Abstract
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.
Similar content being viewed by others
Abbreviations
- ADH:
-
alcohol dehydrogenase
- DDT:
-
threo-1,4-dimercapto-2,3-butanediol
- EDTA:
-
ethylenediaminetetraacetic acid
- GSH:
-
reduced glutathione
- GSSG:
-
oxidized glutathione
- GST:
-
glutathione S-transferase
- HPL:
-
hydroperoxide lyase
- JA:
-
jasmonic acid
- LOX:
-
lipoxygenase
- MeJA:
-
methyl jasmonate
- NADH:
-
nicotinamide adenine dinucleotide reduced form
- SDS-PAGE:
-
sodium dodecyl sulfate-polyacrylamide gel electrophoresis
References
Alscher, R.G.: Biosynthesis and antioxidant function of glutathione in plants.-Physiol. Plant. 77: 457–464, 1989.
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.
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.
Blee, E.: Phytooxylipins and plant defense reactions.-Progress Lipid Res. 37: 33–72, 1998.
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.
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.
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.
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.
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.
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.
Fujita, M., Hossain, M.Z.: Modulation of pumpkin glutathione S-transferases by aldehydes and related compounds.-Plant Cell Physiol. 44: 481–490, 2003.
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.
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.
Howe, G.A., Schilmiller, A.L.: Oxylipin metabolism in response to stress.-Curr. Opinion Plant Biol. 5: 230–236, 2002.
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.
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.
Mannervik, B., Danielson, U.H.: Glutathione transferases — structure and catalytic activity.-CRC Crit. Rev. Biochem. 23: 283–337, 1988.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Vick, B.A.: A spectrophotometric assay for hydroperoxide lyase.-Lipids 26: 315–320, 1991.
Wilce, M.C.J., Parker, M.W.: Structure and function of glutathione S-transferases.-Biochim. biophys. Acta 1205: 1–18, 1994.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Hossain, M.Z., Hossain, M.D. & Fujita, M. Induction of pumpkin glutathione S-transferases by different stresses and its possible mechanisms. Biol Plant 50, 210–218 (2006). https://doi.org/10.1007/s10535-006-0009-1
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/s10535-006-0009-1