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Benzo(a)pyrene inhibits the accumulation and toxicity of cadmium in subcellular fractions of Eisenia fetida

Author:
Zhang, Lihao, Zhou, Lina, Han, Lisi, Zhao, Chenyu, Norton, Jeanette M., Li, Huixin, Hu, Feng, Xu, Li
Source:
Chemosphere 2019 v.219 pp. 740-747
ISSN:
0045-6535
Subject:
Eisenia fetida, acetylcholinesterase, benzo(a)pyrene, cadmium, earthworms, excretion, glutathione transferase, pollutants, pollution, principal component analysis, protein content, protein synthesis, subcellular fractions, toxicity
Abstract:
Cadmium (Cd) and benzo [a]pyrene (BaP) often co-occur in the environment, and the critical body residue of organisms is used as an indicator of the toxic effects of contaminants. However, little is known about their distributions and toxicities when pollution of Cd and BaP are combined. Semi-static solution culture experiment was used to study the impacts of BaP on the subcellular distribution of the toxic metal Cd in the earthworm Eisenia fetida. We explored the mechanisms by which this organism responds to combined exposure to these pollutants by measuring the protein content of each of three subcellular fractions, as well as acetylcholinesterase (AChE) and glutathione S-transferase (GST) activities. The subcellular partitioning of Cd was heterogeneous and Cd mainly accumulated in the cytosolic fraction (Fraction C), which was previously reported to be involved in metal immobilization. In Fraction C, Cd accumulation was correlated with the external concentration to which the earthworm had been exposed; however, in the presence of BaP, Cd accumulation was inhibited and plateaued at high external Cd concentrations. A principal component analysis revealed that this decreased Cd accumulation might be caused by increases in GST activity, which likely increased the excretion of Cd. BaP was also found to stimulate protein biosynthesis and upregulate AChE and GST activities in the debris fraction (Fraction E), indicating other potential detoxification mechanisms in this fraction. Granule fraction (Fraction D) had a lower protein content, AChE and GST activities than the other subcellular fractions, supporting previous findings that Fraction D is largely inert.
Agid:
6257854