Zinc-induced oxidative stress in Verbascum thapsus is caused by an accumulation of reactive oxygen species and quinhydrone in the cell wall
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Morina, Filis
Jovanović, Ljubinko
Mojović, Miloš

Vidović, Marija

Panković, Dejana M

Veljović-Jovanović, Sonja

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Oxidative stress is one aspect of metal toxicity. Zinc, although unable to perform univalent oxido-reduction reactions, can induce the oxidative damage of cellular components and alter antioxidative systems. Verbascum thapsus L. plants that were grown hydroponically were exposed to 1 and 5 mM Zn2+. Reactive oxygen species (ROS) accumulation was demonstrated by the fluorescent probe H(2)DCFDA and EPR measurements. The extent of zinc-induced oxidative damage was assessed by measuring the level of protein carbonylation. Activities and isoform profiles of some antioxidant enzymes and the changes in ascorbate and total phenolic contents of leaves and roots were determined. Stunted growth because of zinc accumulation, preferentially in the roots, was accompanied by H2O2 production in the leaf and root apoplasts. Increased EPR signals of the endogenous oxidant quinhydrone, center dot CH3 and center dot OH, were found in the cell walls of zinc-treated plants. The activities of the antioxidativ...e enzymes ascorbate peroxidase (APX) (EC 1.11.1.11), soluble superoxide dismutase (SOD) (EC 1.15.1.1), peroxidase (POD), (EC 1.11.1.7) and monodehydroascorbate reductase (EC 1.6.5.4) were increased; those of glutathione reductase (EC 1.6.4.2), dehydroascorbate reductase (EC 1.8.5.1) and ascorbate oxidase (AAO) (EC 1.10.3.3) were decreased with zinc treatment. Zinc induced a cell-wall-bound SOD isoform in both organs. Leaves accumulated more ascorbate and phenolics in comparison to roots. We propose a mechanism for zinc-promoted oxidative stress in V. thapsus L. through the generation of charge transfer complexes and quinhydrone because of phenoxyl radical stabilisation by Zn2+ in the cell wall. Our results suggest that the SOD and APX responses are mediated by ROS accumulation in the apoplast. The importance of the POD/Phe/AA (ascorbic acid) scavenging system in the apoplast is also discussed.
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Physiologia Plantarum, 2010, 140, 3, 209-224Publisher:
- Wiley, Hoboken
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DOI: 10.1111/j.1399-3054.2010.01399.x
ISSN: 0031-9317
PubMed: 20626644
WoS: 000282874100001
Scopus: 2-s2.0-78649397055
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Institut za multidisciplinarna istraživanjaTY - JOUR AU - Morina, Filis AU - Jovanović, Ljubinko AU - Mojović, Miloš AU - Vidović, Marija AU - Panković, Dejana M AU - Veljović-Jovanović, Sonja PY - 2010 UR - http://rimsi.imsi.bg.ac.rs/handle/123456789/379 AB - Oxidative stress is one aspect of metal toxicity. Zinc, although unable to perform univalent oxido-reduction reactions, can induce the oxidative damage of cellular components and alter antioxidative systems. Verbascum thapsus L. plants that were grown hydroponically were exposed to 1 and 5 mM Zn2+. Reactive oxygen species (ROS) accumulation was demonstrated by the fluorescent probe H(2)DCFDA and EPR measurements. The extent of zinc-induced oxidative damage was assessed by measuring the level of protein carbonylation. Activities and isoform profiles of some antioxidant enzymes and the changes in ascorbate and total phenolic contents of leaves and roots were determined. Stunted growth because of zinc accumulation, preferentially in the roots, was accompanied by H2O2 production in the leaf and root apoplasts. Increased EPR signals of the endogenous oxidant quinhydrone, center dot CH3 and center dot OH, were found in the cell walls of zinc-treated plants. The activities of the antioxidative enzymes ascorbate peroxidase (APX) (EC 1.11.1.11), soluble superoxide dismutase (SOD) (EC 1.15.1.1), peroxidase (POD), (EC 1.11.1.7) and monodehydroascorbate reductase (EC 1.6.5.4) were increased; those of glutathione reductase (EC 1.6.4.2), dehydroascorbate reductase (EC 1.8.5.1) and ascorbate oxidase (AAO) (EC 1.10.3.3) were decreased with zinc