In vitro effects of cadmium, zinc and lead on calmodulin-dependent actions inOncorhynchus mykiss, Mytilus sp., andChlamydomonas reinhardtii

  • Renata Behra


The potential of cadmium, zinc, and lead to interact with calmodulin (CaM) was investigated by examiningin vitro CaM-dependent protein phosphorylation in tissues from rainbow trout (Oncorhynchus mykiss) and sea mussel (Mytilus sp.) and CaM-dependent phosphodiesterase (PDE) activation by algal (Chlamydomonas reinhardtii) extracts. Cadmium, zinc, and lead proved effective in sustaining CaM-dependent protein phosphorylation in systems containing calcium, whereas only lead was capable of CaM activation in systems depleted of calcium. Cadmium lead to a small activation of CaM-dependent PDE activity by algal extracts, corresponding to ∼25% of that induced by calcium. Cadmium-induced PDE-activation could be attributed to the residual calcium present in the extract. The results indicate that metal-induced CaM activation is primarily mediated in the case of cadmium and zinc by resulting calcium/CaM complexes and in the case of lead by lead/CaM complexes.


Calcium Zinc Waste Water Cadmium Water Management 
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Copyright information

© Springer-Verlag New York Inc 1993

Authors and Affiliations

  • Renata Behra
    • 1
  1. 1.EAWAG (Swiss Federal Institute for Water Resources and Water Pollution Control)DuebendorfSwitzerland

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