Tributyltin-binding protein type 1, a lipocalin, prevents inhibition of osteoblastic activity by tributyltin in fish scales

Hina Satone, Jae Man Lee, Yumi Oba, Takahiro Kusakabe, Eriko Akahoshi, Shizuho Miki, Nobuo Suzuki, Yuichi Sasayama, Mohamed Nassef, Yohei Shimasaki, Shun ichiro Kawabata, Tsuneo Honjo, Yuji Oshima

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

Tributyltin-binding protein type 1 (TBT-bp1) is a member of the lipocalin family of proteins which bind to small hydrophobic molecules. In this study, we expressed a recombinant TBT-bp1 (rTBT-bp1, ca. 35. kDa) in a baculovirus expression system and purified the protein from the hemolymph of silkworm larvae injected with recombinant baculovirus. After incubation of a mixture of rTBT-bp1 and TBT and its fractionation by means of gel filtration chromatography, TBT was detected in the elution peak of rTBT-bp1, confirming the binding potential of rTBT-bp1 for TBT. An assay of the ability of rTBT-bp1 or native TBT-bp1 (nTBT-bp1) to restore osteoblastic activity inhibited by TBT showed that co-treatment of the scales with rTBT-bp1 or nTBT-bp1 in combination with TBT restored osteoblastic activity in goldfish scales, whereas treatment with TBT alone significantly inhibited osteoblastic activity. These results suggest that TBT-bp1 as a lipocalin member might function to decrease the toxicity of TBT by binding to TBT.

Original languageEnglish
Pages (from-to)79-84
Number of pages6
JournalAquatic Toxicology
Volume103
Issue number1-2
DOIs
Publication statusPublished - May 1 2011

Keywords

  • Detoxicification
  • Endocrine disruptor
  • Recombinant
  • TBT-bp1
  • Tributyltin

ASJC Scopus subject areas

  • Aquatic Science
  • Health, Toxicology and Mutagenesis

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