Fujisawa Nozomi, Kawai Yusuke K, Nakayama Shouta M M, Ikenaka Yoshinori, Yamamoto Hideaki, Ishizuka Mayumi
Laboratory of Toxicology, Department of Environmental Veterinary Science, Graduate School of Veterinary Medicine, Hokkaido University, N18 W9, Kita-ku, Sapporo, Hokkaido 060-0818, Japan.
J Vet Med Sci. 2013 Dec 30;75(12):1577-83. doi: 10.1292/jvms.13-0179. Epub 2013 Aug 2.
There are two arylhydrocarbon receptor (AhR) isoforms in birds, AhR1 and AhR2. The varying sensitivity of AhR is reported to be related to two critical amino acids at positions 325 and 381 in the AhR1 ligand-binding domain. In this study, seven avian species whose in vivo dioxin sensitivity was known, and 13 species with no data regarding their in vivo dioxin sensitivity were examined. The two critical amino acids in the ligand-binding domain were investigated in avian species, and the results were compared with the taxonomy or phylogenetic trees for the bird AhR proteins. We found that the two critical amino acids did not correlate with the taxonomy or phylogeny of these proteins, suggesting that dioxin sensitivity was independent of taxonomy.
鸟类中有两种芳烃受体（AhR）亚型，即AhR1和AhR2。据报道，AhR的敏感性差异与AhR1配体结合域中第325位和第381位的两个关键氨基酸有关。在本研究中，检测了7种已知体内二噁英敏感性的鸟类物种，以及13种无体内二噁英敏感性数据的物种。对鸟类物种配体结合域中的两个关键氨基酸进行了研究，并将结果与鸟类AhR蛋白的分类学或系统发育树进行了比较。我们发现这两个关键氨基酸与这些蛋白的分类学或系统发育无关，这表明二噁英敏感性与分类学无关。
