Influence of a Toxic Microcystis aeruginosa Strain on Glutathione Synthesis and Glutathione-S-Transferase Activity in Common Carp Cyprinus carpio (Teleostei: Cyprinidae)

  • Lílian Lund Amado
  • Márcia Longaray Garcia
  • Patrícia Baptista Ramos
  • João Sarkis Yunes
  • José Maria MonserratEmail author


We evaluated the effects of aqueous extracts of the cyanobacterium-producing microcystin (MC), Microcystis aeruginosa (strain RST9501), on detoxification capacity and glutathione (GSH) synthesis in liver, brain, gill, and muscle—as well as apoptotic protease (calpain) activity in liver and brain—in the common carp Cyprinus carpio (Teleostei: Cyprinidae). Experimental groups were defined as follows: (1) control (CTR); (2) carp treated with an aqueous extract from the toxic cyanobacteria M. aeruginosa in a final MC concentration of 25 μg/kg (MC 25); and (3) carp treated with an aqueous extract from the toxic cyanobacteria M. aeruginosa in a final MC concentration of 50 μg/kg (MC 50). Carp were gavaged with a cyanobacterial aqueous solution or MilliQ water (CTR group). The experiment was conducted for period of 48 h comprising two gavages with a 24-h interval between them. Some of the parameters analyzed in liver, brain, gill, and muscle included activity of the enzymes glutathione-S-transferase (GST), glutamate cysteine ligase (GCL), glutathione reductase (GR), and GSH concentration. We also evaluated GST pi concentration by Western blot as well as calpain activity in liver and brain samples. In carp liver from the MC 50 group, we observed a decrease in GST and GCL activity, which was accompanied by a decreased GSH concentration. In addition, liver calpain activity was highly induced in carp at both MC doses. Thus, MC ingestion affected the liver antioxidant status through decreasing the GSH concentration and the activity of the enzyme involved in its synthesis (GCL). It also decreased the MC detoxification capacity of the liver because total GST activity decreased, a result that cannot be ascribed to GST pi levels. Because GSH acts as an uncompetitive inhibitor of calpain, its decrease should explain the higher activity of this apoptotic enzyme. The main goal of this study was to show that a decrease in GSH concentration is related to decreased activity of GCL, the limiting enzyme involved in GSH synthesis. Because MCs are phosphatase inhibitors and GCL is allosterically inhibited by phosphorylation, the cellular hyperphosphorylation state induced by MC exposure could act as a modulator factor for antioxidant defenses.


Common Carp Ethylene Diamine Tetraacetic Acid Ethylene Diamine Tetraacetic Acid Calpain Activity Glutamate Cystein Ligase 
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The study was supported by a productivity research fellowship from the Brazilian Agency CNPq (J. M. M.; Proc. No. 304917/2006-0). J. S. Yunes was awarded a research fellowship from CNPq. This study was also funded by a grant from the International Foundation for Science (L. L. Amado; Proc. No. A4427-1).


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Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Lílian Lund Amado
    • 1
    • 2
  • Márcia Longaray Garcia
    • 2
  • Patrícia Baptista Ramos
    • 2
  • João Sarkis Yunes
    • 3
  • José Maria Monserrat
    • 1
    • 2
    Email author
  1. 1.Curso de Pós-Graduação em Ciências Fisiológicas-Fisiologia Animal ComparadaUniversidade Federal do Rio Grande-FURGRio GrandeBrazil
  2. 2.Instituto de Ciências Biológicas (ICB)Universidade Federal do Rio Grande-FURGRio GrandeBrazil
  3. 3.Unidade de Pesquisa em CianobactériasFURGRio GrandeBrazil

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