RT-PCR- and MALDI-TOF Mass Spectrometry-Based Identification and Discrimination of Isoforms Homologous to Pufferfish Saxitoxin- and Tetrodotoxin-Binding Protein in the Plasma of Non-Toxic Cultured Pufferfish (<i>Takifugu rubripes</i>)

Tatsuno, Ryohei; Yamaguchi, Kensei; Takatani, Tomohiro; Arakawa, Osamu

doi:10.1271/bbb.120701

Cited by 25 publications

(12 citation statements)

References 19 publications

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“…Although PYP1 was identified from the 10-kDa band following SDS-PAGE, the sequence mass of mature PYP1 was calculated as 5,763.3 Da. This observation indicates that PYP1 forms an SDS-resistant dimer, as reported in certain other proteins (22,23). As reported previously, PYP proteins are heat-soluble (7).…”

Section: Discussionsupporting

confidence: 87%

Chemical and mass spectrometry characterization of the red alga Pyropia yezoensis chemoprotective protein (PYP): Protective activity of the N-terminal fragment of PYP1 against acetaminophen-induced cell death in Chang liver cells

Choi

Yamaguchi

Oda

et al. 2014

International Journal of Molecular Medicine

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In the present study, the chemical structure and chemoprotective activity of Pyropia yezoensis protein (PYP) were investigated using sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, automated protein sequencing, matrix-assisted laser desorption/ionization-quadrupole ion trap-time-of-flight mass spectrometry and a chemoprotective assay using a synthetic peptide. The PYP fraction was demonstrated to contain two proteins: PYP1 (10 kDa, SDS-resistant dimer) and PYP2 (10 kDa). PYP1 is a novel protein showing sequence homology with the hypothetical function-unknown proteins of Chondrus crispus (Rhodophyta) and Emiliania huxleyi (Haptophyceae). PYP2 is a paralog of an extrinsic protein of photosystem II found in other Rhodophyta. The synthetic peptide PYP1 (1-20), corresponding to the N-terminal 20 residues of PYP1 (ALEGGKSSGGGEATRDPEPT), exhibits chemoprotective activity against acetaminophen-induced cell death in Chang liver cells, indicating that PYP1 is a chemoprotectant of the PYP fraction. A possible association between the structure of PYP and its chemoprotective activity is discussed.

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Section: Discussionsupporting

confidence: 87%

Chemical and mass spectrometry characterization of the red alga Pyropia yezoensis chemoprotective protein (PYP): Protective activity of the N-terminal fragment of PYP1 against acetaminophen-induced cell death in Chang liver cells

Choi

Yamaguchi

Oda

et al. 2014

International Journal of Molecular Medicine

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“…Yotsu-Yamashita et al [ 48 ] isolated a soluble glycoprotein that binds to STX and TTX from the blood plasma of T. pardalis , and named it the pufferfish saxitoxin and tetrodotoxin binding protein (PSTBP). PSTBP homologous proteins are widely distributed in toxic pufferfish of the genera Takifugu and Arothron , but not found in nontoxic pufferfish species or general fish, and are suggested to be involved in the absorption, transportation, and accumulation of TTX in pufferfish [ 49 , 50 , 51 ]. On the other hand, an ongoing study indicates that freshwater pufferfish of the genus Pao do not have the PSTBP gene (Yamada et al, unpublished data).…”

Section: Discussionmentioning

confidence: 99%

Co-Occurrence of Tetrodotoxin and Saxitoxins and Their Intra-Body Distribution in the Pufferfish Canthigaster valentini

