Tributyltin-binding protein type 1 has a distinctive lipocalin-like structure and is involved in the excretion of tributyltin in Japanese flounder, Paralichthys olivaceus

Hina Satone, Yuji Oshima, Yohei Shimasaki, Takahiko Tawaratsumida, Yumi Oba, Eriko Takahashi, Takeshi Kitano, Shun-Ichiro Kawabata, Yoshimitsu Kakuta, Tsuneo Honjo

研究成果: ジャーナルへの寄稿記事

17 引用 (Scopus)

抄録

Tributyltin-binding protein type 1 (TBT-bp1) is a newly discovered protein that binds with TBT in the blood of the Japanese flounder, Paralichthys olivaceus. We determined the genomic sequence of TBT-bp1 and found that this protein has a conserved exon-intron structure that is common to the lipocalin protein family. The secondary and tertiary structures of TBT-bp1, predicted from amino acid sequence, included at least two α-helices and eight β-sheets that are conserved in all lipocalins and form a barrel structure that may bind with ligands. Analysis of the gene structure, secondary structure, and tertiary structure demonstrated that TBT-bp1 could be classified as a lipocalin. A homology search revealed the presence of TBT-bp1-like proteins in eight species of teleost. When flounder were injected intraperitoneally with TBT-d27 at 11.6 μg/fish, TBT-d27 was detected in the blood and in the skin mucus. The concentration of TBT-d27 in mucus was approximately 1/100 of that in the serum. Western blotting analysis revealed that TBT-bp1 was present in the skin mucus. These results suggest that TBT-bp1 in Japanese flounder binds with TBT and is excreted from the body via the mucus.

元の言語英語
ページ(範囲)292-299
ページ数8
ジャーナルAquatic Toxicology
90
発行部数4
DOI
出版物ステータス出版済み - 12 11 2008

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Lipocalins
Flounder
Paralichthys olivaceus
tributyltin
excretion
binding proteins
Carrier Proteins
Mucus
protein
mucus
skin (animal)
Proteins
proteins
Skin
blood
flounder
skin
blood serum
Introns
exons

All Science Journal Classification (ASJC) codes

  • Aquatic Science
  • Health, Toxicology and Mutagenesis

これを引用

Tributyltin-binding protein type 1 has a distinctive lipocalin-like structure and is involved in the excretion of tributyltin in Japanese flounder, Paralichthys olivaceus. / Satone, Hina; Oshima, Yuji; Shimasaki, Yohei; Tawaratsumida, Takahiko; Oba, Yumi; Takahashi, Eriko; Kitano, Takeshi; Kawabata, Shun-Ichiro; Kakuta, Yoshimitsu; Honjo, Tsuneo.

:: Aquatic Toxicology, 巻 90, 番号 4, 11.12.2008, p. 292-299.

研究成果: ジャーナルへの寄稿記事

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abstract = "Tributyltin-binding protein type 1 (TBT-bp1) is a newly discovered protein that binds with TBT in the blood of the Japanese flounder, Paralichthys olivaceus. We determined the genomic sequence of TBT-bp1 and found that this protein has a conserved exon-intron structure that is common to the lipocalin protein family. The secondary and tertiary structures of TBT-bp1, predicted from amino acid sequence, included at least two α-helices and eight β-sheets that are conserved in all lipocalins and form a barrel structure that may bind with ligands. Analysis of the gene structure, secondary structure, and tertiary structure demonstrated that TBT-bp1 could be classified as a lipocalin. A homology search revealed the presence of TBT-bp1-like proteins in eight species of teleost. When flounder were injected intraperitoneally with TBT-d27 at 11.6 μg/fish, TBT-d27 was detected in the blood and in the skin mucus. The concentration of TBT-d27 in mucus was approximately 1/100 of that in the serum. Western blotting analysis revealed that TBT-bp1 was present in the skin mucus. These results suggest that TBT-bp1 in Japanese flounder binds with TBT and is excreted from the body via the mucus.",
author = "Hina Satone and Yuji Oshima and Yohei Shimasaki and Takahiko Tawaratsumida and Yumi Oba and Eriko Takahashi and Takeshi Kitano and Shun-Ichiro Kawabata and Yoshimitsu Kakuta and Tsuneo Honjo",
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AU - Satone, Hina

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AU - Shimasaki, Yohei

AU - Tawaratsumida, Takahiko

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AU - Takahashi, Eriko

AU - Kitano, Takeshi

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AU - Kakuta, Yoshimitsu

AU - Honjo, Tsuneo

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