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

Author:

Koch J,Wielgus S,Shankara B,Saryan L A,Shaw C F,Petering D H

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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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1. Cellular Inorganic Chemistry Concepts and Examples;Cellular and Molecular Biology of Metals;2010-05-21

2. Metal-dependent protein folding: Metallation of metallothionein;Journal of Inorganic Biochemistry;2006-12

3. [36] Role of matallothionein in essential, toxic, and therapeutic metal metabolism in Ehrlich cells;Metallobiochemistry Part B Metallothionein and Related Molecules;1991

4. Lipid peroxidation in mitochondria and microsomes from adult and fetal rat tissues;Biological Trace Element Research;1989-11

5. Plasma and cellular zinc levels and membrane lipid composition in streptozotocin diabetic rats;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1989-01

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