Amino acid sequence of two sea anemone toxins from Anthopleura fuscoviridis

Sunahara, Satoshi; Muramoto, Koji; Tenma, Kyosuke; Kamiya, Hisao

doi:10.1016/0041-0101(87)90243-1

Cited by 41 publications

(16 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…ATX-II was obtained from Sigma, and AFT-II was a kind gift from Dr. Koji Muramoto (Department of Biological Science at Tohoku University) (4). All of the chemicals were of the highest purity available, and double-distilled water was used throughout.…”

Section: Bc-iii Purificationmentioning

confidence: 99%

“…We used three sea anemone toxins, which have a range of sequence similarity, that were purified from different animals: the well known Anemonia sulcata ATX-II peptide (3); the Anthopleura fuscoviridis AFT-II peptide (4); and the Bunodosoma caissarum Bc-III peptide (5). They are all 47-48-aa-long and have three disulfide bonds; however, interestingly, two peptides (ATX-II and AFT-II) differ by only one amino acid, whereas Bc-III has only a 70% identity.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Binding Specificity of Sea Anemone Toxins to Nav 1.1-1.6 Sodium Channels

Oliveira

Redaelli

Zaharenko

et al. 2004

Journal of Biological Chemistry

102

View full text Add to dashboard Cite

Sea anemones are an important source of various biologically active peptides, and it is known that ATX-II from Anemonia sulcata slows sodium current inactivation. Using six different sodium channel genes (from Na v 1.1 to Na v 1.6), we investigated the differential selectivity of the toxins AFT-II (purified from Anthopleura fuscoviridis) and Bc-III (purified from Bunodosoma caissarum) and compared their effects with those recorded in the presence of ATX-II. Interestingly, ATX-II and AFT-II differ by only one amino acid (L36A) and Bc-III has 70% similarity. The three toxins induced a low voltage-activated persistent component primarily in the Na v 1.3 and Na v 1.6 channels. An analysis showed that the 18 dose-response curves only partially fit the hypothesized binding of Lys-37 (sea anemone toxin Anthopleurin B) to the Asp (or Glu) residue of the extracellular IV/S3-S4 loop in cardiac (or nervous) Na ؉ channels, thus suggesting the substantial contribution of some nearby amino acids that are different in the various channels. As these channels are atypically expressed in mammalian tissues, the data not only suggest that the toxicity is highly dependent on the channel type but also that these toxins and their various physiological effects should be considered prototype models for the design of new and specific pharmacological tools.

show abstract

Section: Bc-iii Purificationmentioning

confidence: 99%

mentioning

confidence: 99%

Binding Specificity of Sea Anemone Toxins to Nav 1.1-1.6 Sodium Channels

Oliveira

Redaelli

Zaharenko

et al. 2004

Journal of Biological Chemistry

102

View full text Add to dashboard Cite

show abstract

“…The corresponding three-dimensional representation in Figure 4 results in The sequences were obtained from the following papers: AeI (Actinia equina): [27], AETX I (Anemonia erythraea): [28], APE 1-1, APE 1-2, APE 2-1 (Anthopleura elegantissima): [29], AFT-I, AFT-II (Anthopleura fuscoviridis): [30], ATX-Ia, ATX-I, ATX-II, ATX-V ATX-III, ATX-IV (Anemonia sulcata): [31][32][33][34][35][36], Ap-A, Ap-B, PCR1-2, PCR 2-1, PCR2-5, PCR 2-10, PCR 3-3, PCR 3-6, PCR 3-7 (Anthopleura xanthogrammica): [37][38][39], BcIII (Bunodosoma caissarum): [40], Bg II, Bg III (Bunodosoma granulifera): [41], Cp II (Condylactis passiflora): [42], RTX-I, RTX-II, RTX-III, RTX-IV, RTX-V (Radianthus macrodactylus/previously Heteractis macrodactylus): [43][44][45], RpII, RpIII (Radianthus paumotensis/previously Heteractis magnífica or Heteractis paumotensis): [46][47], Sh I (Stichodactylae helianthus): [48], CLX-I, CLX-II (Calliactis parasitica): [19], Halcurin (Halcurias carlgreni): [49], PA-TX (Parasicyonis actinostoloides/previously Entacmaea quadricolor): [50].…”

Section: Resultsmentioning

confidence: 99%

Functional discrimination of sea anemone neurotoxins using 3D-plotting

et al. 2009

View full text Add to dashboard Cite

Abstract:One of the most important goals in structural biology is the identification of functional relationships among the structure of proteins and peptides. The purpose of this study was to (1) generate a model based on theoretical and computational considerations among amino acid sequences within select neurotoxin peptides, and (2) compare the relationship these values have to the various toxins tested. We employed isolated neurotoxins from sea anemones with established specific potential to act on voltage-dependent sodium and potassium channel activity as our model. Values were assigned to each amino acid in the peptide sequence of the neurotoxins tested using the Number of Lareo and Acevedo algorithm (NULA). Once the NULA number was obtained, it was then plotted using three dimensional space coordinates. The results of this study allow us to report, for the first time, that there is a different numerical and functional relationship between the sequences of amino acids from sea anemone neurotoxins, and the resulting numerical relationship for each peptide, or NULA number, has a unique location in three-dimensional space.

show abstract

“…9 ) The final purification was achieved by reversed-phase HPLC to give three toxins, AFT-I, AFT-II, and AFT-III. The yields of these toxins were SS.9mg/kg, S3.7mg/kgj and 2.1 mg/kg, respectively.…”

Section: Hydrolysis Of Dns Amino Acidsmentioning

confidence: 99%