Protein Carbonyl Formation in Blood Plasma by Cephalosporins

Jung, Yoon Young; Chay, Kee-Oh; Song, Dong-up; Yang, Suhui; Lee, Min-wha; Ahn, Byungchan

doi:10.1006/abbi.1997.0268

Cited by 13 publications

(7 citation statements)

References 20 publications

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“…It is an irreversible modification and is a widely used general marker for oxidative damage in proteins . FTSC labelling has previously been used in the detection of protein carbonyls and FTSC‐labelled proteins can be detected without Western blotting . Considering these results, it is plausible that xenobiotics entering animals via gills may cause transient OS resulting in protein glutathionylation and long‐term chronic exposure to pollutants.…”

Section: Resultsmentioning

confidence: 99%

A redox proteomic investigation of oxidative stress caused by benzoylecgonine in the freshwater bivalve Dreissena polymorpha

Pedriali

Riva

Parolini

et al. 2012

Drug Testing and Analysis

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Drugs of abuse and their human metabolites have been recently recognized as emerging environmental contaminants. Notwithstanding the fact that these kinds of compounds share some features with pharmaceuticals, their ecotoxicology has not yet been extensively investigated, although some of their characteristics may potentially threaten aquatic ecosystems. One of the most abundant drugs found in rivers and wastewaters is benzoylecgonine (BE), the main metabolite of cocaine. We applied a redox proteomics approach to evaluate changes in the proteome of Dreissena polymorpha exposed to two different concentrations of BE (0.5 and 1 µg/l). Exposures were performed in vivo for a period of 14 days and the effect of oxidative stress on protein thiol and carbonyl groups in mussel gills were evaluated. One-dimensional electrophoresis did not reveal a reduction in protein thiol content but showed a significant increase of protein carbonylation at both doses tested. Then, protein profiling using two-dimensional gel electrophoresis was performed with subsequent matrix assisted laser desorption/ionization time-of-flight (MALDI-TOF) and TOF/TOF with LIFT technique and linear ion trap combined with orbitrap mass spectrometer (LTQ-Orbitrap). This yielded de novo protein sequences suitable for database searching. These preliminary results and protein identifications obtained suggest that BE causes oxidative stress. Oxidative modifications were detected in differing classes of proteins such as those of the cytoskeleton, energetic metabolism and stress response.

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Section: Resultsmentioning

confidence: 99%

A redox proteomic investigation of oxidative stress caused by benzoylecgonine in the freshwater bivalve Dreissena polymorpha

Pedriali

Riva

Parolini

et al. 2012

Drug Testing and Analysis

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“…Statistics: one-way ANOVA (P < 0.05) followed by Newman-Keuls test; * P < 0.05 for STZ-diabetic group versus control group for the corresponding PC data; § Nonsignificant for the same samples assayed with NBDH versus DNPH. the analysis of protein carbonyls such as fluorescein-5-thiosemicarbazide [43,44] and fluorescence hydroxylamine [45]. But as for DNPH, the limitation of these probes for carbonyl content quantification involves the difficulty to completely remove the excess of probes following TCA precipitation or gel filtration [46].…”

Section: Resultsmentioning

confidence: 99%

Fluorimetric screening assay for protein carbonyl evaluation in biological samples

Stocker

Ricquebourg

Vidal

et al. 2015

Analytical Biochemistry

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“…Two visible-wavelength fluorescence probes have been reported in the literature for the analysis of protein carbonyls: fluorescein-5-thiosemicarbazide (FTC) [21,72,73] and Alexa 488 fluorescence hydroxylamine (FHA, Invitrogen) [22]. Both probes are commercially available and have been successfully used in 2D gel-based proteomic analysis of carbonylated proteins.…”

Section: Analysis Of Carbonylated Proteins Relies On the Use Of Chementioning

confidence: 99%

Chemical probes for analysis of carbonylated proteins: A review

Forster

2011

Journal of Chromatography B

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Protein carbonylation is a major form of protein oxidation and is widely used as an indicator of oxidative stress. Carbonyl groups do not have distinguishing UV or visible, spectrophotometric absorbance/fluorescence characteristics and thus their detection and quantification can only be achieved using specific chemical probes. In this paper, we review the advantages and disadvantages of several chemical probes that have been and are still being used for protein carbonyl analysis. These probes include 2, 4-dinitrophenylhydazine (DNPH), tritiated sodium borohydride ([3H]NaBH4), biotin-containing probes, and fluorescence probes. As our discussions lean toward gel-based approaches, utilizations of these probes in 2D gel-based proteomic analysis of carbonylated proteins are illustrated where applicable. Analysis of carbonylated proteins by ELISA, immunofluorescent imaging, near infrared fluorescence detection, and gel-free proteomic approaches are also discussed where appropriate. Additionally, potential applications of blue native gel electrophoresis as a tool for first dimensional separation in 2D gel-based analysis of carbonylated proteins are discussed as well.

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Protein Carbonyl Formation in Blood Plasma by Cephalosporins

Cited by 13 publications

References 20 publications

A redox proteomic investigation of oxidative stress caused by benzoylecgonine in the freshwater bivalve Dreissena polymorpha

A redox proteomic investigation of oxidative stress caused by benzoylecgonine in the freshwater bivalve Dreissena polymorpha

Fluorimetric screening assay for protein carbonyl evaluation in biological samples

Chemical probes for analysis of carbonylated proteins: A review

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