Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
, 10 (2), 389-406

Protein Carbonylation, Cellular Dysfunction, and Disease Progression

Affiliations
Review

Protein Carbonylation, Cellular Dysfunction, and Disease Progression

Isabella Dalle-Donne et al. J Cell Mol Med.

Abstract

Carbonylation of proteins is an irreversible oxidative damage, often leading to a loss of protein function, which is considered a widespread indicator of severe oxidative damage and disease-derived protein dysfunction. Whereas moderately carbonylated proteins are degraded by the proteasomal system, heavily carbonylated proteins tend to form high-molecular-weight aggregates that are resistant to degradation and accumulate as damaged or unfolded proteins. Such aggregates of carbonylated proteins can inhibit proteasome activity. Alarge number of neurodegenerative diseases are directly associated with the accumulation of proteolysis-resistant aggregates of carbonylated proteins in tissues. Identification of specific carbonylated protein(s) functionally impaired and development of selective carbonyl blockers should lead to the definitive assessment of the causative, correlative or consequential role of protein carbonylation in disease onset and/or progression, possibly providing new therapeutic approaches.

Similar articles

See all similar articles

Cited by 178 PubMed Central articles

See all "Cited by" articles

References

    1. Thannickal VJ, Fanburg BL. Reactive oxygen species in cell signaling. Am J Physiol Lung Cell Mol Physiol. 2000;279:L1005–28. - PubMed
    1. Moldovan L, Moldovan NI. Oxygen free radicals and redox biology of organelles. Histochem Cell Biol. 2004;122:395–412. - PubMed
    1. Davies MJ, Fu S, Wang H, Dean RT. Stable markers of oxidant damage to proteins and their application in study of human disease. Free Radic Biol Med. 1999;27:1151–61. - PubMed
    1. Cabiscol E, Ros J. Oxidative damage to proteins: Structural modifications and consequences in cell function. In: Dalle-Donne I, Scaloni A, Butterfield DA, editors. Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Disease. Hoboken: John Wiley & Sons, Inc; 2006. pp. 399–471.
    1. Levine RL, Moskovitz J, Stadtman ER. Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life. 2000;50:301–7. - PubMed

Publication types

LinkOut - more resources

Feedback