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Glyceraldehyde-3-phosphate dehydrogenase as a biochemical marker of cytotoxicity by vinyl sulfones in cultured murine spleen lymphocytes

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Abstract

Recently, vinyl sulfones have been observed to selectively inhibit glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is an important ATP-generating enzyme in glycolysis. The possibility of using GAPDH as a biochemical parameter of cytotoxicity by vinyl sulfones was investigated using mouse lymphocytes. Incubation of lymphocyte GAPDH with ethylvinyl sulfone resulted in a pseudo-first-order loss of enzyme activity. The exposure of lymphocytes to ethylvinyl sulfone resulted in the decrease of GAPDH activity followed by ATP depletion and cell death, which were both dependent on the concentration of ethylvinyl sulfone. A further study on the time-dependent change indicated that cell death was preceded by ATP loss. Compared to ethylvinyl sulfone, divinyl sulfone was more than 8 times more potent in causing either ATP depletion or cell death.

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Abbreviations

DTT:

dithiothreitol

GAPDH:

glyceraldehyde-3-phosphate dehydrogenase

NAD:

nicotinamide adenine dinucleotide

References

  • Andreoli SP. Mechanisms of endothelial cell ATP depletion after oxidant injury. Pediatr Res. 1989;25:97–101.

    Google Scholar 

  • Bastyns K, Engelborghs Y. The interaction of acrylamide with glyceraldehyde-3-phosphate dehydrogenase. Structural modifications in the enzyme studies by fluorescence techniques. Photochem Photobiol. 1992;55:9–16.

    Google Scholar 

  • Hartmann S, Neeff J, Heer V, Mecke D. Arenamycin: a specific inhibitor of glycolysis. FEBS Lett. 1978;93:339–42.

    Google Scholar 

  • Hyslop PA, Hinshaw DB, Halsey WA Jr et al. Mechanisms of oxidant-mediated cell injury. J Biol Chem. 1989;263:1665–75.

    Google Scholar 

  • Kitz RJ, Braswell LM, Ginsburg S. On the question: is acetylcholinesterase an allosteric protein. Mol Pharmacol. 1970;6:108–21.

    Google Scholar 

  • Mol MAE, VanDe Ruit ABC, Kluivers AW. NAD levels and glucose uptake of cultured human epidermal cells exposed to sulfur mustard. Toxicol Appl Pharmacol. 1989;98:159–65.

    Google Scholar 

  • Porath J, Laas T, Janson J-C. Agar derivatives for chromatography, electrophoresis and gel-bound enzymes. III. Rigid agarose gels cross-linked with divinyl sulfone. J Chromatogr. 1975;103:49–52.

    Google Scholar 

  • Rosenberg Y, Lafrage-Frayssinet C. Inhibitory effect ofFusarium T2-toxin on lymphoid DNA and protein synthesis. Toxicol Appl Pharmacol. 1973;70:283–8.

    Google Scholar 

  • Scheek RM, Slater EC. Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. Methods Enzymol. 1982;89:305–9.

    Google Scholar 

  • Sok D-E, Choi D-S, Kim Y-B, Lee Y-H, Cha S-H. Selective inactivation of glyceraldehyde-3-phosphate dehydrogenase by vinyl sulfones. Biochem Biophys Res Commun. 1993;195: 1224–9.

    Google Scholar 

  • Wormser U. Toxicology of mustard gas. Trends Pharmacol Sci 1991;12:164–7.

    Google Scholar 

Download references

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Choi, D.S., Kim, Y.B., Lee, Y.H. et al. Glyceraldehyde-3-phosphate dehydrogenase as a biochemical marker of cytotoxicity by vinyl sulfones in cultured murine spleen lymphocytes. Cell Biol Toxicol 11, 23–28 (1995). https://doi.org/10.1007/BF00769989

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  • DOI: https://doi.org/10.1007/BF00769989

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