Cited by 459Advanced Glycation End Products researchPotato Plant ResearchGlycosylation and Glycoproteins Research

Dicarbonyl Intermediates in the Maillard Reaction

THORNALLEY, PAUL J.·2005·Annals of the New York Academy of Sciences

Abstract

A bstract : The complexity of the Maillard reaction arises partly from multiple fragmentation reactions of the sugar moiety, constituting branch points in the reaction progress and establishing many parallel reaction pathways. Reactive intermediates produced by these processes are often α‐oxoaldehydes. The formation of α‐oxoaldehydes enhances and redirects glycating activity in the Maillard reaction since α‐oxoaldehydes are up to 20,000‐fold more reactive than glucose in glycation processes and are predominantly arginine‐directed glycating agents. α‐Oxoaldehydes bypass a requirement for a fructosamine precursor in the formation of advanced glycation end products (AGEs) since α‐oxoaldehydes react with proteins (also nucleotides and basic phospholipids) to form AGEs directly. The major AGE formed from α‐oxoaldehydes is generally a hydroimidazolone with other products—although for glyoxal, N ω ‐carboxymethylarginine is a major product. α‐Oxoaldehyde formation also occurs in the absence of an amine substrate, particularly during heat processing of sugar solutions and lipid peroxidation processes—in the latter case, the glycation adducts are advanced lipoxidation products (ALEs). Hydroimidazolones are quantitatively important AGEs in cellular and extracellular proteins in physiological systems. Hydroimidazolone free adducts are liberated by cellular proteolysis and digestion. They are released into blood plasma for urinary excretion. Modification of arginine residues by α‐oxoaldehydes may be particularly damaging since arginine residues have high‐frequency occurrence in ligand and substrate recognition sites in receptor and enzyme active sites. Along with fructosamine formation, α‐oxoaldehyde intermediates of the Maillard reaction represent a major source of damage to the proteome and genome.

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Crossref · 10.1196/annals.1333.014

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Authors
THORNALLEY, P. J.
Affiliations
University of Essex (GB)
Corresponding author
THORNALLEY, PAUL J.
Venue
Annals of the New York Academy of Sciences
Publisher
Wiley
Published
2005-06
Volume
1043
Issue
1
Pages
111-117
ISSN
  • 0077-8923 (ISSN-L)
  • 1749-6632
OpenAlex
W2077319761
Cited by
459
References
26
Citations by year
2026: 14 · 2025: 20 · 2024: 25 · 2023: 17 · 2022: 29 · 2021: 32 · 2020: 30 · 2019: 26 · 2018: 24 · 2017: 28 · 2016: 27 · 2015: 22 · 2014: 23 · 2013: 22 · 2012: 22
FWCI
8.20
Type
journal article
Language
en
Open access
closed
Locations
  • Annals of the New York Academy of Sciences (publishedVersion)
  • PubMed (publishedVersion)
Funders
Wellcome Trust
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Keywords
Maillard reaction, alpha-oxoaldehydes, advanced glycation end products, hydroimidazolone, advanced lipoxidation end products, glyoxal, arginine modification, fructosamine, lipid peroxidation, protein glycation
MeSH terms
Animals, Carbon, Humans, Imidazoles, Kinetics, Organ Specificity, Pyruvaldehyde, Lipid Peroxidation, Maillard Reaction, Glycation End Products, Advanced, Rats

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