Toxic effects of the novel protein UPI from the sea anemone

Cline, Edith I.; Wiebe, Leonard I.; Young, James D.; Samuel, John

doi:10.1016/s1043-6618(05)80020-9

Cited by 22 publications

(10 citation statements)

References 24 publications

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“…Chemotherapeutic agents induce apoptosis in cancer cells via a variety of mechanisms (Cline et al 1995;Lowe et al 2004). Caspases perform critically important roles in the induction of apoptosis (Friesen et al 2008).…”

Section: H Magnifica Venom Extract Induces Apoptosis Of T47d and Mcfmentioning

confidence: 99%

The effect of sea anemone (H. magnifica) venom on two human breast cancer lines: death by apoptosis

2013

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Venom from the sea anemone, Heteractis magnifica, has multiple biological effects including, cytotoxic, cytolytic and hemolytic activities. In this study, cytotoxicity induced by H. magnifica venom was investigated using the crystal violet assay on human breast cancer T47D and MCF7 cell lines and normal human breast 184B5 cell line. Apoptosis was also assayed via Annexin V-flourescein isothiocyanate and propidium iodide (PI) staining followed by flow cytometric analysis. Cell cycle progression and mitochondria membrane potential were studied via flow cytometry following PI and JC-1 staining respectively. H. magnifica venom induced significant reductions in viable cell numbers and increases in apoptosis in T47D and MCF7 in dose-dependent manners. A significant apoptosisrelated increase in the sub G1 peak of the cell cycle in both breast cancer cell lines was also observed. Moreover, treatment by venom cleaved caspase-8, caspase-9, and activated caspase-3. Overall, H. magnifica venom was highly cytotoxic to T47D and MCF7 human breast cancer cells, and the phenomenon could be the killing phenomenon via the death receptor-mediated and the mitochondria-mediated apoptotic pathways. Consequently, H. magnifica venom has potential for the development of a breast cancer therapeutic.

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Section: H Magnifica Venom Extract Induces Apoptosis Of T47d and Mcfmentioning

confidence: 99%

The effect of sea anemone (H. magnifica) venom on two human breast cancer lines: death by apoptosis

2013

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“…Their diverse assemblage of proteinaceous toxins includes phospholipases, neurotoxins, protease inhibitors, and pore-forming toxins [1]. Pore-forming toxins are widespread in Cnidaria and include membrane attack complex component/perforin (MACPF) toxins [2], phospholipase-like cytolysins [3], fire coral cytotoxins [4], hydralysins [5,6], box jellyfish cytotoxins [7], and actinoporins [8]. Among these, actinoporins remain the best studied group and are found exclusively in sea anemones.…”

Section: Introductionmentioning

confidence: 99%

Evolution of the Cytolytic Pore-Forming Proteins (Actinoporins) in Sea Anemones

Macrander

Daly

2016

Toxins

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Sea anemones (Cnidaria, Anthozoa, and Actiniaria) use toxic peptides to incapacitate and immobilize prey and to deter potential predators. Their toxin arsenal is complex, targeting a variety of functionally important protein complexes and macromolecules involved in cellular homeostasis. Among these, actinoporins are one of the better characterized toxins; these venom proteins form a pore in cellular membranes containing sphingomyelin. We used a combined bioinformatic and phylogenetic approach to investigate how actinoporins have evolved across three superfamilies of sea anemones (Actinioidea, Metridioidea, and Actinostoloidea). Our analysis identified 90 candidate actinoporins across 20 species. We also found clusters of six actinoporin-like genes in five species of sea anemone (Nematostella vectensis, Stomphia coccinea, Epiactis japonica, Heteractis crispa, and Diadumene leucolena); these actinoporin-like sequences resembled actinoporins but have a higher sequence similarity with toxins from fungi, cone snails, and Hydra. Comparative analysis of the candidate actinoporins highlighted variable and conserved regions within actinoporins that may pertain to functional variation. Although multiple residues are involved in initiating sphingomyelin recognition and membrane binding, there is a high rate of replacement for a specific tryptophan with leucine (W112L) and other hydrophobic residues. Residues thought to be involved with oligomerization were variable, while those forming the phosphocholine (POC) binding site and the N-terminal region involved with cell membrane penetration were highly conserved.

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“…Phospholipase activity was also reported in Up1, from the crude extract of the sea anemone Urcinia piscivora [122,123]. Up1 is a potent hemolysin on erythrocytes of rat, guinea pig, dog, and humans causing numerous holes and breaks on membranes as indicated by scanning electron microscopy.…”

Section: Cytolisinsmentioning

confidence: 77%

“…Up1 is a potent hemolysin on erythrocytes of rat, guinea pig, dog, and humans causing numerous holes and breaks on membranes as indicated by scanning electron microscopy. Its hemolytic activity is not inhibited by cholesterol [122]. According to Cline [123] it produces a potent positive inotropic effect of the left atria of the heart of rat and guinea pig with little or no increase in heart rate in vivo.…”

Section: Cytolisinsmentioning

confidence: 99%

Bioactive peptides from marine sources: pharmacological properties and isolation procedures

Aneiros¹,

Garateix²

2004

Journal of Chromatography B

294

180

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Marine organisms represent a valuable source of new compounds. The biodiversity of the marine environment and the associated chemical diversity constitute a practically unlimited resource of new active substances in the field of the development of bioactive products. In this paper, the molecular diversity of different marine peptides is described as well as information about their biological properties and mechanisms of action is provided. Moreover, a short review about isolation procedures of selected bioactive marine peptides is offered. Novel peptides from sponges, ascidians, mollusks, sea anemones and seaweeds are presented in association with their pharmacological properties and obtainment methods.

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Toxic effects of the novel protein UPI from the sea anemone

Cited by 22 publications

References 24 publications

The effect of sea anemone (H. magnifica) venom on two human breast cancer lines: death by apoptosis

The effect of sea anemone (H. magnifica) venom on two human breast cancer lines: death by apoptosis

Evolution of the Cytolytic Pore-Forming Proteins (Actinoporins) in Sea Anemones

Bioactive peptides from marine sources: pharmacological properties and isolation procedures

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