Comparison of analytical methods using enzymatic activity, immunoaffinity and selenium-specific mass spectrometric detection for the quantitation of glutathione peroxidase 1

Analytica Chimica Acta

Volumn 1011, Issue , 2018, Pages 11-19

  Sonet, Jordan ^a   Bierla, Katarzyna ^a   Bulteau, Anne Laure ^a   Lobinski, Ryszard ^a   Chavatte, Laurent ^a,b  

^a CNRS   (France)

^b CENTRE INTERNATIONAL DE RECHERCHE EN INFECTIOLOGIE   (France)

Author keywords

Enzymatic assay; Gel electrophoresis; Glutathione peroxidase 1; ICP MS; Laser ablation ICP MS; LC; Selenium; Western blot

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; ELECTROPHORESIS; INDUCTIVELY COUPLED PLASMA MASS SPECTROMETRY; LASER ABLATION; PEPTIDES; QUALITY ASSURANCE; QUALITY CONTROL; SELENIUM; SIZE EXCLUSION CHROMATOGRAPHY;

ENZYMATIC ASSAY; GEL ELECTROPHORESIS; GLUTATHIONE PEROXIDASE; ICP MS; LASER-ABLATION-ICP-MS; WESTERN BLOTS;

MASS SPECTROMETERS;

GLUTATHIONE PEROXIDASE 1; HORSERADISH PEROXIDASE; PYROXYLIN; GLUTATHIONE PEROXIDASE; SELENIUM;

ANALYTIC METHOD; ANTIBODY AFFINITY; ARTICLE; ATOMIC ABSORPTION SPECTROMETRY; ENZYME ACTIVITY; ENZYME ANALYSIS; IMMUNOBLOTTING; IMMUNOREACTIVITY; LASER SURGERY; LIMIT OF DETECTION; MASS SPECTROMETRY; PRIORITY JOURNAL; QUALITY CONTROL; QUANTITATIVE ANALYSIS; SIZE EXCLUSION CHROMATOGRAPHY; VALIDATION PROCESS; ANIMAL; BOVINE; CHEMISTRY; COMPARATIVE STUDY; ENZYME ACTIVATION; ERYTHROCYTE; IMMUNOASSAY; METABOLISM;

ANIMALS; CATTLE; ENZYME ACTIVATION; ERYTHROCYTES; GLUTATHIONE PEROXIDASE; IMMUNOASSAY; MASS SPECTROMETRY; SELENIUM;

EID: 85044572948     PISSN: 00032670     EISSN: 18734324     Source Type: Journal    
DOI: 10.1016/j.aca.2018.01.068     Document Type: Article

References (25)

