Sea Anemone Polypeptide Toxins Affecting Sodium Channels

1990 ◽  
pp. 279-289 ◽  
Author(s):  
William R. Kem ◽  
Michael W. Pennington ◽  
Ben M. Dunn
Keyword(s):  
Sodium Channels ◽  
Sea Anemone

scholarly journals Neuro- and Cardiotoxins from Sea Anemones: Structure, Function and Potential of Application in Research and Medical Practice

2019 ◽  
Vol 3 (2) ◽  
pp. 117-136
Author(s):  
Kalina R.S. Monastyrnaya M.M.
Keyword(s):  
Sodium Channels ◽  
Fluorescent Proteins ◽  
World Ocean ◽  
Chemical Warfare Agents ◽  
Sea Anemone ◽  
Biologically Active ◽  
Sea Anemones ◽  
Separate Object ◽  
Warfare Agents ◽  
Main Instrument

Sea anemones are well-spread everywhere in the World Ocean and represent the most ancient active poisonous organisms. Their main instrument of attack on other animals are the nematocysts – stinging organelles with the curtailed hollow thread with poisonous edge on the end. In order to attract their potential victims, they use fluorescent proteins. These proteins became a separate object of research as genetically coded markers for the observation of activity of promotors of genes. The poisonous secret of sea anemones is characterized by the presence of maximum number of peptides of various structural classes and spatial structures among the studied land and marine organisms (bees, spiders, scorpions, snakes ect.). This fact complicates the identification of sea anemones' secret and its differentiation from poisons of animals of other taxons, if the concrete source of its origin is unknown. The toxicity of some biologically active sea anemone peptides (RpI, RpIII) at intravenous administration to experimental animals is comparable with that of the most well-known and dangerous representatives of natural toxins with the similar mechanism of action (an alpha-hemolysine and tetrodotoxin), or chemical warfare agents, such as sarin and hydrogen cyanide. Based on their toxic effect, the biologically active sea anemone peptides generally can be classified as neurotoxins due to their impact on the functioning of sodium channels in the cells of the nervous system of animals. cardiotoxic effect of sea anemone secret is caused by the specificity of interaction between its separate neurotoxins and one of the sub-types of sodium channels of muscle cells, characteristic for heart tissues. The main ways of identification of sea anemone neurotoxins in samples (for example, during the investigation of biological crimes) can be sequence by Edman`s method or tandem mass spectrometry (the analysis of fragments of toxin molecule for the establishment of its structure). Further study on the mechanisms of interaction between the sea anemone neurotoxins and the ion channels of the cells of nervous and muscular systems may result in the creation of medicines for treatment of channelopathy, as well as pluripotential antidotes, blocking the toxins, that influence on sodium channels

The specificity of Av3 sea anemone toxin for arthropods is determined at linker DI/SS2–S6 in the pore module of target sodium channels

2014 ◽  
Vol 463 (2) ◽  
pp. 271-277 ◽  
Author(s):  
Maya Gur Barzilai ◽  
Roy Kahn ◽  
Noa Regev ◽  
Dalia Gordon ◽  
Yehu Moran ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Sodium Channels ◽  
Receptor Site ◽  
Sea Anemone ◽  
Sea Anemone Toxin

A sodium channel determinant that dictates the specificity of Av3 sea anemone toxin for arthropods was identified using channel-swapping experiments and mutagenesis. This finding provides a clue as to the receptor site of Av3 on the sodium channel.

Expression and Mutagenesis of the Sea Anemone Toxin Av2 Reveals Key Amino Acid Residues Important for Activity on Voltage-Gated Sodium Channels†

Biochemistry ◽  
2006 ◽  
Vol 45 (29) ◽  
pp. 8864-8873 ◽  
Author(s):  
Yehu Moran ◽  
Lior Cohen ◽  
Roy Kahn ◽  
Izhar Karbat ◽  
Dalia Gordon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sodium Channels ◽  
Sea Anemone ◽  
Amino Acid Residues ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Sea Anemone Toxin

scholarly journals Binding Specificity of Sea Anemone Toxins to Nav1.1-1.6 Sodium Channels

2004 ◽  
Vol 279 (32) ◽  
pp. 33323-33335 ◽  
Author(s):  
Joacir Stolarz Oliveira ◽  
Elisa Redaelli ◽  
André J. Zaharenko ◽  
Rita Restano Cassulini ◽  
Katsuhiro Konno ◽  
...  
Keyword(s):  
Sodium Channels ◽  
Binding Specificity ◽  
Sea Anemone

Type 2 sea anemone toxins compete with type 1 sea anemone and scorpion alpha-toxins for binding to nerve sodium channels

Toxicon ◽  
1995 ◽  
Vol 33 (3) ◽  
pp. 268-269
Author(s):  
W.R. Kem ◽  
V.M. Mahnir ◽  
M.W. Pennington
Keyword(s):  
Sodium Channels ◽  
Sea Anemone

scholarly journals Binding specificity of sea anemone toxins to Nav 1.1-1.6 sodium channels. Unexpected contributions from differences in the IV/S3-S4 outer loop. Vol. 279 (2004) 33323-33335

2004 ◽  
Vol 279 (42) ◽  
pp. 44229-44230
Author(s):  
Joacir Stolarz Oliveira ◽  
Elisa Redaelli ◽  
André J. Zaharenko ◽  
Rita Restano Cassulini ◽  
Katsuhiro Konno ◽  
...  
Keyword(s):  
Sodium Channels ◽  
Binding Specificity ◽  
Sea Anemone ◽  
Outer Loop

New Sea Anemone Toxin RTX-VI Selectively Modulates Voltage-Gated Sodium Channels

2020 ◽  
Vol 495 (1) ◽  
pp. 292-295
Author(s):  
R. S. Kalina ◽  
S. Peigneur ◽  
I. N. Gladkikh ◽  
P. S. Dmitrenok ◽  
N. Y. Kim ◽  
...  
Keyword(s):  
Sodium Channels ◽  
Sea Anemone ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Sea Anemone Toxin
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