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Induction of Metallothionein Synthesis in the Gill and Kidney of Littorina Littorea Exposed to Cadmium

Published online by Cambridge University Press:  11 May 2009

M.J. Bebianno
Affiliation:
Plymouth Marine Laboratory, Citadel Hill, Plymouth, PL1 2PB.
W.J. Langston
Affiliation:
†Corresponding author.

Extract

Induction of metallothionein synthesis in Littorina littorea exposed to cadmium (400 µg I-1) is tissue dependent. Concentrations of the metal-binding protein increased by a factor of four in the gills and by a factor of three in the kidney.

Gel filtration chromatography of heat-treated cytosolic extracts reveals that cadmium, accumulated in both the gills and the kidney, is bound principally to the newly formed metallothionein. Cadmium saturation of the protein (at an MT:Cd molar ratio of 1:5) and the approach of steady-state condition for Cd accumulation was indicated in the latter tissue, but there was little evidence for Cd equilibrium in gills.

Metallothionein levels in the kidney of L. littorea can be determined on a routine basis in laboratory experiments and in field samples by differential pulse polarography of wholecytosol preparations: heat-treatment/centrifugation is sufficient to remove most of the interference from high-molecular-weight thiolic proteins. In contrast, the use of gelfiltration chromatography is recommended alongside polarographic analysis of the gill cytosol to enable quantification of, and compensation for, such interferences, and hence to ensure that only metallothionein is determined.

Measurements of metallothionein induction in the kidney of Littorina may therefore prove useful in the determination of sublethal biological response to metal contamination. Background metallothionein concentrations of 3–4 mg g-1 (measured polarographically) serve as a baseline against which samples from contaminated sites can be assessed.

INTRODUCTION

Exposure of marine organisms to metals such as cadmium can induce the synthesis of low molecular weight, cysteine-rich proteins, metallothioneins (MTs), which are capable of sequestering and detoxifying excess intra-cellular metal.

Type
Research Article
Copyright
Copyright © Marine Biological Association of the United Kingdom 1995

