Biochemical Journal · 1980 · 33 citations · 17 references
Chemical BiologyTumor BiologyOxidative StressLess CadmiumToxicologyProteomicsCancer ResearchBiochemistryTrace MetalCopper-binding ProteinCell BiologyTumor MicroenvironmentNatural SciencesMetalloproteinBioactive MetalCadmium-binding ProteinMetal ToxicityMedicineZinc Status
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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George L. Ellman · Archives of Biochemistry and Biophysics · 1959 · 25.9K citations
Binding of cadmium ions by rat liver and kidney
Michael Webb · Biochemical Pharmacology · 1972 · 260 citations
Biological function of metallothionein
R.W. Chen, P.D. Whanger, P.H. Weswig · Biochemical Medicine · 1975 · 163 citations