RESUMO
Morphological and proteomic changes in the kidney of scallops exposed to acute cadmium chloride (CdCl2) were observed, analyzed and compared with those in the non-exposed control group. Under microscopy the paraffin-embedded sections of the kidney revealed that the microstructure of the tissue had been severely deformed after Cd exposure. Two dimensional electrophoresis, MALDI-TOF mass spectrometry and database searches showed 13 differentially expressed protein spots, of which 11 were up-regulated, while two were down-regulated. Among these proteins, guanylate kinase (GK) and C2H2-type zinc finger protein are considered to be tightly connected with Cd toxicity. Further studies using quantitative PCR method validated that the GK mRNA was induced under Cd stress. Other proteins identified which had some relevance to Cd toxicity are also discussed. We suggested that differential proteins such as GK could play a potential role as novel biomarkers for monitoring the level of Cd contamination in seawater.
Assuntos
Cloreto de Cádmio/toxicidade , Rim/efeitos dos fármacos , Pectinidae/efeitos dos fármacos , Poluentes Químicos da Água/toxicidade , Animais , Biomarcadores/metabolismo , Cloreto de Cádmio/metabolismo , Regulação para Baixo , Guanilato Quinases/metabolismo , Rim/metabolismo , Rim/patologia , Pectinidae/metabolismo , Proteínas/metabolismo , Proteoma/metabolismo , RNA Mensageiro/metabolismo , Regulação para Cima , Poluentes Químicos da Água/metabolismoRESUMO
Cadmium (Cd) is an extremely toxic metal that induces a wide spectrum of toxic responses in organisms in the environment. In the present study, scallops (Patinopecten yessoensis), after acclimation for 1 week in the laboratory, were subjected to acute Cd chloride (CdCl2) toxicity, and ultramorphological and proteomic changes in their heart tissues were analyzed and compared with those of the nonexposed control group. Electron microscopy showed that ultrastructures of the cytoplasm and mitochondria in scallop hearts were badly damaged, and two-dimensional gel electrophoresis showed 32 protein spots that were differentially expressed after exposure to 10 mg/l CdCl2 for 24 h. Of these spots, 8 were upregulated, 16 were downregulated, and 8 showed low expression. Proteins from these spots were identified using matrix-assisted laser desorption/ionization-time of flight mass spectrometry and database searching. The results indicated that these proteins are involved in the regulation of cell structure, transport, signal transduction, and metabolism. Among other things, four proteins-identified as amino acid adenosine triphosphate (ATP)-binding cassette transporter, glycerol-3-phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate), nicotinamide adenine dinucleotide oxidase, and ATPase-were demonstrated to be especially associated with Cd toxicity. Some of the other proteins observed in this work are of particular interest in terms of their responses to Cd, which have not been reported previously. These data may provide novel biomarkers for monitoring the Cd contamination level of flowing seawater as well as provide useful insights into the mechanisms of Cd toxicity.