biologia plantarum

International journal on Plant Life established by Bohumil Němec in 1959

Biologia plantarum 50:210-218, 2006 | DOI: 10.1007/s10535-006-0009-1

Induction of pumpkin glutathione S-transferases by different stresses and its possible mechanisms

M. Z. Hossain1, M. D. Hossain1, M. Fujita1,*
1 Department of Plant Sciences, Faculty of Agriculture, Kagawa University, Miki-cho, Kagawa, Japan

Induction of pumpkin (Cucurbita maxima Duch.) glutathione S-transferases (GSTs) by different stresses and endogenous trans-2-hexenal content were determined in search of a common signal for GST induction. All of the stresses showed significant induction, As2O3 causing the highest induction followed by trans-2-hexenal. The trans-2-hexenal content was highest in trans-2-hexenal-treated seedlings and next-highest in methyl jasmonate-treated seedlings, whereas high temperature- and As2O3-treated seedlings had trans-2-hexenal contents lower than that of control seedlings. Induction of GST, lipoxygenase (LOX) and hydroperoxide lyase (HPL) was compared, since trans-2-hexenal and methyl jasmonate are the products of the LOX pathway. All four stresses showed weak LOX induction, high temperature causing the highest induction. However, only methyl jasmonate caused weak HPL induction. Both antioxidants or oxidants induced GST to different degrees. Glutathione contents of reduced glutathione (GSH) or oxidized glutathione (GSSG)-treated seedlings were significantly higher than the content of control seedlings, whereas those treated with other antioxidants or oxidants had contents similar to or less than control seedlings. The GSH:GSSG ratio was lowest in GSSG-treated seedlings and next-lowest in GSH-treated seedlings. The results of this study suggest that pumpkin GSTs are not induced through a common signalling pathway and that redox perturbation plays a role in pumpkin GST induction.

Keywords: antioxidants; Cucurbita maxima; glutathione; lipoxygenase pathway; oxidants; redox homeostasis; trans-2-hexenal
Subjects: antioxidants, antioxidative enzymes; Cucurbita maxima; glutathione transferase; homeostasis; hydroperoxide lyase; jasmonic acid, jasmonate, methyl jasmonate; lipoxygenase pathway; Northern blot analysis; pumpkin; trans-2-hexenal; Western blot analysis

Received: April 13, 2004; Accepted: September 5, 2005; Published: June 1, 2006  Show citation