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References

Bebianno, M.J. & Langston, W.J., 1989. Quantification of metallothioneins in marine invertebrates using differential pulse polarography. Portugaliae Electrochimica Acta, 7, 5964.Google Scholar
Bebiann, M.J. & Langston, W.J., 1991. Metallothionein induction in Mytilus edulis exposed to cadmium. Marine Biology, 108, 9196.CrossRefGoogle Scholar
Bebianno, M.J. & Langston, W.J., 1992. Cadmium induction of metallothionein synthesis in Mytilus galloprovincialis. Comparative Biochemistry and Physiology, 103C, 7985.Google Scholar
Bebianno, M.J. & Langston, W.J., 1993. Turnover rate of metallothionein and cadmium in Mytilus edulis. BioMetals, 6, 239244.CrossRefGoogle ScholarPubMed
Bebianno, M.J., Langston, W.J. & Simkiss, K., 1992. Metallothionein induction in Littorina littorea (Mollusca: Prosobranchia) on exposure to cadmium. Journal of the Marine Biological Association of the United Kingdom, 72, 329343.CrossRefGoogle Scholar
Brdicka, R., 1933. Polarographic studies with dropping mercury kathode. Part XXXI. A new test for proteins in the presence of cobalt salts in ammoniacal solutions of ammonium chloride. Collection of Czechoslovak Chemical Communications, 5, 112128.CrossRefGoogle Scholar
Bryan, G.W., Langston, W.J., Hummerstone, L.G., Burt, G.R. & Ho, Y.B., 1983. An assessment of the gastropod, Littorina littorea, as an indicator of heavy-metal contamination in United Kingdom estuaries. Journal of the Marine Biological Association of the United Kingdom, 63, 5357.CrossRefGoogle Scholar
Frazier, J.M. & George, S.G., 1983. Cadmium kinetics in oysters - a comparative study of Crassostrea gigas and Ostrea edulis. Marine Biology, 76, 5561.CrossRefGoogle Scholar
George, S.G., Carpene, E., Coombs, T.L., Overnell, J. & Youngston, A., 1979. Characterization of cadmium-binding proteins from mussels, Mytilus edulis (L.), exposed to cadmium. Biochimica et Biophysica Acta, 580, 225233.CrossRefGoogle ScholarPubMed
George, S.G. & Viarengo, A., 1985. A model for heavy metal homeostasis and detoxification in mussels. In Marine pollution and physiology: recent advances (ed. F.J., Vernberg et al.), pp. 125143. Columbia, South Carolina: University of South Carolina Press.Google Scholar
Howard, A.G. & Nickless, G., 1978. Heavy metal complexation in polluted molluscs. III. Periwinkles (Littorina littorea), cockles (Cardium edule) and scallops (Chlamys opercularis). Chemico-Biological Interactions, 23, 227231.CrossRefGoogle ScholarPubMed
Kojima, Y., Berger, C, Vallee, B.L. & Kagi, J.H.R., 1976. Amino-acid sequence of equine renal metallothionein-lB. Proceedings of the National Academy of Sciences of the United States of America, 73, 34133417.CrossRefGoogle Scholar
Langston, W.J., Bebianno, M.J. & Zhou, M., 1989. A comparison of metal-binding proteins and cadmium metabolism in the marine molluscs Littorina littorea (Gastropoda), Mytilus edulis and Macoma balthica (Bivalvia). Marine Environmental Research, 28, 195200.CrossRefGoogle Scholar
Langston, W.J. & Zhou, M., 1986. Evaluation of the significance of metal-binding proteins in the gastropod Littorina littorea. Marine Biology, 92, 505515.CrossRefGoogle Scholar
Langston, W.J. & Zhou, M., 1987. Cadmium accumulation, distribution and metabolism in the gastropod Littorina littorea: the role of metal-binding proteins. Journal of the Marine Biological Association of the United Kingdom, 67, 585601.CrossRefGoogle Scholar
Marigomez, J.A. & Ireland, M.P., 1989. Accumulation, distribution and loss of cadmium in the marine prosobranch Littorina littorea (L.). The Science of the Total Environment, 78, 112.CrossRefGoogle ScholarPubMed
Noel-Lambot, F., Bouquegneau, J.M., Frankenne, F. & Disteche, A., 1978. Le role des metallothioneines dans le stockage des metaux lourds chez les animaux marins. Revue Internationale d'Oceanographie Medicale, 49, 1320.Google Scholar
Nolan, C.V. & Duke, E.J., 1983. Cadmium accumulation and toxicity in Mytilus edulis: involvement of metallothioneins and heavy molecular weight proteins. Aquatic Toxicology, 4, 153163.CrossRefGoogle Scholar
Olafson, R.W., Sim, R.G. & Boto, K.G., 1979. Isolation and chemical characterization of the heavy metal-binding protein metallothionein from marine invertebrates. Comparative Biochemistry and Physiology, 62B, 404416.Google Scholar
Otvos, J.D., Olafson, R.W. & Armitage, I.M., 1982. Structure of an invertebrate metallothionein from Scylla serrata. Journal of Biological Chemistry, 357, 24272431.CrossRefGoogle Scholar
Roesijadi, G., 1986. Mercury-binding proteins from the marine mussel, Mytilus edulis. Environmental Health Perspectives, 65, 4548.Google ScholarPubMed
Roesijadi, G., Calabrese, A. & Nelson, D.A., 1982. Mercury-binding proteins of Mytilus edulis. In Physiological mechanisms of marine pollutant toxicity (ed. W.B., Vernberg et al.), pp. 7587. New York: Academic Press.CrossRefGoogle Scholar
Viarengo, A., Palmero, S., Zanicchi, G., Capelli, R., Vaissiere, R. & Orunesu, M., 1985. Role of metallothioneins in Cu and Cd accumulation and elimination in the gill and digestive gland cells of Mytilus galloprovincialis Lam. Marine Environmental Research, 16, 2336.CrossRefGoogle Scholar