1. Flohe, L., Gunzler, W.A., Schock, H.H., Glutathione peroxidase: a selenoenzyme. FEBS Lett. 32 (1973), 132–134.
2. Rotruck, J.T., Pope, A.L., Ganther, H.E., Swanson, A.B., Hafeman, D.G., Hoekstra, W.G., Selenium: biochemical role as a component of glutathione peroxidase. Science 179 (1973), 588–590.
3. Kryukov, G.V., Castellano, S., Novoselov, S.V., Lobanov, A.V., Zehtab, O., Guigo, R., Gladyshev, V.N., Characterization of mammalian selenoproteomes. Science 300 (2003), 1439–1443.
4. Touat-Hamici, Z., Legrain, Y., Sonet, J., Bulteau, A.-L., Chavatte, L., Alteration of selenoprotein expression during stress and in aging. S.U. Hatfield, D.L., Tsuji, P.A., Gladyshev, V.N., (eds.) Selenium: its Molecular Biology and Role in Human Health, fourth ed., 2016, Springer Science+Business Media, LLC, New York, NY, 539–551.
5. Sonet, J., Bulteau, A.-L., Chavatte, L., Selenium and selenoproteins in human health and diseases. Michalke, B., (eds.) Metallomics: Analytical Techniques and Speciation Methods, 2016, Wiley-VCH Verlag GmbH & Co, 364–381 KGaA2016.
6. Bulteau, A.-L., Chavatte, L., Update on selenoprotein biosynthesis. Antioxid Redox Signal 23 (2015), 775–794.
7. Brigelius-Flohe, R., Maiorino, M., Glutathione peroxidases. Biochim. Biophys. Acta 1830 (2012), 3289–3303.
8. Touat-Hamici, Z., Legrain, Y., Bulteau, A.-L., Chavatte, L., Selective up-regulation of human selenoproteins in response to oxidative stress. J. Biol. Chem. 289 (2014), 14750–14761.
9. Legrain, Y., Touat-Hamici, Z., Chavatte, L., Interplay between selenium levels, selenoprotein expression, and replicative senescence in WI-38 human fibroblasts. J. Biol. Chem. 289 (2014), 6299–6310.
10. Papp, L.V., Lu, J., Striebel, F., Kennedy, D., Holmgren, A., Khanna, K.K., The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function. Mol. Cell Biol. 26 (2006), 4895–4910.
11. Bermano, G., Nicol, F., Dyer, J.A., Sunde, R.A., Beckett, G.J., Arthur, J.R., Hesketh, J.E., Selenoprotein gene expression during selenium-repletion of selenium-deficient rats. Biol. Trace Elem. Res. 51 (1996), 211–223.
12. Bermano, G., Nicol, F., Dyer, J.A., Sunde, R.A., Beckett, G.J., Arthur, J.R., Hesketh, J.E., Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats. Biochem. J. 311:Pt 2 (1995), 425–430.
13. Paglia, D.E., Valentine, W.N., Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 70 (1967), 158–169.
14. Lei, X.G., Evenson, J.K., Thompson, K.M., Sunde, R.A., Glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase are differentially regulated in rats by dietary selenium. J. Nutr. 125 (1995), 1438–1446.
15. Sonet, J., Mounicou, S., Chavatte, L., Nonradioactive isotopic labeling and tracing of selenoproteins in cultured cell lines. Methods Mol Biol 1661 (2018), 193–203.
16. Callejon-Leblic, B., Rodriguez-Moro, G., Garcia-Barrera, T., Gomez-Ariza, J.L., Simultaneous speciation of selenoproteins and selenometabolites in plasma and serum. Meth. Mol. Biol. 1661 (2018), 163–175.
17. Sonet, J., Mounicou, S., Chavatte, L., Detection of selenoproteins by laser ablation inductively coupled plasma mass spectrometry (LA-ICP MS) in immobilized pH gradient (IPG) strips. Methods Mol Biol 1661 (2018), 205–217.
18. Bianga, J., Touat-Hamici, Z., Bierla, K., Mounicou, S., Szpunar, J., Chavatte, L., Lobinski, R., Speciation analysis for trace levels of selenoproteins in cultured human cells. J Proteomics 108 (2014), 316–324.
19. Bianga, J., Ballihaut, G., Pecheyran, C., Touat, Z., Preud'homme, H., Mounicou, S., Chavatte, L., Lobinski, R., Szpunar, J., Detection of selenoproteins in human cell extracts by laser ablation-ICP MS after separation by polyacrylamide gel electrophoresis and blotting. J Anal Atom Spectrom 27 (2012), 25–32.
20. Latreche, L., Duhieu, S., Touat-Hamici, Z., Jean-Jean, O., Chavatte, L., The differential expression of glutathione peroxidase 1 and 4 depends on the nature of the SECIS element. RNA Biol. 9 (2012), 681–690.
21. Ballihaut, G., Mounicou, S., Lobinski, R., Multitechnique mass-spectrometric approach for the detection of bovine glutathione peroxidase selenoprotein: focus on the selenopeptide. Anal. Bioanal. Chem. 388 (2007), 585–591.
22. Ito, K., Nakagawa, K., Murakami, S., Arakawa, H., Maeda, M., Highly sensitive simultaneous bioluminescent measurement of acetate kinase and pyruvate phosphate dikinase activities using a firefly luciferase-luciferin reaction and its application to a tandem bioluminescent enzyme immunoassay. Anal. Sci. 19 (2003), 105–109.
23. Kricka, L.J., Ultrasensitive immunoassay techniques. Clin. Biochem. 26 (1993), 325–331.
24. Marschall, T.A., Bornhorst, J., Kuehnelt, D., Schwerdtle, T., Differing cytotoxicity and bioavailability of selenite, methylselenocysteine, selenomethionine, selenosugar 1 and trimethylselenonium ion and their underlying metabolic transformations in human cells. Mol. Nutr. Food Res. 60 (2016), 2622–2632.
25. Bishop, D.P., Hare, D.J., Fryer, F., Taudte, R.V., Cardoso, B.R., Cole, N., Doble, P.A., Determination of selenium in serum in the presence of gadolinium with ICP-QQQ-MS. Analyst 140 (2015), 2842–2846.