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Cited by 641Advanced Glycation End Products researchAntioxidant Activity and Oxidative StressRedox biology and oxidative stress

Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors

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Negre‐Salvayre, A, Coatrieux, C, Ingueneau, C, Salvayre, R·2008·British Journal of Pharmacology
DOI 10.1038/sj.bjp.0707395PMC PMC2199390
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Abstract

Reactive carbonyl compounds (RCCs) formed during lipid peroxidation and sugar glycoxidation, namely Advanced lipid peroxidation end products (ALEs) and Advanced Glycation end products (AGEs), accumulate with ageing and oxidative stress‐related diseases, such as atherosclerosis, diabetes or neurodegenerative diseases. RCCs induce the ‘carbonyl stress’ characterized by the formation of adducts and cross‐links on proteins, which progressively leads to impaired protein function and damages in all tissues, and pathological consequences including cell dysfunction, inflammatory response and apoptosis. The prevention of carbonyl stress involves the use of free radical scavengers and antioxidants that prevent the generation of lipid peroxidation products, but are inefficient on pre‐formed RCCs. Conversely, carbonyl scavengers prevent carbonyl stress by inhibiting the formation of protein cross‐links. While a large variety of AGE inhibitors has been developed, only few carbonyl scavengers have been tested on ALE‐mediated effects. This review summarizes the signalling properties of ALEs and ALE‐precursors, their role in the pathogenesis of oxidative stress‐associated diseases, and the different agents efficient in neutralizing ALEs effects in vitro and in vivo . The generation of drugs sharing both antioxidant and carbonyl scavenger properties represents a new therapeutic challenge in the treatment of carbonyl stress‐associated diseases. British Journal of Pharmacology (2008) 153 , 6–20; doi: 10.1038/sj.bjp.0707395 ; published online 23 July 2007

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  • Formation of carbonylated proteins can induce conformational changes and permanent damage to the polypeptide chain.

    “This results in carbonylated proteins formation, and this can induce conformational changes and permanent damage to the polypeptide chain26.”

    From Air Pollution and Skin Diseases (2025) · cites this paper as [26]

    The Introduction says carbonyl-related compounds form stable adducts and cross-links on proteins, progressively altering their structure and function. This supports structural change and protein damage, but the paper does not establish that the damage to the polypeptide chain is permanent. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • 4-HNE and MDA are prominent precursors of ALE formation.

    “Recent clinical studies focused mainly on reactive intermediates 4-HNE and MDA, which are prominent precursors of ALE formation [174].”

    From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [174]

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Cited by

Sorted by citations

Authors
Negre‐Salvayre, A., Coatrieux, C., Ingueneau, C., & Salvayre, R.
Affiliations
Université Toulouse III - Paul Sabatier (FR)
ORCID
Ingueneau, C
Venue
British Journal of Pharmacology
Publisher
Wiley
Published
2008-01
Volume
153
Issue
1
Pages
6-20
ISSN
  • 0007-1188 (ISSN-L)
  • 1476-5381
DOI
10.1038/sj.bjp.0707395
PMC
PMC2199390
OpenAlex
W2043250256
Cited by
641
References
4
Citations by year
2026: 23 · 2025: 29 · 2024: 26 · 2023: 29 · 2022: 42 · 2021: 37 · 2020: 53 · 2019: 45 · 2018: 36 · 2017: 35 · 2016: 50 · 2015: 40 · 2014: 39 · 2013: 40 · 2012: 29
FWCI
2.77
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 394 d)
Locations
  • British Journal of Pharmacology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
Funders
  • Institut National de la Santé et de la Recherche Médicale
  • Fondation pour la Recherche Médicale
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
advanced glycation end products, carbonyl stress, protein oxidation, protein cross-linking, AGE inhibitors, oxidative stress, atherosclerosis, diabetes mellitus, neurodegenerative diseases, aging, antioxidants, radical scavengers, protein adducts
MeSH terms
Aging, Aldehydes, Animals, Antioxidants, Cardiovascular Diseases, Cell Cycle, Humans, Inflammation, Lipoproteins, LDL, Neoplasms, Oxidation-Reduction, Proteins, Lipid Peroxidation, Signal Transduction, NF-kappa B, Neurodegenerative Diseases

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