Mass spectrometric approaches for the identification and quantification of reactive carbonyl species protein adducts

Colzani, Mara; Aldini, Giancarlo; Carini, Marina

doi:10.1016/j.jprot.2013.03.030

Cited by 48 publications

(42 citation statements)

References 142 publications

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“…Spectrophotometric assays have shown a decrease in the free Cys 34 content of albumin following exposure to cigarette smoke extracts in vitro (74,76). The diminution of free Cys 34 content may be attributed to adducts formed with aldehydes or by oxidation with ROS (26,74,77); however, a correlation between the level of adduct formation at Cys 34 of albumin and cigarette smoking constituents remains to established in vivo. Recently, elevated levels of Cys 34 -SO 2 H of albumin were detected in plasma of smokers in a small pilot study (65).…”

Section: Discussionmentioning

confidence: 99%

2-Amino-9H-pyrido[2,3-b]indole (AαC) Adducts and Thiol Oxidation of Serum Albumin as Potential Biomarkers of Tobacco Smoke

Pathak

Bellamri

Wang

et al. 2015

Journal of Biological Chemistry

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Background:The reactivity of A␣C, a tobacco smoke carcinogen, was investigated with DNA and albumin of human hepatocytes. Results: Hepatocytes bioactivate A␣C to metabolites, which adduct to DNA and albumin. Conclusion: Cys 34 and Met 329 of serum albumin are targets for A␣C electrophiles. Significance: A␣C forms macromolecular adducts and induces oxidative stress, which may be contributing factors to liver damage and cancer risk in smokers.

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Section: Discussionmentioning

confidence: 99%

2-Amino-9H-pyrido[2,3-b]indole (AαC) Adducts and Thiol Oxidation of Serum Albumin as Potential Biomarkers of Tobacco Smoke

Pathak

Bellamri

Wang

et al. 2015

Journal of Biological Chemistry

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“…Because of the above mentioned aspects, most of the analytical methods so far proposed are based on a sample preparation procedure aimed at isolating/enriching AGEs and ALEs from native proteins followed by their identification and characterization by off target LC-MS approaches [6], [7]. Molecular recognition/enrichment based on immunoaffinity chromatography techniques is limited due to the chemical diversity of the analytes.…”

Section: Introductionmentioning

confidence: 99%

A capture method based on the VC1 domain reveals new binding properties of the human receptor for advanced glycation end products (RAGE)

et al. 2017

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The Advanced Glycation and Lipoxidation End products (AGEs and ALEs) are a heterogeneous class of compounds derived from the non-enzymatic glycation or protein adduction by lipoxidation break-down products. The receptor for AGEs (RAGE) is involved in the progression of chronic diseases based on persistent inflammatory state and oxidative stress. RAGE is a pattern recognition receptor (PRR) and the inhibition of the interaction with its ligands or of the ligand accumulation have a potential therapeutic effect. The N-terminal domain of RAGE, the V domain, is the major site of AGEs binding and is stabilized by the adjacent C1 domain. In this study, we set up an affinity assay relying on the extremely specific biological interaction AGEs ligands have for the VC1 domain. A glycosylated form of VC1, produced in the yeast Pichia pastoris, was attached to magnetic beads and used as insoluble affinity matrix (VC1-resin). The VC1 interaction assay was employed to isolate specific VC1 binding partners from in vitro generated AGE-albumins and modifications were identified/localized by mass spectrometry analysis. Interestingly, this method also led to the isolation of ALEs produced by malondialdehyde treatment of albumins. Computational studies provided a rational-based interpretation of the contacts established by specific modified residues and amino acids of the V domain. The validation of VC1-resin in capturing AGE-albumins from complex biological mixtures such as plasma and milk, may lead to the identification of new RAGE ligands potentially involved in pro-inflammatory and pro-fibrotic responses, independently of their structures or physical properties, and without the use of any covalent derivatization process. In addition, the method can be applied to the identification of antagonists of RAGE-ligand interaction.

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“…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: 99%

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

Takahashi

Goto

et al. 2015

Chemico-Biological Interactions

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Mass spectrometric approaches for the identification and quantification of reactive carbonyl species protein adducts

Cited by 48 publications

References 142 publications

2-Amino-9H-pyrido[2,3-b]indole (AαC) Adducts and Thiol Oxidation of Serum Albumin as Potential Biomarkers of Tobacco Smoke

2-Amino-9H-pyrido[2,3-b]indole (AαC) Adducts and Thiol Oxidation of Serum Albumin as Potential Biomarkers of Tobacco Smoke

A capture method based on the VC1 domain reveals new binding properties of the human receptor for advanced glycation end products (RAGE)

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

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