Advertisement

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

  • Renata Behra
Article

Abstract

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.

Keywords

Calcium Zinc Waste Water Cadmium Water Management 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Behra R, Gall R (1991) Calcium/calmodulin-dependent phosphorylation and the effect of cadmium in cultured fish cells. Comp Biochem Physiol 100C:191–195Google Scholar
  2. Bradford MM (1976) A rapid method for the quantification of microgram quantities of protein using the principle of dye binding. Anal Biochem 72:248–254PubMedGoogle Scholar
  3. Chao S-H, Suzuki Y, Zysk JR, Cheung WY (1984) Activation of calmodulin by various cations as a function of ionic radius. Mol Pharmacol 26:75–82PubMedGoogle Scholar
  4. Cheung WY (1980) Calmodulin plays a pivotal role in cellular regulation. Science 207:19–27PubMedGoogle Scholar
  5. — (1984) Calmodulin: its potential role in cell proliferation and heavy metal toxicity. Federation Proc 43:2995–2999PubMedGoogle Scholar
  6. Dreisbach RH (1983) Handbook of poisoning: prevention, diagnosis and treatment, 11th ed Lange Medical Publications, Los Altos, CAGoogle Scholar
  7. Flik G, Van de Winkel JGJ, Pärt P, Wendelaar Bonga SE, Lock RAC (1987) Calmodulin mediated cadmium inhibition of phosphodiesterase activity,in vitro. Arch Toxicol 59:353–359PubMedGoogle Scholar
  8. Förstner U, Wittmann GTW (1981) Metal pollution in the aquatic environment, 2nd revised ed. Springer-Verlag, BerlinGoogle Scholar
  9. Geiser JR, van Tuinen D, Brockerhoff SE, Neff MM, Davis TN (1991) Can calmodulin function without binding calcium? Cell 65:949–959PubMedGoogle Scholar
  10. Goldstein GW, Ar D (1983) Lead activates calmodulin sensitive processes. Life Sci 33:1001–1006PubMedGoogle Scholar
  11. Habermann E, Crowell K, Janicki P (1983) Lead and other metals can substitute for Ca2+ in calmodulin. Arch Toxicol 54:61–70PubMedGoogle Scholar
  12. Jones HS, Fowler BA (1980) Biological interactions of cadmium with calcium. Ann NY Acad Sci 355:309–318PubMedGoogle Scholar
  13. Klee CB, Vanaman TC (1982) Calmodulin. Adv Protein Chem 35:213–321PubMedGoogle Scholar
  14. Lämmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 277:680–685Google Scholar
  15. Lewis TL, Yuan Y, Haug A (1990) Calmodulin concentration in mucus of rainbow trout,Salmo gairdneri, exposed to combinations of acid, aluminum, and calcium. Bull Environ Contam Toxicol 44:449–455PubMedGoogle Scholar
  16. Markovac J, Goldstein GW (1988) Picomolar concentrations of lead stimulate brain protein kinase C. Nature (Lond) 334:71–73Google Scholar
  17. Mazzei GJ, Girard PR, Kuo JF (1984) Environmental pollutant Cd2+ biphasically and differentially regulates myosin light chain kinase and phospholipid/Ca2+-dependent protein kinase. FEBS Lett 173:124–128PubMedGoogle Scholar
  18. Nordberg GF, Fowler BA, Friberg L, Jernelov A, Nelson N, Piscator M, Sanstead HH, Vostal J, Vouk VB (1978) Factors influencing metabolism and toxicity of metals: a consensus report. Environ Health Perspect 25:3–41PubMedGoogle Scholar
  19. Sillen LG, Martell A (1971) Stability constants, Suppl. No. 1, Special Publication 25, The Chemical Society. Burlington House, LondonGoogle Scholar
  20. Simons JJB (1986) Cellular interactions between lead and calcium. Br Med Bull 42:431–434PubMedGoogle Scholar
  21. Smith RM, Martell AE (1975) Critical stability constants, Vol 3. Plenum Press, New YorkGoogle Scholar
  22. Staub R (1961) Ernährungsphysiologisch-autökologisch Untersuchungen an der planktischen BlaualgeOscillatoria rubescens. Schw Z Hydro 23:82–198Google Scholar
  23. Suzuki Y, Chao S-H, Zysk JR, Cheung WY (1985) Stimulation of calmodulin by cadmium ion. Arch Toxicol 57:205–211PubMedGoogle Scholar
  24. Van Belle H (1981) R 24571: A potent inhibitor of calmodulin-activated enzymes. Cell Calcium 2:483–493Google Scholar
  25. Verbost PM, Flik G, Lock RAC, Wendelaar Bonga SE (1988) Cadmium inhibits plasma membrane calcium transport. J Membr Biol 102:97–104PubMedGoogle Scholar
  26. Verbost PM, Van Rooij J, Flik G, Lock RAC, Wendelaar Bonga SE (1989) The movement of cadmium through freshwater trout branchial epithelium and its interference with calcium transport. J Exp Biol 145:185–197Google Scholar
  27. Viarengo A (1985) Biochemical effects of trace metals. Mar Pollut Bull 16:153–158Google Scholar
  28. Westall J (1979) MICROQL, a chemical equilibrium program in BASIC, Internal Report. EAWAG, DübendorfGoogle Scholar

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

Personalised recommendations