Identification of aryl hydrocarbon receptor 2 in aquatic birds; cDNA cloning of AHR1 and AHR2 and characteristics of their amino acid sequences.
The toxic effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and its related planar halogenated aromatic hydrocarbons (PHAHs) are mediated by the aryl hydrocarbon receptor (AHR). To investigate the potential sensitivity to PHAHs and the evolutional diversity of AHR in aquatic birds, AHR cDNAs were initially cloned and sequenced from the livers of a black-footed albatross (Diomedea nigripes) and a common cormorant (Phalacrocorax carbo). In this study, we report the identification of two distinct AHR paralog genes in these species. The two full-length AHR cDNAs from albatross were highly divergent (33% overall amino acid identity, and 60% identity in the N-terminal half). Phylogenetic analysis showed that one of them belongs to the AHR1 clade and the other one to the AHR2 clade, which has been identified only from fishes, but not yet from mammals and birds. Albatross AHR1 encoded a 861-residue protein with a predicted molecular mass of 96.7 kDa, and in the case of albatross AHR2, 925 amino acids and 100.7 kDa. From cormorant liver, the full-length AHR1 cDNA and the partial AHR2 cDNA were cloned. This result strongly suggests that bird species also possess two distinct AHR genes (AHR1 and AHR2). To our knowledge, this is the first report on the presence of an AHR2-like isoform in bird species as well as in fish.