ACS AIP APA ASA Harvard Chicago IEEE ISO690 MLA NLM Turabian Vancouver
Hossain, M.Z., Hossain, M.D., & Fujita, M. (2006). Induction of pumpkin glutathione S-transferases by different stresses and its possible mechanisms. Biologia plantarum, 50(2), 210-218. doi: 10.1007/s10535-006-0009-1
Share...
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. Alscher, R.G.: Biosynthesis and antioxidant function of glutathione in plants.-Physiol. Plant. 77: 457-464, 1989. Go to original source...
    2. Bate, N.J., Rothstein, S.J.: C6-volatiles derived from the lipoxygenase pathway induce a subset of defense-related genes.-Plant J. 16: 561-569, 1998. Go to original source...
    3. Bernardi, R., Nali, C., Ginestri, P., Pugliesi, C., Lorenzini, G., Durante, M.: Antioxidant enzyme isoforms on gels in two poplar clones differing in sensitivity after exposure to ozone.-Biol. Plant. 48: 41-48, 2004. Go to original source...
    4. Blee, E.: Phytooxylipins and plant defense reactions.-Progress Lipid Res. 37: 33-72, 1998. Go to original source...
    5. Bradford, M.M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.-Anal. Biochem. 72: 248-254, 1976. Go to original source...
    6. Buwalda, F., De Kok, L.J., Stulen, I., Kuiper, P.J.C.: Cysteine, γ-glutamylcysteine and glutathione contents of spinach leaves as affected by darkness and application of excess sulfur.-Physiol. Plant. 74: 663-668, 1988. Go to original source...
    7. Croft, K.P.C., Voisey, C.R., Slusarenko, A.J.: Mechanism of hypersensitive cell collapse: correlation of increased lipoxygenase activity with membrane damage in leaves of Phaseolus vulgaris (L.) cv. Red Mexican inoculated with avirulent race 1 cells of Pseudomonas syringae pv. phaseolicola.-Physiol. mol. Plant Pathol. 36: 49-62, 1990. Go to original source...
    8. DeRidder, B.P., Dixon, D.P., Beussman, D.J., Edwards, R., Goldsbrough, P.B.: Induction of glutathione S-transferases in Arabidopsis by herbicide safeners.-Plant Physiol. 130: 1497-1505, 2002. Go to original source...
    9. Dixon, D.P., Davis, B.G., Edwards, R.: Functional divergence in the glutathione transferase superfamily in plants - identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana.-J. biol. Chem. 277: 30859-30869, 2002. Go to original source...
    10. Frear, D.S., Swanson, H.R.: Biosynthesis of S-(4-ethylamino-6-isopropylamino-2-s-triazine) glutathione: partial purification and properties of glutathione S-transferase from corn.-Phytochemistry 9: 2123-2132, 1970. Go to original source...
    11. Fujita, M., Hossain, M.Z.: Modulation of pumpkin glutathione S-transferases by aldehydes and related compounds.-Plant Cell Physiol. 44: 481-490, 2003. Go to original source...
    12. Grant, C. M., MacIver, F.H., Dawes, I.W.: Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae.-Curr. Genet. 29: 511-515, 1996. Go to original source...
    13. Hayes, J.D., Pulford, D.J.: The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance.-Crit. Rev. Biochem. mol. Biol. 30: 445-600, 1995. Go to original source...
    14. Howe, G.A., Schilmiller, A.L.: Oxylipin metabolism in response to stress.-Curr. Opinion Plant Biol. 5: 230-236, 2002. Go to original source...
    15. Knorzer, O.C., Durner, J., Boger, P.: Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress.-Physiol. Plant. 97: 388-396, 1996. Go to original source...
    16. Komives, T., Gullner, G., Kiraly, Z.: The ascorbate-glutathione cycle and oxidative stresses in plants.-In: Hatzios, K.K. (ed.): Regulation of Enzymatic Systems Detoxifying Xenobiotics in Plants. Pp. 85-96. Kluwer Academic Publishers, Dordrecht 1997. Go to original source...
    17. Mannervik, B., Danielson, U.H.: Glutathione transferases - structure and catalytic activity.-CRC Crit. Rev. Biochem. 23: 283-337, 1988. Go to original source...
    18. Mauch, F., Dudler, R.: Differential induction of distinct glutathione S-transferases of wheat by xenobiotics and by pathogen attack.-Plant Physiol. 102: 1193-1201, 1993. Go to original source...
    19. Noctor, G., Arisi, A.C.M., Jouanin, L., Valadier, M.H., Roux, Y., Foyer, C.H.: Light-dependent modulation of foliar glutathione synthesis and associated amino acid metabolism in transformed poplar.-Planta 202: 357-369, 1997a. Go to original source...
    20. Noctor, G., Arisi, A.C.M., Jouanin, L., Valadier, M.H., Roux, Y., Foyer, C.H.: The role of glycine in determining the rate of glutathione synthesis in poplars. Possible implications for glutathione production during stress.-Physiol. Plant. 100: 255-263, 1997b. Go to original source...
    21. Noctor, G., Gomez, L., Helene, V., Foyer, C.H.: Interactions between biosynthesis, compartmentation and transport in the control of glutathione homeostasis and signaling.-J. exp. Bot. 53: 1283-1304, 2002. Go to original source...
    22. Noctor, G., Strohm, M., Jouanin, L., Kunert, K.J., Foyer, C.H., Rennenberg, H.: Synthesis of glutathione in leaves of transgenic poplar (Populus tremula × P. alba) overexpressing γ-glutamylcysteine synthetase.-Plant Physiol. 112: 1071-1078, 1996. Go to original source...
    23. Pinkus, R., Weiner, L.M., Daniel, V.: Role of oxidants and antioxidants in the induction of AP-1, NF-κB, and glutathione S-transferase gene expression.-J. biol. Chem. 271: 13422-13429, 1996. Go to original source...
    24. Polidoros, A.N., Scandalios, J.G.: Role of hydrogen peroxide and different classes of antioxidants in the regulation of catalase and glutathione S-transferase gene expression in maize (Zea mays L.).-Physiol. Plant. 106: 112-120, 1999. Go to original source...
    25. Roxas, V.P., Lodhi, S.A., Garrett, D.K., Mahan, J.R., Allen, R.D.: Stress tolerance in transgenic tobacco seedlings that overexpress glutathione S-transferase/glutathione peroxidase.-Plant Cell Physiol. 41: 1229-1234, 2000. Go to original source...
    26. Roxas, V.P., Smith, R.K., Jr., Allen, E.R., Allen, R.D.: Overexpression of glutathione S-transferase/glutathione peroxidase enhances the growth of transgenic tobacco seedlings during stress.-Nat. Biotechnol. 15: 988-991, 1997. Go to original source...
    27. Skorzynska-Polit, E., Drazkiewicz, E., Krupa, Z.: The activity of the antioxidative system in cadmium-treated Arabidopsis thaliana.-Biol. Plant. 47: 71-78, 2003/4. Go to original source...
    28. Strohm, M., Jouanin, L., Kunert, K.J., Pruvost, C., Polle, A., Foyer, C.H., Rennenberg, H.: Regulation of glutathione synthesis in leaves of transgenic poplar (Populus tremula × P. alba) overexpressing glutathione synthetase.-Plant J. 7: 141-145, 1995. Go to original source...
    29. Ulmasov, T., Ohmiya, A., Hagen, G., Guilfoyle, T.: The soybean GH2/4 gene that encodes a glutathione S-transferase has a promoter that is activated by a wide range of chemical agents.-Plant Physiol. 108: 919-927, 1995. Go to original source...
    30. Vancanneyt, G., Sanz, C., Farmaki, T., Paneque, M., Ortego, M., Castanera, P., Sanchez-Serrano, J.J.: Hydroperoxide lyase depletion in transgenic potato plants leads to an increase in lipid performance.-Proc. nat. Acad. Sci. USA 98: 8139-8144, 2001. Go to original source...
    31. Vick, B.A.: A spectrophotometric assay for hydroperoxide lyase.-Lipids 26: 315-320, 1991. Go to original source...
    32. Wilce, M.C.J., Parker, M.W.: Structure and function of glutathione S-transferases.-Biochim. biophys. Acta 1205: 1-18, 1994. Go to original source...

    Return to the content