Change in the transfer profile of orally administered tetrodotoxin to non-toxic cultured pufferfish Takifugu rubripes depending of its development stage

Tatsuno, Ryohei; Shikina, Miwako; Shirai, Yuko; Wang, Junjie; Soyano, Kiyoshi; Nishihara, Gregory N.; Takatani, Tomohiro; Arakawa, Osamu

doi:10.1016/j.toxicon.2013.01.011

Cited by 33 publications

(30 citation statements)

References 20 publications

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“…TTX in marine animals is thought to come from external origin, since TTX-producing marine bacteria have been reported [17,18], and pufferfish has been experimentally shown to have an ability to accumulate TTX administrated dietarily [19,20] and intramuscularly [21,22,23]. However, the origin of TTX in amphibians is still controversial [24], and the biosynthetic pathways of TTX in both marine and terrestrial organisms still remain to be clarified.…”

Section: Introductionmentioning

confidence: 99%

First Identification of 5,11-Dideoxytetrodotoxin in Marine Animals, and Characterization of Major Fragment Ions of Tetrodotoxin and Its Analogs by High Resolution ESI-MS/MS

et al. 2013

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Even though tetrodotoxin (TTX) is a widespread toxin in marine and terrestrial organisms, very little is known about the biosynthetic pathway used to produce it. By describing chemical structures of natural analogs of TTX, we can start to identify some of the precursors that might be important for TTX biosynthesis. In the present study, an analog of TTX, 5,11-dideoxyTTX, was identified for the first time in natural sources, the ovary of the pufferfish and the pharynx of a flatworm (planocerid sp. 1), by comparison with totally synthesized (−)-5,11-dideoxyTTX, using high resolution ESI-LC-MS. Based on the presence of 5,11-dideoxyTTX together with a series of known deoxy analogs, 5,6,11-trideoxyTTX, 6,11-dideoxyTTX, 11-deoxyTTX, and 5-deoxyTTX, in these animals, we predicted two routes of stepwise oxidation pathways in the late stages of biosynthesis of TTX. Furthermore, high resolution masses of the major fragment ions of TTX, 6,11-dideoxyTTX, and 5,6,11-trideoxyTTX were also measured, and their molecular formulas and structures were predicted to compare them with each other. Although both TTX and 5,6,11-trideoxyTTX give major fragment ions that are very close, m/z 162.0660 and 162.1020, respectively, they are distinguishable and predicted to be different molecular formulas. These data will be useful for identification of TTXs using high resolution LC-MS/MS.

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Section: Introductionmentioning

confidence: 99%

First Identification of 5,11-Dideoxytetrodotoxin in Marine Animals, and Characterization of Major Fragment Ions of Tetrodotoxin and Its Analogs by High Resolution ESI-MS/MS

et al. 2013

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“…The epithelial gland cells take up different compounds from transport systems, which include blood and lymphatic systems, the coelomic cavity, parenchymal tissue, etc. The role of transport systems in TTX transfer to target organs has been confirmed for puffer fishes [98,99,100]. For example, TTX administered to nontoxic puffer fish T. rubripes intravenously accumulated predominantly in the skin and liver within 12 hours [98].…”

Section: Discussionmentioning

confidence: 99%

“…For example, TTX administered to nontoxic puffer fish T. rubripes intravenously accumulated predominantly in the skin and liver within 12 hours [98]. Only one way of TTX transferring into the transport system through the intestine has been proven to date [98,99,100]. TTX administered into the gastrointestinal tract of nontoxic puffer fish T. rubripes was detected in the blood within 30 minutes [98].…”

Section: Discussionmentioning

confidence: 99%

Tetrodotoxin-Producing Bacteria: Detection, Distribution and Migration of the Toxin in Aquatic Systems

