Cited by 961Redox biology and oxidative stressAntioxidant Activity and Oxidative StressAdvanced Glycation End Products research

Protein carbonylation in human diseases

Dalle-Donne, Isabella, Giustarini, Daniela, Colombo, Roberto, Rossi, Ranieri, Milzani, Aldo·2003·Trends in Molecular Medicine

Abstract

Oxidative modifications of enzymes and structural proteins play a significant role in the aetiology and/or progression of several human diseases. Protein carbonyl content is the most general and well-used biomarker of severe oxidative protein damage. Human diseases associated with protein carbonylation include Alzheimer's disease, chronic lung disease, chronic renal failure, diabetes and sepsis. Rapid recent progress in the identification of carbonylated proteins should provide new diagnostic (possibly pre-symptomatic) biomarkers for oxidative damage, and yield basic information to aid the establishment an efficacious antioxidant therapy.

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Registry

Crossref · 10.1016/s1471-4914(03)00031-5

Cites

69 of 69 references verified0 citation errors · 0 not checkable

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  • Protein carbonylation is a stable modification induced by ROS via three pathways: direct oxidation of protein-bound amino acids, oxidative cleavage of the protein backbone, and incorporation of carbonyls from glycoxidation or lipoxidation.

    “Protein carbonylation is a stable modification induced by ROS via three pathways: direct oxidation of protein-bound amino acids, oxidative cleavage of the protein backbone, and incorporation of carbonyls from glycoxidation or lipoxidation [63].”
  • Protein carbonyls are relevant in aging and age-related diseases.

    “together indicating the relevance of protein carbonyls in aging and age-related diseases”
  • Elevated protein carbonyl levels have been found in neurodegenerative disease, such as AD.

    “elevated protein carbonyl levels have been found in neurodegenerative disease, such as AD”
  • Peroxidation of polyunsaturated fatty acids in membrane lipids by ROS can generate highly reactive aldehydes, such as 4-hydroxynonenal, which irreversibly modify proteins by carbonylation.

    “Peroxidation of polyunsaturated fatty acids in membrane lipids60 by ROS can generate highly reactive aldehydes, such as 4-hydroxynonenal, which irreversibly modify proteins by carbonylation.61,62”

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Authors
Dalle-Donne, I., Giustarini, D., Colombo, R., Rossi, R., & Milzani, A.
Affiliations
  • University of Siena (IT)
  • University of Milan (IT)
Venue
Trends in Molecular Medicine
Publisher
Elsevier BV
Published
2003-04
Volume
9
Issue
4
Pages
169-176
ISSN
1471-4914 (ISSN-L)
OpenAlex
W2134724878
Cited by
961
References
69
Citations by year
2026: 17 · 2025: 20 · 2024: 30 · 2023: 45 · 2022: 36 · 2021: 45 · 2020: 50 · 2019: 50 · 2018: 40 · 2017: 41 · 2016: 48 · 2015: 57 · 2014: 54 · 2013: 70 · 2012: 44
FWCI
2.10
Type
journal article
Language
en
Open access
closed
Locations
  • Trends in Molecular Medicine (publishedVersion)
  • PubMed (publishedVersion)
  • Use Siena air (University of Siena) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Keywords
protein carbonylation, oxidative protein damage, oxidative stress biomarkers, Alzheimer's disease, chronic lung disease, chronic kidney disease, diabetes mellitus, sepsis, antioxidant therapy, protein carbonyls
MeSH terms
Antioxidants, Disease, Humans, Oxidation-Reduction, Proteins, Reactive Oxygen Species, Oxidative Stress

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