Novel lipid hydroperoxide‐derived hemoglobin histidine adducts as biomarkers of oxidative stress

Yocum, Anastasia K.; Oe, Tomoyuki; Yergey, Alfred L.; Blair, Ian A.

doi:10.1002/jms.847

Cited by 32 publications

(32 citation statements)

References 49 publications

(84 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These adducts are relatively unstable and could be further converted into stable products including dihydrofuran, dihydropyrrole, and isomeric 4-ketoamide derivatives originating from the reaction of ONE with lysine (41) and a substituted imidazole derivative with arginine (42). ONE also forms furan derivatives upon its reaction with the cysteine and histidine derivatives (43,44). In our recent study, we carried out a comprehensive study on the identification of the ONE-N-acetyl-L-cysteine adducts and identified several advanced reaction products that originated from the initial Michael adducts (45).…”

Section: Discussionmentioning

confidence: 99%

Identification of a Lipid Peroxidation Product as the Source of Oxidation-specific Epitopes Recognized by Anti-DNA Autoantibodies*

Otaki

Chikazawa

Nagae

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

Lipid peroxidation in tissue and in tissue fractions represents a degradative process, which is the consequence of the production and the propagation of free radical reactions primarily involving membrane polyunsaturated fatty acids, and has been implicated in the pathogenesis of numerous diseases, including systemic lupus erythematosus (SLE). We have found that bovine serum albumin incubated with peroxidized polyunsaturated fatty acids significantly cross-reacted with the sera from MRLlpr mice, a representative murine model of SLE. To identify the active substances responsible for the generation of autoantigenic epitopes recognized by the SLE sera, we performed the activity-guiding separation of a principal source from 13-hydroperoxy-9Z,11E-octadecadienoic acid and identified 4-oxo-2-nonenal (ONE), a highly reactive aldehyde originating from the peroxidation of 6 polyunsaturated fatty acids, as the source of the autoantigenic epitopes. When the age-dependent change in the antibody titer against the ONE-modified protein was measured in the sera from MRL-lpr mice and control MRL-MpJ mice, all of the MRL-lpr mice developed an anti-ONE titer, which was comparable with the anti-DNA titer. Strikingly, a subset of the anti-DNA monoclonal antibodies generated from the SLE mice showing recognition specificity toward DNA cross-reacted with the ONE-specific epitopes. Furthermore, these dual-specific antibodies rapidly bound and internalized into living cells. These findings raised the possibility that the enhanced lipid peroxidation followed by the generation of ONE may be involved in the pathogenesis of autoimmune disorders.

show abstract

Section: Discussionmentioning

confidence: 99%

Identification of a Lipid Peroxidation Product as the Source of Oxidation-specific Epitopes Recognized by Anti-DNA Autoantibodies*

Otaki

Chikazawa

Nagae

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…A peculiar group of lipid-derived activated olefins is that generated by peroxidation of polyunsaturated lipids, which give rise to intermediate oxidation products among which trans-4-hydroxynonenal (HNE) is the most widely studied, due to its reactivity towards several biologically relevant proteins, such as albumin (Aldini et al, 2006(Aldini et al, , 2008, actin c (Toshimitsu et al, 2000;Aldini et al, 2005;Dalle-Donne et al, 2007a;Aldini et al, 2007a) cytochrome c (Isom et al, 2004), insulin (Fenaille, Guy, & Tabet, 2003) and myoglobin (Liu et al, 2003), while research on its more reactive cognate, trans-4-oxononenal (ONE), is more recent (Yocum et al, 2005;Zhu & Sayre, 2007).…”

