Growth and physiological responses to cadmium stress of two populations of Dittrichia viscosa (L.) Greuter

► Cd tolerance and accumulation are constitutive traits in D. viscosa. ► The physiological mechanisms involved in Cd stress differed between clones. ► The metallicolous clone was more Cd tolerant than the non-metallicolous one. ► Antioxidant enzymes had important roles in each clone, especially pero...

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Veröffentlicht in:Journal of hazardous materials 2013-01, Vol.244-245, p.555-562
Hauptverfasser: Fernández, R., Bertrand, A., Reis, R., Mourato, M.P., Martins, L.L., González, A.
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Sprache:eng
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Zusammenfassung:► Cd tolerance and accumulation are constitutive traits in D. viscosa. ► The physiological mechanisms involved in Cd stress differed between clones. ► The metallicolous clone was more Cd tolerant than the non-metallicolous one. ► Antioxidant enzymes had important roles in each clone, especially peroxidases. Two clones of Dittrichia viscosa (L.) Greuter from contrasting populations, DV-A (metallicolous) and DV-W (non-metallicolous), were studied to compare Cd accumulation and tolerance. After 10 days of hydroponic culture with 0, 5, 10, and 15mgCdL−1, metal accumulation and plant growth were measured as well as other stress markers such as decrease in the content of photosynthetic pigments, lipid peroxidation, phenols, H2O2, and free proline. We also analyzed the activity of the antioxidant enzymes guaiacol and ascorbate peroxidases, catalase, superoxide dismutase, and glutathione reductase as well as their isoform patterns. Our results confirmed a high Cd tolerance and accumulation in both clones of D. viscosa, which suggests that these traits are constitutive in this species. However, when the Cd concentration in solution exceeded 10mgCdL−1, DV-A was more tolerant than DV-W. The physiological mechanisms involved in Cd tolerance also differed between them, although phenols and guaiacol peroxidase played an important role in both clones. The effective Cd detoxification of DV-A consisted mainly in a promoted ascorbate peroxidase activity and better efficiency of catalase and glutathione reductase enzymes.
ISSN:0304-3894
1873-3336
DOI:10.1016/j.jhazmat.2012.10.044