Skip to main content
SpringerLink
Log in

Effect of Furostanol Glycosides from Dioscorea deltoidea on Redox State of Alfalfa Cells In Vitro

  • RESEARCH PAPERS
  • Published:
Russian Journal of Plant Physiology Aims and scope Submit manuscript

Abstract

The effect of exogenous furostanol glycosides (FG) on the activity of redox enzymes was investigated in suspension cell culture of alfalfa (Medicago sativa L.). It was shown that 60-min-long treatment of alfalfa cells with FG at a concentration of 10–5 M triggered formation of ROS and activated enzymes of the antioxidant complex: superoxide dismutase and guaiacol-dependent peroxidase where the highest activity was associated with ion-bound fraction. Application of inhibitor of NADPH oxidase diphenyliodonium chloride showed that ROS are generated in the presence of FG by NADPH oxidase of plasma membrane. It was found that treatment of alfalfa in vitro cells with FG elevated activity of the key enzyme of pentose phosphate pathway: glucose-6-phosphate dehydrogenase (G-6-P DH) and glutathione reductase. A relationship was revealed between the operation of G-6-P DH, NADPH oxidase, and glutathione reductase. It is assumed that, owing to suppression of one of the main consumers of NADPH (NADPH oxidase), a rise in the activity of glutathione reductase may eliminate the inhibition of G-6-P DH. Under hyperosmotic stress, FG improved the viability of alfalfa cells in vitro to 70%, whereas it was only 24% in control material. At the same time, viability reached 90% in reference cells without treatment. Such an effect of FG became apparent as a result of elevation in activity of aldehyde dehydrogenase, reduction in lipid peroxidation (by 24%), and activation of antioxidant enzymes. Adaptation mechanisms operating on the level of redox systems are discussed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1.
Fig. 2.
Fig. 3.
Fig. 4.
Fig. 5.

Similar content being viewed by others

REFERENCES

  1. Sokolov, Yu.A., Elisitory i ikh primenenie v rastenievodstve (Elicitors and Their Application in Crop Production), Minsk: Belarusskaya Navuka, 2016.

  2. Volkova, L.A., Urmantseva, V.V., Burgutin, A.B., and Nosov, A.M., Sensitivity of antioxidant status of plant cells to furostanol glycosides, Russ. J. Plant Physiol., 2016, vol. 63, p. 784.

    Article  Google Scholar 

  3. Volkova, L.A., Urmantseva, V.V., Burgutin, A.B., and Nosov, A.M., Characteristics of eliciting effects of furostanol glycosides on cultured yam cells, Russ. J. Plant Physiol., 2018, vol. 65, p. 427.

    Article  CAS  Google Scholar 

  4. Volkova, L.A., Urmantseva, V.V., Klyushin, A.G., Burgutin, A.B., and Nosov, A.M., Activity of respiratory pathways in cultured yam cells under the influence of furostanol glycosides, Russ. J. Plant Physiol., 2020, vol. 67, p. 344.

    Article  CAS  Google Scholar 

  5. Jaspers, P. and Kangasjärvi, J., Reactive oxygen species in abiotic stress signaling, Physiol. Plant., 2010, vol. 138, p. 405.

    Article  CAS  Google Scholar 

  6. Pugin, A., Frachisse, J.M., Tavernier, E., Bligny, R., Gout, E., Douce, R., and Guern, J., Early events induced by the elicitor cryptogein in tobacco cells: involvement of a plasma membrane NADPH oxidase and activation of glycolysis and the pentose phosphate pathway, Plant Cell, 1997, vol. 9, p. 2077.

    Article  CAS  Google Scholar 

  7. Kaur, G., Sharma, A., Guruprasad, K., and Pati, P.K., Versatile roles of plant NADPH oxidases and emerging concepts, Biotechnol. Adv., 2014, vol. 32, p. 551.

    Article  CAS  Google Scholar 

  8. Waszczak, C., Carmody, M. and Kangasja, J. Reactive oxygen species in plant signaling, Annu. Rev. Plant Biol., 2018, vol. 69, p. 209.

    Article  CAS  Google Scholar 

  9. Morgan, B., Ezeria, D., Amoako, T.N., Riemer, J., Seedorf, M., and Dick, T.P., Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis, Nat. Chem. Biol., 2013, vol. 9, p. 119.

    Article  CAS  Google Scholar 

  10. Jones, D.P., Redox potential of GSH/GSSG couple: assay and biological significance, Methods Enzymol., 2002, vol. 348, p. 93.

    Article  CAS  Google Scholar 

  11. Volkova, L.A., Urmantseva, V.V., Popova, E.A., and Nosov, A.M., Physiological, cytological and biochemical stability of Medicago sativa L. cell culture after 27 years of cryogenic storage, CryoLett., 2015, vol. 36, no. 4, p. 252.

    CAS  Google Scholar 

  12. Su, P.-H. and Lin, C.-H., Metabolic responses of luffa roots to long-term flooding, J. Plant Physiol., 1996, vol. 148, p. 735.

    Article  CAS  Google Scholar 

  13. Beauchamp, C. and Fridovich, J., Superoxide dismutase: improved assays and an assay applicable to acrylamide gels, Anal. Biochem., 1971, vol. 44, p. 276.

    Article  CAS  Google Scholar 

  14. Lin, C.C. and Kao, C.H., NaCl induced changes in ionically bound peroxidase activity in roots of rice seedlings, Plant Soil, 1999, vol. 216, p. 147.

    Article  CAS  Google Scholar 

  15. Yusupova, Z.R., Khairullin, R.M., and Maksimov, I.V., The activity of peroxidase in various cell fractions of wheat plants infected with Septoria nodorum berk, Russ. J. Plant Physiol., 2006, vol. 53, p. 807.