Section: Mass Spectrometry and Protein Adductsmentioning

confidence: 98%

“…ONE reacts in vitro with human hemoglobin to yield an adduct with histidine residues in the aand b-chains. Mass spectrometric analyses showed that, while reactions performed on separated and denatured globins yielded modifications at His-20 of the a-chain and His-63 b-chain, reaction on the intact Hb tetramer only yielded modification of the latter with a cyclic 2 0 -pentyl-furane lipid-derived portion attached to the t-ring nitrogen of histidine through the 3 0 position (Yocum et al, 2005). Molecular modeling suggests that formation of this adduct seems to be linked to the presence of a specific arrangement of amino acid side chains in the neighborhood of the adducted histidine residue ( 62 AHGK 65 ) which favors cyclization of the lipid keto-aldehyde into a furan ring rather than reaction with the lysine e-amino group to yield a pyrrole derivative.…”

Section: Mass Spectrometry and Protein Adductsmentioning

confidence: 98%

Toward an “omic” physiopathology of reactive chemicals: Thirty years of mass spectrometric study of the protein adducts with endogenous and xenobiotic compounds

Rubino

Pitton

Fabio

et al. 2009

Mass Spectrometry Reviews

109

170

View full text Add to dashboard Cite

Cancer and degenerative diseases are major causes of morbidity and death, derived from the permanent modification of key biopolymers such as DNA and regulatory proteins by usually smaller, reactive molecules, present in the environment or generated from endogenous and xenobiotic components by the body's own biochemical mechanisms (molecular adducts). In particular, protein adducts with organic electrophiles have been studied for more than 30 [see, e.g., Calleman et al., 1978] years essentially for three purposes: (a) as passive monitors of the mean level of individual exposure to specific chemicals, either endogenously present in the human body or to which the subject is exposed through food or environmental contamination; (b) as quantitative indicators of the mean extent of the individual metabolic processing which converts a non-reactive chemical substance into its toxic products able to damage DNA (en route to cancer induction through genotoxic mechanisms) or key proteins (as in the case of several drugs, pesticides or otherwise biologically active substances); (c) to relate the extent of protein modification to that of biological function impairment (such as enzyme inhibition) finally causing the specific health damage. This review describes the role that contemporary mass spectrometry-based approaches employed in the qualitative and quantitative study of protein-electrophile adducts play in the discovery of the (bio)chemical mechanisms of toxic substances and highlights the future directions of research in this field. A particular emphasis is given to the measurement of often high levels of the protein adducts of several industrial and environmental pollutants in unexposed human populations, a phenomenon which highlights the possibility that a number of small organic molecules are generated in the human organism through minor metabolic processes, the imbalance of which may be the cause of "spontaneous" cases of cancer and of other degenerative diseases of still uncharacterized etiology. With all this in mind, it is foreseen that a holistic description of cellular functions will take advantage of new analytical methods based on time-integrated metabolomic measurements of a new biological compartment, the "adductome," aimed at better understanding integrated organism response to environmental and endogenous stressors.

show abstract

“…A number of in vitro studies have shown that ONE and HNE react with various proteins that play key roles in regulating cellular functions such as cytochrome c, thioredoxin, hemoglobin, human serum albumin, and amyloid b [33][34][35]. In most cases, the specific modification sites were identified and the consequent biological effects were elucidated.…”

Section: Discussionmentioning

confidence: 98%

Angiotensin II modification by decomposition products of linoleic acid-derived lipid hydroperoxide

Takahashi

Goto

et al. 2015

Chemico-Biological Interactions

Self Cite

View full text Add to dashboard Cite

Novel lipid hydroperoxide‐derived hemoglobin histidine adducts as biomarkers of oxidative stress

Cited by 32 publications

References 49 publications

Identification of a Lipid Peroxidation Product as the Source of Oxidation-specific Epitopes Recognized by Anti-DNA Autoantibodies*

Identification of a Lipid Peroxidation Product as the Source of Oxidation-specific Epitopes Recognized by Anti-DNA Autoantibodies*

Toward an “omic” physiopathology of reactive chemicals: Thirty years of mass spectrometric study of the protein adducts with endogenous and xenobiotic compounds

Angiotensin II modification by decomposition products of linoleic acid-derived lipid hydroperoxide

Contact Info

Product

Resources

About