Zhu

Sonoyama²,

Yamada

et al. 2020

Toxins

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Pufferfish of the family Tetraodontidae possess tetrodotoxin (TTX) and/or saxitoxins (STXs), but the toxin ratio differs, depending on the genus or species. In the present study, to clarify the distribution profile of TTX and STXs in Tetraodontidae, we investigated the composition and intra-body distribution of the toxins in Canthigaster valentini. C. valentini specimens (four male and six female) were collected from Amami-Oshima Island, Kagoshima Prefecture, Japan, and the toxins were extracted from the muscle, liver, intestine, gallbladder, gonads, and skin. Analysis of the extracts for TTX by liquid chromatography tandem mass spectrometry and of STXs by high-performance liquid chromatography with post-column fluorescence derivatization revealed TTX, as well as a large amount of STXs, with neoSTX as the main component and dicarbamoylSTX and STX itself as minor components, in the skin and ovary. The toxins were also detected in the other tissues, but in much lower amounts than in the skin and ovary. The TTX/STX ratio varied greatly, depending on the tissue, but TTX was the major toxin component in the whole body, and STXs accounted for 25% and 13% of the total toxin amount in males and females, respectively. Like the marine pufferfish of the genus Arothron, C. valentini should be considered a pufferfish with considerable amounts of both TTX and STXs present simultaneously.

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“…Yotsu-Yamashita et al [ 39 ] reported liver-specific expression of pufferfish saxitoxin and tetrodotoxin binding protein (PSTBP) in the marine pufferfish, T. pardalis . In addition, Tatsuno et al [ 40 ] found four genes (Tr1–Tr4) encoding PSTBP homologs from the publicly available Fugu genome database and revealed the constitutive expression of two distinct isoforms (Tr1 and Tr3) in the liver of cultured non-toxic T. rubripes specimens, declining in their toxin-triggered gene expression. In this study, the expression change of genes encoding PSTBP homologs was hardly observed.…”

Section: Discussionmentioning

confidence: 99%

DNA Microarray Analysis on the Genes Differentially Expressed in the Liver of the Pufferfish, Takifugu rubripes, Following an Intramuscular Administration of Tetrodotoxin

et al. 2014

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Pufferfish accumulate tetrodotoxin (TTX) mainly in the liver and ovary. This study aims at investigating the effect of TTX accumulation in the liver of cultured specimens of torafugu Takifugu rubripes on the hepatic gene expression by microarray analysis on Day 5 after the intramuscular administration of 0.25 mg TTX/kg body weight into the caudal muscle. TTX was detected in the liver, skin and ovary in the TTX-administered individuals. The total amount of TTX accumulated in the body was 67 ± 8% of the administered dose on Day 5. Compared with the buffer-administered control group, a total of 59 genes were significantly upregulated more than two-fold in the TTX-administered group, including those encoding chymotrypsin-like elastase family member 2A, transmembrane protein 168 and Rho GTP-activating protein 29. In contrast, a total of 427 genes were downregulated by TTX administration, including those encoding elongation factor G2, R-spondin-3, nuclear receptor activator 2 and fatty acyl-CoA hydrolase precursor. In conclusion, our results demonstrate that the intramuscular administration of TTX changes the expression of hepatic genes involved in various signaling pathways.

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RT-PCR- and MALDI-TOF Mass Spectrometry-Based Identification and Discrimination of Isoforms Homologous to Pufferfish Saxitoxin- and Tetrodotoxin-Binding Protein in the Plasma of Non-Toxic Cultured Pufferfish (Takifugu rubripes)

Cited by 25 publications

References 19 publications

Chemical and mass spectrometry characterization of the red alga Pyropia yezoensis chemoprotective protein (PYP): Protective activity of the N-terminal fragment of PYP1 against acetaminophen-induced cell death in Chang liver cells

Chemical and mass spectrometry characterization of the red alga Pyropia yezoensis chemoprotective protein (PYP): Protective activity of the N-terminal fragment of PYP1 against acetaminophen-induced cell death in Chang liver cells

Co-Occurrence of Tetrodotoxin and Saxitoxins and Their Intra-Body Distribution in the Pufferfish Canthigaster valentini

DNA Microarray Analysis on the Genes Differentially Expressed in the Liver of the Pufferfish, Takifugu rubripes, Following an Intramuscular Administration of Tetrodotoxin

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