enseignement Supérieur et de la Recherche
- Université de La Réunion
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- albumin glycation, glycated albumin, diabetes mellitus, oxidative stress, protein modification, hyperglycemia, antioxidant defense, protein structure, protein unfolding, protein degradation, binding capacity, diabetes biomarkers
- MeSH terms
- Glycated Serum Albumin, Antioxidants, Diabetes Mellitus, Disease, Glucose, Glycosylation, Humans, Hyperglycemia, Protein Processing, Post-Translational, Serum Albumin, Structure-Activity Relationship, Glycation End Products, Advanced, Reactive Oxygen Species, Oxidative Stress
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