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Metal ion trafficking in earthworms - identification of a cadmium specific metallothionein

Stuerzenbaum, Stephen R., Winters, Carole, Kille, Peter ORCID: https://orcid.org/0000-0001-6023-5221 and Morgan, Andrew John 2001. Metal ion trafficking in earthworms - identification of a cadmium specific metallothionein. Journal of Biological Chemistry 276 , pp. 34013-34018. 10.1074/jbc.M103605200

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Abstract

Exposure to cadmium poses a considerable risk to human health and environmental safety. Earthworms reside in the most contaminated sites on earth, displaying a phenomenal tolerance to toxic heavy metals. They exhibit a distinct metabolic pathway that allows the bio-accumulation of cadmium to yield body burdens in excess of 1/1000th of total dry body weight, a most impressive figure by any standard. However, the precise molecular mechanism underlying this phenomenon remains to be unraveled. This study meets this challenge by fully characterizing the major metal-binding protein in earthworms, namely the two isoforms of metallothionein. Chemical analysis of recombinant protein showed that although both isoforms bind equimolar amounts of cadmium (6 mol), wMT-2 is more stable during proton competition. Furthermore, isoform-specific transcript analysis demonstrated that only wMT-2 is responsive to cadmium in a dose and temporal manner. The specific sequestration of cadmium to wMT-2 protein was confirmed in situ using polyclonal antisera. The latter also provided the means for mapping the cellular and intracellular distribution of metallothionein, thus yielding a holistic insight into its involvement in cadmium transit during absorption, storage, and excretion. The structure-function relationship of wMT-2 and its role in cadmium detoxification through sequestration and compartmentalization is discussed.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
ISSN: 0021-9258
Last Modified: 17 Oct 2022 08:50
URI: https://orca.cardiff.ac.uk/id/eprint/1199

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