The electrophile responsive proteome: Integrating proteomics and lipidomics with cellular function

Higdon, Ashlee N.; Landar, Aimee; Barnes, Stephen; Darley-Usmar, Victor M.

doi:10.1089/ars.2012.4523

Cited by 53Redox biology and oxidative stressAntioxidant Activity and Oxidative StressGenomics, phytochemicals, and oxidative stress

The electrophile responsive proteome: Integrating proteomics and lipidomics with cellular function

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Higdon, Ashlee N., Landar, Aimee, Barnes, Stephen, Darley-Usmar, Victor M.·2012·Antioxidants & Redox Signaling

DOI 10.1089/ars.2012.4523PMC PMC3448939

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Abstract

SIGNIFICANCE: The process of lipid peroxidation is emerging as an important mechanism that mediates the post-translational modification of proteins. Through advanced analytical techniques, lipidomics is now emerging as a critical factor in our understanding of the pathology of a broad range of diseases. RECENT ADVANCES: During enzymatic or nonenzymatic lipid peroxidation, the simple structure of an unsaturated fatty acid is converted to an oxylipidome, many members of which are electrophilic and form the reactive lipid species (RLS). This aspect of lipid biology is particularly important, as it directly connects lipidomics with proteomics through the post-translational modification of a sub-proteome in the cell. This arises, because the electrophilic members of the oxylipidome react with proteins at nucleophilic amino-acid residues and so change their structure and function to form electrophile-responsive proteomes (ERP). CRITICAL ISSUES: Biological systems have relatively few but well-defined and mechanistically distinct pro-oxidant pathways generating RLS. Defining the ERPs and the mechanisms underlying their formation and action has been a major focus for the field of lipidomics and redox signaling. FUTURE DIRECTIONS: We propose that a unique oxylipidome can be defined for specific oxidants and will predict the biological responses through the reaction with proteins to form a specific ERP. In this review, we will describe the ERPs that modulate antioxidant and anti-inflammatory protective pathways, including the activation of Keap1/Nrf2 and the promotion of cell death through interactions with mitochondria.

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OH-mediated allylic hydrogen atom abstraction from unsaturated lipid acyl chains initiates lipid peroxidation, leading to highly reactive nucleophilic unsaturated aldehydes such as 4-hydroxynonenal.
“while OH-mediated allylic hydrogen atom abstraction from unsaturated lipid acyl chains initiates the processes of lipid peroxidation, leading to highly reactive nucleophilic unsaturated aldehydes such as 4-hydroxynonenal (HNE) (Figure 2A) [8,13,25,26,27].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [25]
The Introduction identifies HNE as a nonspecific lipid-peroxidation product and describes aldehydes formed by free-radical-catalyzed lipid peroxidation. It does not specify OH-mediated allylic hydrogen abstraction as the initiating step. It also calls HNE an electrophile, contrary to the claim’s description of it as nucleophilic. (LLM, conf=0.88)
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Additional file 2 of Integrative proteomic and lipidomic analysis of Kaili Sour Soup-mediated attenuation of high-fat diet-induced nonalcoholic fatty liver disease in a rat model
Cong, S., Li, Z., Yu, L., Liu, Y., Hu, Y., Bi, Y., & Cheng, M. (2021) · Figshare · doi:10.6084/m9.figshare.14196627
Additional file 1 of Integrative proteomic and lipidomic analysis of Kaili Sour Soup-mediated attenuation of high-fat diet-induced nonalcoholic fatty liver disease in a rat model
Cong, S., Li, Z., Yu, L., Liu, Y., Hu, Y., Bi, Y., & Cheng, M. (2021) · Figshare · doi:10.6084/m9.figshare.14196624
Additional file 3 of Integrative proteomic and lipidomic analysis of Kaili Sour Soup-mediated attenuation of high-fat diet-induced nonalcoholic fatty liver disease in a rat model
Cong, S., Li, Z., Yu, L., Liu, Y., Hu, Y., Bi, Y., & Cheng, M. (2021) · Figshare · doi:10.6084/m9.figshare.14196630

Mechanisms of signal transduction mediated by oxidized lipids: the role of the electrophile-responsive proteome
CEASER, E. K., Moellering, D. R., Shiva, S., Ramachandran, A., Landar, A. L., Venkartraman, A., Crawford, J., Patel, R. P., Dickinson, D. A., Ulasova, E., et al. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320151 · Cited by 87 · see citing works
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Vasil’ev, Y. V., Tzeng, S., Huang, L., & Maier, C. S. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21389 · Cited by 44 · see citing works
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Authors: Higdon, A. N., Landar, A., Barnes, S., & Darley-Usmar, V. M.
Affiliations: University of Alabama at Birmingham (US)
Corresponding author: Darley-Usmar, Victor M.
ORCID: Landar, Aimee
Barnes, Stephen
Darley-Usmar, Victor M.
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2012-12
Volume: 17
Issue: 11
Pages: 1580-1589
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2012.4523
PMC: PMC3448939
OpenAlex: W1966628948
Cited by: 51
References: 102
Citations by year: 2025: 1 · 2024: 2 · 2023: 2 · 2021: 4 · 2020: 1 · 2019: 3 · 2018: 6 · 2016: 9 · 2015: 12 · 2014: 5 · 2013: 4 · 2012: 2
FWCI: 0.67
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Antioxidants and Redox Signaling (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (NIH-R01)
National Institute on Alcohol Abuse and Alcoholism (R01-AA13395, R01AA013395)
National Heart, Lung, and Blood Institute (R01HL096638, HL-096638)
National Cancer Institute (U54CA100949)
National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK075867)
National Institute of Environmental Health Sciences (R01 ES10167, R01ES010167)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (P30AR050948)
National Center for Complementary and Integrative Health (P50 AT-00477, P50AT000477, R21AT004661)
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 › Molecular Biology › Genomics, phytochemicals, and oxidative stress
Keywords: lipid peroxidation, electrophilic metabolites, post-translational modification, redox signaling, Nrf2/Keap1 pathway, mitochondria, cell death, antioxidant pathways, anti-inflammatory pathways
MeSH terms: Antioxidants, Fatty Acids, Unsaturated, Humans, Mitochondria, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins, Lipid Peroxidation, Signal Transduction, Cell Death, Proteome

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The electrophile responsive proteome: Integrating proteomics and lipidomics with cellular function

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