S-phenylcysteine in albumin as a benzene biomarker.

Bechtold, William E.; Strunk, Michael R.

doi:10.1289/ehp.961041147

Cited by 7 publications

(3 citation statements)

References 4 publications

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“…This mild degradation reaction has been performed in deuterated water to yield monodeutero-benzene and applied to the measurement of albumin-bound benzene (Bechtold & Strunk, 1996). For the quantitative study of styrene oxide adducts to albumin and hemoglobin, the reaction products, a mixture of (AE)-1-and 2-phenylethanol isomers, is extracted from the reaction mixture and the derivatives are separated by GC measured by ECNICI-GC-MS (Ting et al, 1990).…”

Section: Mass Spectrometry and Protein Adductsmentioning

confidence: 99%

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

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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.

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Section: Mass Spectrometry and Protein Adductsmentioning

confidence: 99%

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

show abstract

“…Home made ELISA was elaborated for detection of specific IgG antibodies (Abs) to p-BQ and HQ. The data published concerning covalent binding of p-BQ to nucleophilic aminoacids with formation of 2,5-dihydroxyphenyl-protein derivates ( [4,3,9,13,12,14]) were the basis for the development of ELISA detection technique. Bovine serum albumin 2% (BSA) was applied as a carrier to fix the haptens on the flat-bottom micro plates.…”

Section: Toxic Substance Concentrations In the Workplacementioning

confidence: 99%

Specific immune responses in workers exposed to benzene

Dimitrova

Kostadinova

Marinova

et al. 2005

International Immunopharmacology

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“…As shown in Figure 1, benzene is metabolically transformed to a host of reactive electrophiles, namely, benzene oxide, 1,2-and 1,4-benzoquinone, the muconaldehydes, and benzene diol epoxide (BDE) 1 (reviewed in ref 6), all of which can react with DNA and proteins to form adducts. Because these reactive electrophiles are shortlived, protein adducts in serum albumin and hemoglobin have been used to study the in vivo disposition of benzene oxide and 1,2-and 1,4-benzoquinone (8)(9)(10)(11)(12)(13)(14)(15)(16)(17).…”

Section: Introductionmentioning

confidence: 99%

Characterization and Quantification of Cysteinyl Adducts of Benzene Diol Epoxide

Waidyanatha

Sangaiah

Rappaport

2005

Chem. Res. Toxicol.

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The production of macromolecular adducts of benzene diol epoxide (BDE), a toxic metabolite of benzene, has received little attention despite the demonstrated mutagenicity and carcinogenicity of BDE in rodents. Syn and anti enantiomers of BDE were relatively stable in 0.1 M ammonium acetate buffer, pH 7.6 (half times were greater than 5 h), and showed evidence of pseudo-first-order reactions with albumin (half times were about 4 h) and glutathione (GSH) (half times were about 0.3-0.4 h). Reaction products of BDE isomers with l-cysteine, N-acetyl-l-cysteine, N-acetyl-l-cysteine methyl ester, and GSH were characterized by a combination of electrospray ionization mass spectrometry and/or gas chromatography-mass spectrometry with electron impact ionization of trimethylsilyl derivatives of the adducts. Products corresponded to 1:1 addition of BDE isomers with each nucleophilic species, suggesting that adduction occurred primarily at the free sulfhydryl group. To investigate the disposition of the BDEs in vivo, we developed an assay for cysteinyl BDE-protein adducts. The assay involves enzymatic hydrolysis of the protein followed by derivatization of the released adducts and gas chromatography-negative ion chemical ionization-mass spectrometry. Preliminary applications of the assay showed linear increases in the formation of BDE-GSH adducts in samples of GSH incubated with increasing concentrations of BDE (10-300 microM) and showed the presence of BDE-albumin following incubation of albumin with 10 microM BDE.

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S-phenylcysteine in albumin as a benzene biomarker.

Cited by 7 publications

References 4 publications

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

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

Specific immune responses in workers exposed to benzene

Characterization and Quantification of Cysteinyl Adducts of Benzene Diol Epoxide

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