Oxidative stress and covalent modification of protein with bioactive aldehydes

Paul A. Grimsrud, Hongwei Xie, Timothy J. Griffin, David A. Bernlohr

Research output: Contribution to journalShort survey

332 Citations (Scopus)

Abstract

The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes.

Original languageEnglish (US)
Pages (from-to)21837-21841
Number of pages5
JournalJournal of Biological Chemistry
Volume283
Issue number32
DOIs
StatePublished - Aug 8 2008

Fingerprint

Protein Carbonylation
Oxidative stress
Aldehydes
Oxidative Stress
Lipids
Carbonylation
Lipid Peroxides
Proteome
Histidine
Hydroxyl Radical
Lysine
Cysteine
Insulin Resistance
Reactive Oxygen Species
Proteins
Antioxidants
Carbohydrates
Inflammation
Addition reactions
DNA

Cite this

Oxidative stress and covalent modification of protein with bioactive aldehydes. / Grimsrud, Paul A.; Xie, Hongwei; Griffin, Timothy J.; Bernlohr, David A.

In: Journal of Biological Chemistry, Vol. 283, No. 32, 08.08.2008, p. 21837-21841.

Research output: Contribution to journalShort survey

@article{c7bd407f8bf3462a8f9447bd52a5743f,
title = "Oxidative stress and covalent modification of protein with bioactive aldehydes",
abstract = "The term {"}oxidative stress{"} links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as {"}protein carbonylation.{"} Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes.",
author = "Grimsrud, {Paul A.} and Hongwei Xie and Griffin, {Timothy J.} and Bernlohr, {David A.}",
year = "2008",
month = "8",
day = "8",
doi = "10.1074/jbc.R700019200",
language = "English (US)",
volume = "283",
pages = "21837--21841",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "32",

}

TY - JOUR

T1 - Oxidative stress and covalent modification of protein with bioactive aldehydes

AU - Grimsrud, Paul A.

AU - Xie, Hongwei

AU - Griffin, Timothy J.

AU - Bernlohr, David A.

PY - 2008/8/8

Y1 - 2008/8/8

N2 - The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes.

AB - The term "oxidative stress" links the production of reactive oxygen species to a variety of metabolic outcomes, including insulin resistance, immune dysfunction, and inflammation. Antioxidant defense systems down-regulated due to disease and/or aging result in oxidatively modified DNA, carbohydrates, proteins, and lipids. Increased production of hydroxyl radical leads to the formation of lipid hydroperoxides that produce a family of α,β-unsaturated aldehydes. Such reactive aldehydes are subject to Michael addition reactions with the side chains of lysine, histidine, and cysteine residues, referred to as "protein carbonylation." Although not widely appreciated, reactive lipids can accumulate to high levels in cells, resulting in extensive protein modification leading to either loss or gain of function. The use of mass spectrometric methods to identify the site and extent of protein carbonylation on a proteome-wide scale has expanded our view of how oxidative stress can regulate cellular processes.

UR - http://www.scopus.com/inward/record.url?scp=52049088770&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=52049088770&partnerID=8YFLogxK

U2 - 10.1074/jbc.R700019200

DO - 10.1074/jbc.R700019200

M3 - Short survey

C2 - 18445586

AN - SCOPUS:52049088770

VL - 283

SP - 21837

EP - 21841

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 32

ER -