treatment. Zinc induced a cell-wall-bound SOD isoform in both organs. Leaves accumulated more ascorbate and phenolics in comparison to roots. We propose a mechanism for zinc-promoted oxidative stress in V. thapsus L. through the generation of charge transfer complexes and quinhydrone because of phenoxyl radical stabilisation by Zn2+ in the cell wall. Our results suggest that the SOD and APX responses are mediated by ROS accumulation in the apoplast. The importance of the POD/Phe/AA (ascorbic acid) scavenging system in the apoplast is also discussed. PB - Wiley, Hoboken T2 - Physiologia Plantarum T1 - Zinc-induced oxidative stress in Verbascum thapsus is caused by an accumulation of reactive oxygen species and quinhydrone in the cell wall EP - 224 IS - 3 SP - 209 VL - 140 DO - 10.1111/j.1399-3054.2010.01399.x ER -
@article{ author = "Morina, Filis and Jovanović, Ljubinko and Mojović, Miloš and Vidović, Marija and Panković, Dejana M and Veljović-Jovanović, Sonja", year = "2010", abstract = "Oxidative stress is one aspect of metal toxicity. Zinc, although unable to perform univalent oxido-reduction reactions, can induce the oxidative damage of cellular components and alter antioxidative systems. Verbascum thapsus L. plants that were grown hydroponically were exposed to 1 and 5 mM Zn2+. Reactive oxygen species (ROS) accumulation was demonstrated by the fluorescent probe H(2)DCFDA and EPR measurements. The extent of zinc-induced oxidative damage was assessed by measuring the level of protein carbonylation. Activities and isoform profiles of some antioxidant enzymes and the changes in ascorbate and total phenolic contents of leaves and roots were determined. Stunted growth because of zinc accumulation, preferentially in the roots, was accompanied by H2O2 production in the leaf and root apoplasts. Increased EPR signals of the endogenous oxidant quinhydrone, center dot CH3 and center dot OH, were found in the cell walls of zinc-treated plants. The activities of the antioxidative enzymes ascorbate peroxidase (APX) (EC 1.11.1.11), soluble superoxide dismutase (SOD) (EC 1.15.1.1), peroxidase (POD), (EC 1.11.1.7) and monodehydroascorbate reductase (EC 1.6.5.4) were increased; those of glutathione reductase (EC 1.6.4.2), dehydroascorbate reductase (EC 1.8.5.1) and ascorbate oxidase (AAO) (EC 1.10.3.3) were decreased with zinc treatment. Zinc induced a cell-wall-bound SOD isoform in both organs. Leaves accumulated more ascorbate and phenolics in comparison to roots. We propose a mechanism for zinc-promoted oxidative stress in V. thapsus L. through the generation of charge transfer complexes and quinhydrone because of phenoxyl radical stabilisation by Zn2+ in the cell wall. Our results suggest that the SOD and APX responses are mediated by ROS accumulation in the apoplast. The importance of the POD/Phe/AA (ascorbic acid) scavenging system in the apoplast is also discussed.", publisher = "Wiley, Hoboken", journal = "Physiologia Plantarum", title = "Zinc-induced oxidative stress in Verbascum thapsus is caused by an accumulation of reactive oxygen species and quinhydrone in the cell wall", pages = "224-209", number = "3", volume = "140", doi = "10.1111/j.1399-3054.2010.01399.x" }
Morina, F., Jovanović, L., Mojović, M., Vidović, M., Panković, D. M.,& Veljović-Jovanović, S.. (2010). Zinc-induced oxidative stress in Verbascum thapsus is caused by an accumulation of reactive oxygen species and quinhydrone in the cell wall. in Physiologia Plantarum Wiley, Hoboken., 140(3), 209-224. https://doi.org/10.1111/j.1399-3054.2010.01399.x
Morina F, Jovanović L, Mojović M, Vidović M, Panković DM, Veljović-Jovanović S. Zinc-induced oxidative stress in Verbascum thapsus is caused by an accumulation of reactive oxygen species and quinhydrone in the cell wall. in Physiologia Plantarum. 2010;140(3):209-224. doi:10.1111/j.1399-3054.2010.01399.x .
Morina, Filis, Jovanović, Ljubinko, Mojović, Miloš, Vidović, Marija, Panković, Dejana M, Veljović-Jovanović, Sonja, "Zinc-induced oxidative stress in Verbascum thapsus is caused by an accumulation of reactive oxygen species and quinhydrone in the cell wall" in Physiologia Plantarum, 140, no. 3 (2010):209-224, https://doi.org/10.1111/j.1399-3054.2010.01399.x . .