Biologia plantarum 2014, 58:773-777 | DOI: 10.1007/s10535-014-0412-y

Effect of cadmium on antioxidative enzymes, glutathione content, and glutathionylation in tall fescue

D. Del Buono1,*, T. Mimmo2, R. Terzano3, N. Tomasi4, S. Cesco2
1 Dipartimento di Scienze Agrarie, Alimentari e Ambientali, Università degli Studi di Perugia, Perugia, Italia
2 Facoltà di Scienze e Tecnologie, Libera Università di Bolzano, Bolzano, Italia
3 Dipartimento di Scienze del Suolo, della Pianta e degli Alimenti, Università degli studi di Bari "Aldo Moro", Bari, Italia
4 Dipartimento di Scienze Agrarie e Ambientali, Università di Udine, Udine, Italia

The aim of this work was to assess the effect of different Cd2+concentrations on some antioxidant enzymes in Festuca arundinacea. Increased activities of ascorbate peroxidase, monodehydroascorbate reductase, dehydroascorbate reductase, glutathione S-transferase, and glutathione reductase were ascertained in response to low Cd2+ concentrations (0-20 μM), whereas the enzyme activities were less increased or decreased at a higher Cd2+ dosage (50 μM) and a longer exposure. The content of reduced glutathione (GSH) decreased significantly with increasing Cd2+ concentrations, whereas the content of oxidized glutathione (GSSG) increased proportionally to the amount of Cd2+ applied. Further experiments, performed by incubating the enzyme extracts with oxidized glutathione, evidenced that the addition of GSSG to the incubation mixtures caused significant decreases of some enzymatic activities. Finally, the effect of glutathione S-transferase, FaGST I, extracted from fescue seedlings and purified till homogeneity, on these enzyme activities was investigated. It was found that FaGST I enhanced the decreased enzymatic activities caused by GSSG.

Keywords: ascorbate peroxidase; dehydroascorbate reductase; Festuca arundinacea; glutathione peroxidase; glutathione reductase; glutathione S-transferase; monodehydroascorbate reductase; oxidative stress
Subjects: cadmium; ascorbate peroxidase; peroxidase; glutathione reductase; glutathione S-transferase; tall fescue
Species: Festuca arundinacea

Received: October 4, 2013; Revised: January 22, 2014; Accepted: February 6, 2014; Published: December 1, 2014Show citation

ACS AIP APA ASA Harvard Chicago IEEE ISO690 MLA NLM Turabian Vancouver
Buono, D., Mimmo, T., Terzano, R., Tomasi, N., & Cesco, S. (2014). Effect of cadmium on antioxidative enzymes, glutathione content, and glutathionylation in tall fescue. Biologia plantarum, 58(4), 773-777. doi: 10.1007/s10535-014-0412-y.
Download citation
  • BibTeX (.bib)
  • Bookends (.ris)
  • EasyBib (.ris)
  • EndNote (.enw)
  • EndNote 8 (.xml)
  • ISI WoS (.isi)
  • Medlars (.medlars)
  • Mendeley (.ris)
  • MODS (.xml)
  • Papers (.ris)
  • RefWorks (.txt)
  • RefManager (.ris)
  • RIS (.ris)
  • MS Word (.xml)
  • Zotero (.ris)

