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. 1980 Jul 1;189(1):95–104. doi: 10.1042/bj1890095

Zinc-, copper- and cadmium-binding protein in Ehrlich ascites tumour cells.

J Koch, S Wielgus, B Shankara, L A Saryan, C F Shaw, D H Petering
PMCID: PMC1161921  PMID: 7458908

Abstract

The properties of Ehrlich ascites tumour cells exposed in vivo to cadmium were investigated as a function of the zinc status of the host animals. Tumour-cell growth was inhibited by cadmium in both zinc-sufficient and zinc-deficient animals. However, cells in zinc-sufficient tumours accumulate much less cadmium than those in deficient tumours. The subcellular distributions of cadmium and zinc do not depend on zinc status. Cadmium and zinc are bound to a low-molecular-weight protein with properties similar to metallothionein. Without exposure to cadmium, a zinc- and copper-binding protein is still present that behaves like a metallothionein. This protein can rapidly bind cadmium added to Ehrlich cells in vitro. It is shown that the zinc- and copper-binding protein contains free thiol groups. Ehrlich cells isolated from cadmium-treated animals are viable and show normal incorporation of uridine into RNA, but the cellular uptake of thymidine and its incorporation into DNA are inhibited.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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