Sea anemone venom as a source of insecticidal peptides acting on voltage-gated Na+ channels

Bosmans, Frank; Tytgat, Jan

doi:10.1016/j.toxicon.2006.11.029

Cited by 99 publications

(71 citation statements)

References 71 publications

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“…These include neurotoxins, cytolysins, toxic phospholipases, many peptidases, and proteins of the SCP_GAPR-1-like family (supplemental Table 1). Their molecular masses range from 25 to 100 kDa, indicating a lack of small peptide toxins affecting Na ϩ and K ϩ channels identified in many sea anemones (31,32). Four venom sequences are cnidarian-specific (supplemental Table 1), and most venom proteins are part of the soluble nematocyst proteome (Fig.…”

Section: Resultsmentioning

confidence: 99%

Proteome of Hydra Nematocyst

Balasubramanian

Beckmann

Warnken

et al. 2012

Journal of Biological Chemistry

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Background: Nematocysts are the most sophisticated organelles in the animal kingdom and a hallmark of the phylum Cnidaria.Results: We present the first complete protein map of the Hydra nematocyst. Conclusion:The nematocyst proteome is highly complex and includes novel structural proteins. Significance: The proteome data reveal a eukaryotic origin of the nematocyst and point to common molecular features with the extracellular matrix.

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Section: Resultsmentioning

confidence: 99%

Proteome of Hydra Nematocyst

Balasubramanian

Beckmann

Warnken

et al. 2012

Journal of Biological Chemistry

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“…Sea anemones are a known pharmacological treasure of biological active compounds acting upon a diverse panel of ion channels such as TRPV1, voltage-gated sodium and potassium channels [8][9][10][11]. Of these different toxins those that target sodium channels are the best studied group with more then 100 known toxins [12]. In contrast, no more then 12 potassium channel toxins have been characterized to date.…”

Section: Introductionmentioning

confidence: 99%

A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties

Peigneur¹,

Billen²,

Derua³

et al. 2011

Biochemical Pharmacology

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104

101

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Page 1 of 22A c c e p t e d M a n u s c r i p t Abstract Sea anemone venom is a known source of interesting bioactive compounds, including peptide toxins which are invaluable tools for studying structure and function of voltage-gated potassium channels. APEKTx1 is a novel peptide isolated from the sea anemone Anthopleura elegantissima, containing 63 amino acids cross-linked by 3 disulfide bridges. Sequence alignment reveals that APEKTx1 is a new member of the type 2 sea anemone peptides targeting voltage-gated potassium channels (K V 's), which also include the kalicludines from Anemonia sulcata. Similar to the kalicludines, APEKTx1 shares structural homology with both the basic pancreatic trypsin inhibitor (BPTI), a very potent Kunitz-type protease inhibitor, and dendrotoxins which are powerful blockers of voltage-gated potassium channels. In this study, APEKTx1 has been subjected to a screening on a wide range of 23 ion channels expressed in Xenopus leavis oocytes: 13 cloned voltage-gated potassium channels (K V 1.1-K V 1.6, K V 1.1 triple mutant, K V 2.1, K V 3.1, K V 4.2, K V 4.3, hERG, the insect channel Shaker IR), 2 cloned hyperpolarization-activated cyclic nucleotidesensitive cation non-selective channels (HCN1 and HCN2) and 8 cloned voltage-gated sodium channels (Na V 1.2-Na V 1.8 and the insect channel DmNa V 1). Our data shows that APEKTx1 selectively blocks K V 1.1 channels in a very potent manner with an IC 50 value of 0.9 nM. Furthermore, we compared the trypsin inhibitory activity of this toxin with BPTI. APEKTx1 inhibits trypsin with a dissociation constant of 124 nM. In conclusion, this study demonstrates that APEKTx1 has the unique feature to combine the dual functionality of a potent and selective blocker of K V 1.1 channels with that of a competitive inhibitor of trypsin.Keywords Anthopleura elegantissima · K V channel inhibitor · sea anemone toxin · protease inhibitor ·

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“…Sea anemones were named after a terrestrial flower and have a central mouth surrounded by tentacles in a symmetrical structure (2). There are symbiotic relationships between some sea anemones and some clown fish (3).…”

Section: Introductionmentioning

confidence: 99%

Differential susceptibilities of human lung, breast and skin cancer cell lines to killing by five sea anemone venoms

Ramezanpour¹,

Silva²,

Sanderson³

2012

J. Venom. Anim. Toxins incl. Trop. Dis

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Although sea anemones are well known for being rich sources of toxins, including cytolysins and neurotoxins, their venoms and toxins have been poorly studied. In the present study, the venoms from five sea anemones (Heteractis crispa, Heteractis magnifica, Heteractis malu, Cryptodendrum adhaesivum and Entacmaea quadricolor) were obtained by the milking technique, and the potential of these venoms to kill cancer cells was tested on three cell lines (A549 lung cancer, T47D breast cancer and A431 skin cancer). The total protein level in the crude extract was determined by the bicinchoninic acid (BCA) protein assay. The cytotoxicity on different cell lines was assayed using the 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) assay which measures survival based on the detection of mitochondrial activity and by the crystal violet assay, which measures survival based on the ability of cells to remain adherent to microplates. The results indicate that the sea anemone venom is cytotoxic to human cancer cells. The A549 cell line was the most sensitive of the cell lines tested with a significant reduction in viability observed at 40 µg/mL. H. malu, C. adhaesivum and E. quadricolor had a significant inhibitory effect on A431 cells. Furthermore, H. malu and C. adhaesivum had a significant inhibitory effect on T47D cell line at 40 µg/mL. In conclusion, the sea anemone venoms tested have the potential to be developed as anticancer agents.

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Sea anemone venom as a source of insecticidal peptides acting on voltage-gated Na+ channels

Cited by 99 publications

References 71 publications

Proteome of Hydra Nematocyst

Proteome of Hydra Nematocyst

A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties

Differential susceptibilities of human lung, breast and skin cancer cell lines to killing by five sea anemone venoms

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