Identification, sequencing and expression of selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254.

Comp Biochem Physiol C Toxicol Pharmacol

Lab. E.S.E., Ecotoxicité, Santé Environnementale-CNRS UMR 7146, Université de Metz, rue Delestraint, 57070 Metz, France.

Published: October 2006

Glutathione peroxidases (GPx) and glutathione S-transferases (GST) are essential enzymes of the cellular defense system. The aim of this work was the identification of GPx transcript in a freshwater bivalve, Unio tumidus, and the effects of Aroclor 1254 on GPx and pi-class GST (pi-GST) expression pattern. The GPx full-length coding sequence was obtained by reverse transcription PCR using degenerated primers followed by 5' and 3' rapid amplification of cDNA ends. The GPx cDNA encodes a protein of 232 amino acids. The 72nd amino acid corresponds to a selenocysteine encoded by a TGA codon. Residues essential to the enzymatic function are conserved in GPx of U. tumidus. Specific amplifications of the Se-GPx mRNA from U. tumidus were performed on the digestive gland, the excretory system and the gills. Se-GPx expression level is highest in the digestive gland. No induction of the Se-GPx was observed at the transcriptional level in the digestive gland and the excretory system of Aroclor-treated mussels, while an increase of the pi-GST mRNA level was observed in the excretory system.

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http://dx.doi.org/10.1016/j.cbpc.2006.07.002DOI Listing

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