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Nematode and snail metallothioneins

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Abstract

Metallobiologists have, at large, neglected soil dwelling invertebrates; exceptions are the nematode (Caenorhabditis elegans) and snails (Helix pomatia and Cantareus aspersus). This review aims to compare and contrast the molecular, protein and cellular mechanisms of the multifunctional nematode and snail metallothioneins (MTs). The C. elegans genome contains two MT genes, mtl-1, which is constitutively expressed in the pharynx and likely to act as an essential and/or toxic metal sensor, and mtl-2, which plays a negligible role under normal physiological conditions but is strongly induced (as mtl-1) in intestinal cells upon metal exposure. It has been possible to follow the intricate phenotypic responses upon the knockdown/knockout of single and multiple MT isoforms and we have started to decipher the multifunctional role of C. elegans MTs. The snails have contributed to our understanding regarding MT evolution and diversity, structure and metal-specific functionality. The H. pomatia and C. aspersus genomes contain at least three MT isoform genes. CdMT is responsible for cadmium detoxification, CuMT is involved in copper homeostasis and Cd/CuMT is a putative ancestral MT possibly only of minor importance in metal metabolism. Further investigations of nematode, snail and other invertebrate MTs will allow the development of alternative biomarker approaches and lead to an improved understanding of metallobiology, protein evolution and toxicogenomics.

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Acknowledgments

We wish to thank the Natural Environmental Research Council (NERC) and the Biotechnology and Biological Sciences Research Council (BBSRC) for continuous financial assistance to the S.R.S. laboratory. The work on pulmonate snail MTs has been kindly supported by the Austrian Science Foundation (FWF), project no. P19782-B03.

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Correspondence to Stephen R. Stürzenbaum.

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This article is part of a JBIC special issue on metallothioneins.

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Höckner, M., Dallinger, R. & Stürzenbaum, S.R. Nematode and snail metallothioneins. J Biol Inorg Chem 16, 1057–1065 (2011). https://doi.org/10.1007/s00775-011-0826-3

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