Magarlamov

Melnikova

Chernyshev

2017

Toxins

126

105

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This review is devoted to the marine bacterial producers of tetrodotoxin (TTX), a potent non-protein neuroparalytic toxin. In addition to the issues of the ecology and distribution of TTX-producing bacteria, this review examines issues relating to toxin migration from bacteria to TTX-bearing animals. It is shown that the mechanism of TTX extraction from toxin-producing bacteria to the environment occur through cell death, passive/active toxin excretion, or spore germination of spore-forming bacteria. Data on TTX microdistribution in toxic organs of TTX-bearing animals indicate toxin migration from the digestive system to target organs through the transport system of the organism. The role of symbiotic microflora in animal toxicity is also discussed: despite low toxin production by bacterial strains in laboratory conditions, even minimal amounts of TTX produced by intestinal microflora of an animal can contribute to its toxicity. Special attention is paid to methods of TTX detection applicable to bacteria. Due to the complexity of toxin detection in TTX-producing bacteria, it is necessary to use several methods based on different methodological approaches. Issues crucial for further progress in detecting natural sources of TTX investigation are also considered.

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“…For example, Kono et al [ 23 ] reported that dietary TTX administered to cultured juvenile Takifugu alboplumbeus was accumulated in the liver and then gradually moved to the skin. Tatsuno and Arakawa et al [ 24 , 25 ] reported that accumulated TTX in the liver is transferred to pufferfish ovaries depending on its stage of development and maturation. We found PSTBP in the pufferfish of the genus Takifugu , and proposed it is implicated in accumulation of TTX [ 1 , 4 ].…”

Section: Discussionmentioning

confidence: 99%

Pufferfish Saxitoxin and Tetrodotoxin Binding Protein (PSTBP) Analogues in the Blood Plasma of the Pufferfish Arothron nigropunctatus, A. hispidus, A. manilensis, and Chelonodon patoca

et al. 2018

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Pufferfish saxitoxin and tetrodotoxin (TTX) binding protein (PSTBP) is a glycoprotein that we previously isolated from the blood plasma of the pufferfish Takifugu pardalis; this protein was also detected in seven species of the genus Takifugu. We proposed that PSTBP is a carrier protein for TTX in pufferfish; however, PSTBP had not yet been found in genera other than Takifugu. In this study, we investigated the presence of PSTBP-like proteins in the toxic pufferfish Arothron nigropunctatus, A. hispidus, A. manilensis, and Chelonodon patoca. On the basis of ultrafiltration experiments, TTX was found to be present and partially bound to proteins in the plasma of these pufferfish, and Western blot analyses with anti-PSTBP antibody revealed one or two bands per species. The observed decreases in molecular mass following deglycosylation with glycopeptidase F suggest that these positive proteins are glycoproteins. The molecular masses of the deglycosylated proteins detected in the three Arothron species were larger than that of PSTBP in the genus Takifugu, whereas the two bands detected in C. patoca had molecular masses similar to that of tributyltin-binding protein-2 (TBT-bp2). The N-terminal amino acid sequences of 23–29 residues of these detected proteins were all homologous with those of PSTBP and TBT-bp2.

show abstract

Change in the transfer profile of orally administered tetrodotoxin to non-toxic cultured pufferfish Takifugu rubripes depending of its development stage

Cited by 33 publications

References 20 publications

First Identification of 5,11-Dideoxytetrodotoxin in Marine Animals, and Characterization of Major Fragment Ions of Tetrodotoxin and Its Analogs by High Resolution ESI-MS/MS

First Identification of 5,11-Dideoxytetrodotoxin in Marine Animals, and Characterization of Major Fragment Ions of Tetrodotoxin and Its Analogs by High Resolution ESI-MS/MS

Tetrodotoxin-Producing Bacteria: Detection, Distribution and Migration of the Toxin in Aquatic Systems

Pufferfish Saxitoxin and Tetrodotoxin Binding Protein (PSTBP) Analogues in the Blood Plasma of the Pufferfish Arothron nigropunctatus, A. hispidus, A. manilensis, and Chelonodon patoca

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