    Article  CAS  Google Scholar 

  16. Fomina, E.V. and Davidov, V.V., Aldehyde reductase activity of the liver of different-age rats under immobilization stress, Probl. Stareniya Dolgoletiya, 2004, vol. 13, p. 510.

    Google Scholar 

  17. Li, N.G. and Osakovskii, V.L., Aldehyde dehydrogenase of chloroplast leaves of higher plants, Sib. Biol. Zh., 1991, no. 2, p. 20.

  18. Radyuk, M.S., Domanskaya, I.N., Shcherbakov, R.A., and Shalygo, N.V., Effect of low above-zero temperature on the content of low-molecular antioxidants and activities of antioxidant enzymes in green barley leaves, Russ. J. Plant Physiol., 2009, vol. 56, p. 175.

    Article  CAS  Google Scholar 

  19. Heath, R.L. and Packer, L., Photoperoxidation in isolated chloroplasts. 1. Kinetics and stoichiometry of fatty acid peroxidation, Arch. Biochem. Biophys., 1969, vol. 125, p. 189.

    Article  Google Scholar 

  20. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J., Protein measurement with Folin phenol reagent, J. Biol. Chem., 1951, vol. 193, p. 265.

    Article  CAS  Google Scholar 

  21. Sagi, M. and Fluhr, R., Production of reactive oxygen species by plant NADPH oxidases, Plant Physiol., 2006, vol. 141, p. 336.

    Article  CAS  Google Scholar 

  22. O’Brien, J.A., Daudi, A., Butt, V.S., and Bolwell, G.P., Reactive oxygen species and their role in plant defence and cell wall metabolism, Planta, 2012, vol. 236, p. 765.

    Article  Google Scholar 

  23. Francoz, E., Ranocha, P., Nguyen-Kim, H., Jamet, E., Burlat, V., and Dunand, C., Roles of cell wall peroxidases in plant development, Phytochemistry, 2015, vol. 112, p. 15.

    Article  CAS  Google Scholar 

  24. Fry, S.C., Oxidative coupling of tyrosine and ferulic acid residues: Intra- and extra-protoplasmic occurrence, predominance of trimers and larger products, and possible role in inter-polymeric cross-linking, Phytochem. Rev., 2004, vol. 3, p. 97.

    Article  CAS  Google Scholar 

  25. Cosio, C. and Dunand, C., Specific function of individual class III peroxidase genes, J. Exp. Bot., 2009, vol. 60, p. 391.

    Article  CAS  Google Scholar 

  26. Elmayan, T. and Simon-Plas, F., Regulation of plant NADPH oxidase, Plant Signaling Behav., 2007, vol. 2, p. 505.

    Article  Google Scholar 

  27. Diaz Vivancos, P., Woleff, T., Markovic, J., Pallardó, F.V., and Foyer, C.H., A nuclear glutathione cycle within the cell cycle, Biochem. J., 2010, vol. 431, p. 169.

    Article  CAS  Google Scholar 

  28. Bedard, K. and Krause, K.H., The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology, Physiol. Rev., 2007, vol. 87, p. 245.

    Article  CAS  Google Scholar 

  29. Evstigneev, M.P., Zav’yalova, O.S., and Savchenko, E.V., Biofizika membrane: uchebnoe posobie (Membrane Biophysics: Manual), Sevastopol: Sevastopol. Gos. Univ., 2019.

  30. Stepovaya, E.A., Shakhristova, E.V., Ryazantseva, N.V., Nosareva, O.L., Yakushina, V.D., Nosova, A.I., Gulaya, V.S., Stepanova, E.A., Chil’chigashev, R.I., and Novitsky, V.V., The role of oxidative protein modification and the glutathione system in modulation of the redox status of breast epithelial cells, Biochemistry (Moscow) Suppl. Ser. B: Biomed. Chem., 2016, vol. 10, p. 235.

    Google Scholar 

Download references

Funding

The experiments were conducted with equipment belonging to the Research-and-Production Complex for Nature-Friendly Hi-Tech Biotechnology of High-Quality Pharmaceutical and Food Raw Materials with the Use of Cultured Cells, Organs of Higher Plants, and Microalgae. This work was supported by the government of the Russian Federation (Mega grant no. 075-15-2019-1882).

Author information

Authors and Affiliations

  1. Timiryazev Institute of Plant Physiology, Russian Academy of Sciences, Moscow, Russia

    L. A. Volkova, V. V. Urmantseva, A. B. Burgutin & A. M. Nosov

Authors
  1. L. A. Volkova
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. V. V. Urmantseva
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. A. B. Burgutin
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. A. M. Nosov
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to L. A. Volkova.

Ethics declarations

Conflict of interests. The authors declare that they have no conflict of interests.

Statement on the welfare of humans or animals. This article does not contain any studies involving animals performed by any of the authors.

Additional information

Translated by N. Balakshina

Abbreviations: ADH—aldehyde dehydrogenase; AR—aldehyde reductase; DPI—diphenyliodonium chloride; FG—furostanol glycosides; G-6-P DH—glucose-6-phosphate dehydrogenase; GR—glutathione reductase; PO—peroxidase; SOD—superoxide dismutase.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Volkova, L.A., Urmantseva, V.V., Burgutin, A.B. et al. Effect of Furostanol Glycosides from Dioscorea deltoidea on Redox State of Alfalfa Cells In Vitro. Russ J Plant Physiol 68, 1098–1106 (2021). https://doi.org/10.1134/S102144372105023X

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S102144372105023X

Keywords:

Search

Navigation