Modification of <i>Cytochrome c</i> by 4-hydroxy- 2-nonenal: Evidence for histidine, lysine, and arginine-aldehyde adducts

Isom, Amanda; Barnes, Stephen; Wilson, Landon; Kirk, Marion; Coward, Lori; Darley‐Usmar, Victor

doi:10.1016/j.jasms.2004.03.013

Cited by 134 publications

(97 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The reaction of cytochrome C with HNE had been examined previously by Isom, et al, who showed that HNE formed several adducts including a Michael adduct on H 33 (20). We confirmed their finding, and also showed that this adduct is the initial product formed in the reaction of HNE with cytochrome C. Under our conditions HNE was, along with EDE, the least reactive of the aldehydes; no adduct was observed at molar ratios less than 2:1 HNE:cytochrome C. In addition at a 5:1molar ratio of HNE to cytochrome C, a substantial amount of unreacted protein remained.…”

Section: Discussionmentioning

confidence: 99%

Covalent Adducts Arising from the Decomposition Products of Lipid Hydroperoxides in the Presence of Cytochrome c

Williams

Wishnok

Tannenbaum

2007

Chem. Res. Toxicol.

View full text Add to dashboard Cite

Polyunsaturated fatty acids can be converted to lipid hydroperoxides through non-enzymatic and enzymatic pathways. The prototypic ω-6 lipid hydroperoxide 13-hydroperoxy-octadecadienoic acid (13-HPODE) decomposes homolytically to form highly reactiveα,β-unsaturated aldehydes, such as 9,12-dioxo-10(E)-dodecenoic acid (DODE), 4-oxo-2(E)-nonenal (ONE), 4,5-epoxy-2(E)-decenal (EDE), and 4-hydroxy-2(E)-nonenal (HNE), that can form covalent adducts with DNA. Both 4-oxo-2 (E)-nonenal and 4-hydroxy-2(E)-nonenal can also modify proteins to form products that can potentially serve as biomarkers of lipid hydroperoxide-mediated macromolecule damage. In this study cytochrome C was used to identify and characterize the modification sites individually for each of these aldehydes and also to determine the most abundant adduct formed following decomposition of 13-HPODE. The adducts were characterized by ESI-TOF/MS analysis of the intact proteins and by a combination of ESI-ion-trap/MS n and quadrupole-TOF/MS/MS analysis of the tryptic and chymotryptic peptides.

show abstract

Section: Discussionmentioning

confidence: 99%

Covalent Adducts Arising from the Decomposition Products of Lipid Hydroperoxides in the Presence of Cytochrome c

Williams

Wishnok

Tannenbaum

2007

Chem. Res. Toxicol.

View full text Add to dashboard Cite

show abstract

“…Both the Az-and Al-HNE probes are comparable in the proteins they modify and are similar in reactivity with peptides and toxicity in cells. One discrepancy between the in vitro and in vivo studies was the use of NaCNBH 3 following cell lysis to stabilize Az-and Al-HNE Schiff base adducts on Lys residues of proteins (47). However, reversible Michael adducts on Lys residues must be stabilized with NaBH 4 (14).…”

mentioning

confidence: 99%

Identification of Protein Targets of 4-Hydroxynonenal Using Click Chemistry for ex Vivo Biotinylation of Azido and Alkynyl Derivatives

Vila

Tallman

Jacobs

et al. 2008

Chem. Res. Toxicol.

189

270

View full text Add to dashboard Cite

Polyunsaturated fatty acids (PUFA) are primary targets of free radical damage during oxidative stress. Diffusible electrophilic R, -unsaturated aldehydes, such as 4-hydroxynonenal (HNE), have been shown to modify proteins that mediate cell signaling (e.g., IKK and Keap1) and alter gene expression pathways responsible for inducing antioxidant genes, heat shock proteins, and the DNA damage response. To fully understand cellular responses to HNE, it is important to determine its protein targets in an unbiased fashion. This requires a strategy for detecting and isolating HNE-modified proteins regardless of the nature of the chemical linkage between HNE and its targets. Azido or alkynyl derivatives of HNE were synthesized and demonstrated to be equivalent to HNE in their ability to induce heme oxygenase induction and induce apoptosis in colon cancer (RKO) cells. Cells exposed to the tagged HNE derivatives were lysed and exposed to reagents to effect Staudinger ligation or copper-catalyzed Huisgen 1,3 dipolar cycloaddition reaction (click chemistry) to conjugate HNE-adducted proteins with biotin for subsequent affinity purification. Both strategies yielded efficient biotinylation of tagged HNE-protein conjugates, but click chemistry was found to be superior for the recovery of biotinylated proteins from streptavidincoated beads. Biotinylated proteins were detected in lysates from RKO cell incubations with azido-HNE at concentrations as low as 1 µM. These proteins were affinity purified with streptavidin beads, and proteomic analysis was performed by linear ion trap mass spectrometry. Proteomic analysis revealed a dose-dependent increase in labeled proteins with increased sequence coverage at higher concentrations. Several proteins involved in stress signaling (heat shock proteins 70 and 90 and the 78-kDa glucoseregulated protein) were selectively adducted by azido-and alkynyl-HNE. The use of azido and alkynyl derivatives in conjunction with click chemistry appears to be a valuable approach for the identification of the protein targets of HNE.

show abstract

“…A common analytical approach includes a stabilization step by reduction with borohydride (NaBH 4 ) prior to protein digestion (240). MS studies with non-reduced peptide adducts have demonstrated that the major product ions upon tandem MS fragmentation result from the neutral loss of the aldehyde residues, difficulting the assignment of the modification site (241,242). Ultimately, this chemical property may provide useful information through neutral loss dependent ion selection for MS/MS peptide identification or data-dependent neutral-loss driven MS3 acquisition (88).…”

Section: Oxidation Of Non-sulphur Containing Residuesmentioning

confidence: 99%

Post-translational Modifications and Mass Spectrometry Detection

Silva

Vitorino

Domingues

et al. 2013

Free Radical Biology and Medicine

114

View full text Add to dashboard Cite

In this review, we provide a comprehensive bibliographic overview of the role of mass spectrometry and the recent technical developments in the detection of post-translational modifications (PTMs). We briefly describe the principles of mass spectrometry for detecting PTMs and the protein and peptide enrichment strategies for PTM analysis, including phosphorylation, acetylation and oxidation. This review presents a bibliographic overview of the scientific achievements and the recent technical development in the detection of PTMs is provided. In order to ascertain the state of the art in mass spectrometry and proteomics methodologies for the study of PTMs, we analyzed all the PTM data introduced in the Universal Protein Resource (UniProt) and the literature published in the last three years. The evolution of curated data in UniProt for proteins annotated as being posttranslationally modified is also analyzed. Additionally, we have undertaken a careful analysis of the research articles published in the years 2010 to 2012 reporting the detection of PTMs in biological samples by mass spectrometry.

show abstract

Modification of Cytochrome c by 4-hydroxy- 2-nonenal: Evidence for histidine, lysine, and arginine-aldehyde adducts

Cited by 134 publications

References 34 publications

Covalent Adducts Arising from the Decomposition Products of Lipid Hydroperoxides in the Presence of Cytochrome c

Covalent Adducts Arising from the Decomposition Products of Lipid Hydroperoxides in the Presence of Cytochrome c

Identification of Protein Targets of 4-Hydroxynonenal Using Click Chemistry for ex Vivo Biotinylation of Azido and Alkynyl Derivatives

Post-translational Modifications and Mass Spectrometry Detection

Contact Info

Product

Resources

About