ArticleAnalytical chemistry2014
Analysis of covalent modifications of proteins by oxidized phospholipids using a novel method of peptide enrichment.
Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Structural Insights into Recognition and Translocation of Oxidized Phospholipid by CD36 Using Mass Spectrometry, Molecular Docking, Dynamics, and Metadynamics Simulations.Journal of the American Chemical Society · 2025Article
- Structure and Dynamics of Oxidized Lipoproteins In Vivo: Roles of High-Density Lipoprotein.Biomedicines · 2021Review
- Circulating CD36 is increased in hyperlipidemic mice: Cellular sources and triggers of release.Free radical biology & medicine · 2021Article
- A Comprehensive Review on Source, Types, Effects, Nanotechnology, Detection, and Therapeutic Management of Reactive Carbonyl Species Associated with Various Chronic Diseases.Antioxidants (Basel, Switzerland) · 2020Review
- Cross-linking modifications of HDL apoproteins by oxidized phospholipids: structural characterization,The Journal of biological chemistry · 2020Article
- Lipoproteins as targets and markers of lipoxidation.Redox biology · 2019Review
- Unbiased Identification of Proteins Covalently Modified by Complex Mixtures of Peroxidized Lipids Using a Combination of Electrophoretic Mobility Band Shift with Mass Spectrometry.Antioxidants (Basel, Switzerland) · 2018Article
- Characterization of covalent modifications of HDL apoproteins by endogenous oxidized phospholipids.Free radical biology & medicine · 2018Article
- Live-cell imaging approaches for the investigation of xenobiotic-induced oxidant stress.Biochimica et biophysica acta · 2016Review
- Protein lipoxidation: Detection strategies and challenges.Redox biology · 2015Review
- HDL inhibits the effects of oxidized phospholipids on endothelial cell gene expression via multiple mechanisms.Journal of lipid research · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Free radical-induced oxidation of phospholipids contributes significantly to pathologies associated with inflammation and oxidative stress. Detection of covalent interaction between oxidized phospholipids (oxPL) and proteins by LC-MS/MS could provide valuable information about the molecular mechanisms of oxPL effects. However, such studies are very limited because of significant challenges in detection of the comparatively low levels of oxPL-protein adducts in complex biological systems. Current approaches have several limitations, most important of which is the inability to detect protein modifications by naturally occurring oxPL. We now report, for the first time, an enrichment method that can be applied to the global analysis of protein adducts with various naturally occurring oxPL in relevant biological systems. This method exploits intrinsic properties of peptides modified by oxPL, allowing highly efficient enrichment of oxPL-modified peptides from biological samples. Very low levels of oxPL-protein adducts (<2 ppm) were detected using this enrichment method in combination with LC-MS/MS. We applied the method to several model systems, including oxidation of high density lipoprotein (HDL) and interaction of human platelets with a specific oxPL, and demonstrated its extremely high efficiency and productivity. We report multiple new modifications of apolipoproteins in HDL and proteins in human platelets.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.