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Subject

Sequencing Analysis of Ligand Binding Domain of Aryl Hydrocarbon Receptor which is a Dioxin Sensitive Gene in the Ornamental Birds
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Type
Academic journal
Author
Hae-Jeong Park (Kyung Hee University) Ji-Hee Hwang (Kyung Hee University) Jin-Young Park (National Institute of Environmental Research) Eun-Young Kim (Kyung Hee University)
Journal
The Ornithological Society Of Korea The Korean Journal of Ornithology Vol.22 No.2 KCI Accredited Journals
Published
2015.12
Pages
1 - 8 (8page)

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Sequencing Analysis of Ligand Binding Domain of Aryl Hydrocarbon Receptor which is a Dioxin Sensitive Gene in the Ornamental Birds
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Toxicity of dioxins and dioxin like compounds (DLCs) is mainly mediated by aryl hydrocarbon receptor (AHR) which is a cytoplasmic transcription factor and highly conserved in animal taxa. Birds are exposed to various environmental contaminants of DLCs and accumulated the high levels of these chemicals in their tissues or organs. Birds have multiple AHR isoforms, such as AHR1 and AHR2. In our previous research, avian AHR1 is dominant isoform to determine the dioxin sensitivity and the two critical amino acid sites (324<SUP>th</SUP> and 380<SUP>th</SUP> site) in its ligand binding domain (LBD) are important to induce the different sensitivity. In this study, to investigate the dioxin sensitivity in ornamental birds, we analyzed the amino acid sequences of AHR LBDs in the four avian species, Budgerigar, Domestic canary, Bengalese finch and Zebra finch. AHR LBD sequences isolated from 4 avian species showed two types of AHR1 LBD which might be predicted in high sensitivity (Ile<SUP>324th</SUP>_Ser<SUP>380th</SUP>, I-S type) and moderate sensitivity (Ile<SUP>324th</SUP>_Ala<SUP>380th</SUP>, I-A type). Although sample numbers are not enough, I-A moderate type is prominently shown in these ornamental avian species than other types such as I-S or V-A types (Val<SUP>324th</SUP>_Ala<SUP>380th</SUP>).

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UCI(KEPA) : I410-ECN-0101-2016-482-002239195