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ECB-ART-31404
Arch Environ Contam Toxicol 1991 Jul 01;211:112-7. doi: 10.1007/bf01055565.
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Effects of cadmium on metal composition and adenylate energy charge in the sea star Asterias rubens L.

den Besten PJ , Bosma PT , Herwig HJ , Zandee DI , Voogt PA .


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Sea stars, Asterias rubens, were exposed to 200 micrograms Cd/L or fed with mussels which contained about 70 micrograms Cd/g dry wt. After 5 weeks, cadmium in the pyloric caeca of directly and indirectly exposed sea stars had reached levels of 12 and 9 micrograms Cd/g dry wt, respectively. For both types of exposure, a reduction of 30% of the zinc levels in the pyloric caeca was found, which was correlated with a comparable displacement of zinc from the metallothionein-like proteins. Copper levels were increased in the pyloric caeca of directly exposed sea stars. In gonads, stomachs, and body wall of directly exposed sea stars, cadmium concentrations were 4 to 9 times higher than those in animals fed with Cd-contaminated mussels. Cadmium exposure also affected metal composition in these tissues. The ovaries contained relatively large amounts of zinc. Gel filtration chromatography revealed that this zinc and the accumulated cadmium were distributed over a large range of high-molecular-weight proteins. Both direct and indirect cadmium exposure resulted in a small, but significant decrease of the adenylate energy charge (AEC) in the pyloric caeca. In the gonads, no effect of the cadmium exposure could be demonstrated on the AEC, but in the ovaries a reduction of the adenylate pool was found. In semi-field experiments, stars were exposed to 25 micrograms Cd/L or fed with mussels collected from the heavily polluted Dutch Western Scheldt. After 6 months of direct or indirect exposure, cadmium in the pyloric caeca had reached comparable levels of 8 and 7 micrograms/g dry wt, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

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Genes referenced: LOC100887844 LOC115925415

References [+] :
Atkinson, Adenosine triphosphate conservation in metabolic regulation. Rat liver citrate cleavage enzyme. 1967, Pubmed