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Cited by 433Advanced Glycation End Products researchProtein Interaction Studies and Fluorescence AnalysisGlycosylation and Glycoproteins Research

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

Rondeau, Philippe, Bourdon, Emmanuel·2011·Biochimie
DOI 10.1016/j.biochi.2010.12.003
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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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Crossref · 10.1016/j.biochi.2010.12.003

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Research works printed but not linked: 5

  1. Thornalley, 1999, The clinical significance of glycation, Clin. Lab., 5–6, 263
  2. Desch, 2001, Aspects biochimiques et analytiques du diagnostic et de la surveillance du diabète, Médecine Nucléaire-Imagerie fonctionnelle et métabolique, 25, 61
  3. Worner, 1990, Non-enzymatic glycation of human serum albumin: influence on the binding kinetics of the benzodiazepine binding sites, J. Clin. Chem. Clin. Biochem., 28, 527
  4. Turk, 1999, Autoantibodies against advanced glycation endproducts (AGEs) in IDDM, Diabet. Suppl., 1, A431
  5. Szwergold, 1997, Identification of a novel protein kinase activity specific for Amadori adducts on glycated proteins, Diabetes, 46, 108A

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Metadata

Authors
Rondeau, P., & Bourdon, E.
Affiliations
University of Reunion Island (RE)
Corresponding author
Rondeau, Philippe
ORCID
Venue
Biochimie
Publisher
Elsevier BV
Published
2011-04
Volume
93
Issue
4
Pages
645-658
ISSN
  • 0037-9042 (ISSN-L)
  • 0300-9084
DOI
10.1016/j.biochi.2010.12.003
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
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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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