Protein carbonylation and metabolic control systems

Jessica M. Curtis, Wendy S. Hahn, Eric K. Long, Joel S. Burrill, Edgar A. Arriaga, David A. Bernlohr

Research output: Contribution to journalReview articlepeer-review

107 Scopus citations


Oxidative stress is linked to the production of reactive lipid aldehydes that non-enzymatically alkylate cysteine, histidine, or lysine residues in a reaction termed protein carbonylation. Reactive lipid aldehydes and their derivatives are detoxified via a variety of phase I and phase II systems, and when antioxidant defenses are compromised or oxidative conditions are increased, protein carbonylation is increased. The resulting modification has been implicated as causative in a variety of metabolic states including neurodegeneration, muscle wasting, insulin resistance, and aging. Although such modifications usually result in loss of protein function, protein carbonylation may be regulatory and activate signaling pathways involved in antioxidant biology and cellular homeostasis.

Original languageEnglish (US)
Pages (from-to)399-406
Number of pages8
JournalTrends in Endocrinology and Metabolism
Issue number8
StatePublished - Aug 2012

Bibliographical note

Funding Information:
We would like to thank members of the Bernlohr and Arriaga groups for comments on this review and to Anthony Hertzel for artwork. This work was supported by NIH grants F32 DK091004 to E.K.L. and RO1 DK084669 to D.A.B.


  • 4-hydroxy trans-2,3-nonenal
  • Carbonylation
  • Metabolism
  • Neurodegeneration
  • Reactive lipid aldehydes
  • Steatosis


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