    • Open full article

    References

    1. Anderson, M.E.: Determination of glutathione and glutathione disulfide in biological samples. - Methods Enzymol. 113: 548-554, 1985. Go to original source...
    2. Borin, M., Vianello, M., Morari, F., Zanin, G.: Effectiveness of buffer strips in removing pollutants in runoff from a cultivated field in North-East Italy. - Agr. Ecosyst. Environ. 105: 101-114, 2005. Go to original source...
    3. Bradford, G.H., Aruni, B.: Protein S-glutathiolation: redoxsensitive regulation of protein function. - J. mol. cell. Cardiol. 52: 559-567, 2012.
    4. Dalle-Donne, I., Rossi, R., Giustarini, D., Colombo, R., Milzani, A.: S-glutathionylation in protein redox regulation. - Free Radicals Biol. Med. 43: 883-898, 2007.
    5. Del Buono, D., Ioli, G.: Glutathione S-transferases of Italian ryegrass (Lolium multiflorum): activity toward some chemicals, safener modulation and persistence of atrazine and fluorodifen in the shoots. - J. Agr. Food Chem. 59: 1324-1329, 2011. Go to original source...
    6. Del Buono, D., Ioli, G., Nasini, L., Proietti, P.: A comparative study on the interference of two herbicides in wheat and Italian ryegrass and on their antioxidant activities and detoxification rates. - J. Agr. Food Chem. 59: 12109-12115, 2011. Go to original source...
    7. Del Buono, D., Prinsi, B., Espen, L., Scarponi, L.: Triosephosphate isomerases in Italian ryegrass (Lolium multiflorum): characterization and susceptibility to herbicides. - J. Agr. Food Chem. 57: 7924-7930, 2009. Go to original source...
    8. Del Buono, D., Scarponi, L., Espen, L.: Glutathione Stransferases in Festuca arundinacea: identification, characterization and inducibility by safener benoxacor. - Phytochemistry 68: 2614-2624, 2007. Go to original source...
    9. Fornazier, R.F., Ferreira, R.R., Vitòria A.P., Molina, S.M.G., Lea, J.P., Azevedo R.A.: Effects of cadmium on antioxidant enzyme activities in sugar cane. - Biol. Plant. 45: 91-97, 2002. Go to original source...
    10. Gao, X.H., Bedhomme, M., Veyel, D., Zaffagnini, M., Lemaire, S.D.: Methods for analysis of protein glutathionylation and their application to photosynthetic organisms. - Mol. Plant 2: 218-235, 2009. Go to original source...
    11. Hodges, D.M., Andrews, C.J., Johnson, D.A., Hamilton, R.I.: Antioxidant enzyme responses to chilling stress in differentially sensitive inbred maize lines. - J. exp. Bot. 48: 1105-1113, 1997. Go to original source...
    12. Liu, J., Zhang, K., Ren, X., Luo, G., Shen, J.: Bioimprinted protein exhibits glutathione peroxidase activity. - Anal. Chim. Acta 504: 185-189, 2004. Go to original source...
    13. Manevich, Y., Fisher, A.B.: Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. - Free Radicals Biol. Med. 38: 1422-1432, 2005.
    14. Panda, S.K., Chaudhury, I., Khan, M.H.: Heavy metals induce lipid peroxidation and affect antioxidant in wheat leaves. - Biol. Plant. 46: 289-294, 2003. Go to original source...
    15. Pastore, A., Piemonte, F.: S-glutathionylation signaling in cell biology: progress and prospects. - Eur. J. Pharm. Sci. 46: 279-292, 2012. Go to original source...
    16. Rizzardo, C., Tomasi, N., Monte, R., Varanini, Z., Nocito, F.F., Cesco, S., Pinton, R.: Cadmium inhibits the induction of high-affinity nitrate uptake in maize (Zea mays L.) roots. - Planta 236: 1701-1712, 2012. Go to original source...
    17. Rouhier, N., Lemaire, S.D., Jacquot, J.P.: The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation. - Ann. Rev. Plant Biol. 59: 143-166, 2008. Go to original source...
    18. Steinkellner, H., Mun-Sik, K., Helma, C., Ecker, S., Ma, T.H., Horak, O., Kundi, M., Knasmuller, S.: Genotoxic effects of heavy metals: comparative investigation with plant bioassays. - Environ. Mol. Mutagen. 31: 183-191, 1998. Go to original source...
    19. Tew, K.D.: Redox in redux: Emergent roles for glutathione Stransferase P (GSTP) in regulation of cell signaling and Sglutathionylation. - Biochem. Pharmacol. 73: 1257-1269, 2007. Go to original source...
    20. Tew, K.D.: Glutathione S-transferases and S-glutathionylation in cancer. - Biomed. Pharmacotherapy 62: 513-525, 2008. Go to original source...
    21. Tian, S.K., Lu, L.L., Yang, X.E., Huang, H.G., Wang, K., Brown, P.H.: Root adaptations to cadmium-induced oxidative stress contribute to Cd tolerance in the hyperaccumulator Sedum alfredii. - Biol. Plant. 56: 344-350, 2012. Go to original source...
    22. Townsend, D.M., Findlay, V.J., Fazilev, F., Ogle, M., Fraser, J., Saavedra, J.E., Ji, X.H., Keefer, L.K., Tew, K.D.: A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins. - Mol. Pharmacol. 69: 501-508, 2006.
    23. Townsend, D.M., Manevich, Y., He, L., Hutchens, S., Pazoles, C.J., Tew, K.D.: Novel role for glutathione S-Transferase π. Regulator of protein S-glutathionylation following oxidative and nitrosative stress. - J. biol. Chem. 284: 436-445, 2009. Go to original source...
    24. Wang, Y., Hu, H., Li, X.X., Zhang, H.J.: Differential proteomic analysis of cadmium-responsive proteins in wheat leaves. - Biol. Plant. 55: 586-590, 2011. Go to original source...
    25. Zagorchev, L., Seal, C.E., Kranner, I., Odjakova, M.: A central role for thiols in plant tolerance to abiotic stress. - Int. J. Mol. Sci. 14: 7405-7432, 2013. Go to original source...

    Return to the content