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Klyshko, E. V.; Ильина, А. П.; Monastyrnaya, Margarita; Burtseva, Yu. V.; Костина, Е. Э.; Зыкова, Т. А.; Menzorova, N. I.; Kozlovskaya, É. P.

doi:10.1023/a:1024668732346

Cited by 5 publications

(7 citation statements)

References 21 publications

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“…Similarly to previous research of extracts of sea anemones inhabiting the southern part of the Sea of Okhotsk, near Sakhalin Island [13], the aqueous extracts of animals studied in this work and ethanol extracts of Commander L. brevicorne and Kuril C. cf. pilatus demonstrated hemolytic activity (Table 2).…”

Section: Discussionmentioning

confidence: 89%

“…This makes it possible to consider unexplored and little-studied species to be sources of new biologically active protein compounds, many of which undoubtedly have pharmacological potential. Sea anemone venoms are a complex mixture of peptide and protein components, such as actinoporins [5][6][7][8][9], phospholipases A2 [10,11], neurotoxins [12], and enzymes and their inhibitors [13,14].…”

Section: Introductionmentioning

confidence: 99%

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Deep-Sea Anemones Are Prospective Source of New Antimicrobial and Cytotoxic Compounds

et al. 2021

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The peculiarities of the survival and adaptation of deep-sea organisms raise interest in the study of their metabolites as promising drugs. In this work, the hemolytic, cytotoxic, antimicrobial, and enzyme-inhibitory activities of tentacle extracts from five species of sea anemones (Cnidaria, orders Actiniaria and Corallimorpharia) collected near the Kuril and Commander Islands of the Far East of Russia were evaluated for the first time. The extracts of Liponema brevicorne and Actinostola callosa demonstrated maximal hemolytic activity, while high cytotoxic activity against murine splenocytes and Ehrlich carcinoma cells was found in the extract of Actinostola faeculenta. The extracts of Corallimorphus cf. pilatus demonstrated the greatest activity against Ehrlich carcinoma cells but were not toxic to mouse spleen cells. Sea anemones C. cf. pilatus and Stomphia coccinea are promising sources of antimicrobial and antifungal compounds, being active against Gram-positive bacteria Bacillus subtilis, Staphylococcus aureus, and yeast Candida albicans. Moreover, all sea anemones contain α-galactosidase inhibitors. Peptide mass fingerprinting of L. brevicorne and C. cf. pilatus extracts provided a wide range of peptides, predominantly with molecular masses of 4000–5900 Da, which may belong to a known or new structural class of toxins. The obtained data allow concluding that deep-sea anemones are a promising source of compounds for drug discovery.

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Section: Discussionmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Deep-Sea Anemones Are Prospective Source of New Antimicrobial and Cytotoxic Compounds

et al. 2021

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“…orientalis had demonstrated this activity [22]. The polypeptides with the Ä 2 phospholipase activity are separated from the group 2 cytolysins at the stage of ion-exchange chromatography ( Fig.…”

Section: Resultsmentioning

confidence: 94%

“…This species is widely distributed in the Possjet Bay of the Sea of Japan, and its aqueous extracts demonstrated significant hemolytic and Ä 2 phospholipase activities, whereas alcoholic extracts, toxic and trypsin-inhibiting activities [22].…”

Section: Resultsmentioning

confidence: 99%

Actinoporins from the Sea of Japan anemone Oulactis orientalis: Isolation and partial characterization

et al. 2005

Russ J Bioorg Chem

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2 Abbreviations: BLM, bilayer lipid membrane.tion is the absence of tryptophan and the presence of six Cys residues.The second group of cytolysins, which is the most thoroughly studied, are the highly basic polypeptides (  I 9 and higher) with the molecular masses of ca. 20 kDa. They are isolated from various species of the Actiniidae and Stichodactylidae families, which mainly inhabit tropical regions of the ocean [1][2][3][4][5]14]. They were shown to exhibit a powerful lytic action on the sphingomyelin-containing membranes of eukaryotes by forming in them cation-selective ion channels (pores), due to which they were named actinoporins [1,15,16]. The absence of cysteine is characteristic of their amino acid composition. The amino acid sequences of eight actinoporins have been elucidated up to date. A steadily increasing interest of researchers to studying the structure and function of recombinant forms of actinoporins prepared by the methods of genetic engineering is now noteworthy [3].The third group of cytolysins comprises the lethal cytolytic phospholipases Ä 2 from Stichodactyla helianthus [17] and Aiptasia pallida [18] with M 30-40 kDa and similar in physicochemical properties cytolysins devoid any enzymatic activity [3].The only representative of the fourth group of cytolysins is metridiolysin, isolated from the sea anemone Abstract -Two cytolytic toxins (cytolysins Or-A and Or-G) were isolated from the Sea of Japan anemone Oulactis orientalis and characterized. Their purification scheme involved a hydrophobic chromatography on Polychrom-1, a gel filtration on Akrilex P-4, a cation-exchange chromatography on CM-32 cellulose, and a reverse-phase HPLC on a Nucleosil C 18 column. The molecular masses of Or-A and Or-G were determined by SDS-PAGE in 14% PAG to be ca. 18 kDa. The absence of Cys residues and a high content of basic amino acid residues are characteristic of their amino acid compositions. The hemolytic activities of Or-A and Or-G were found to be 295.86 and 322.58 HU/mg, respectively; these are by three orders of magnitude lower than those of sphingomyelin-inhibitable cytolysins from the tropic sea anemones. The amino acid sequences of the N -terminal fragments of Or-A and Or-G were determined to be ATFRVLAK and GAIIAGAA, respectively. Action of the cytolysins on the erythrocyte membrane is inhibited by exogenous sphingomyelin. They form ion channels in bilayer lipid membranes with the conductivity of 16, 32, and 40 pSm in 0.1 M NaCl and 168, 240, and 320 pSm in 1 M NaCl at pH 7.2. Therefore, they were attributed to the group of actinoporins.

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“…We have previously found that the hemolytic activity of water extracts of several sea anemone species occurring in the Sea of Okhotsk and the Sea of Japan was two-three order of magnitude lower than those of the tropic species [16]. This fact prompted us to isolate actinoporins from the Sea of Japan O. orientalis sea anemone (the family Actiniidae) and to study its physicochemical properties and structure.…”

Section: Introductionmentioning

confidence: 99%

Primary Structures of Actinoporins from Sea Anemone Oulactis orientalis

et al. 2005

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Partial amino acid sequences of the actinoporins Or-A (136 aa) and Or-G (144 aa) isolated from the Sea of Japan sea anemone O ulactis orientalis were determined by sequencing the clones obtained by the amplification of genomic DNA and cDNA with primers specific to the N -terminal regions of the O. orientalis actinoporin sequences and to the ë -terminal region, which is highly conservative in all the known actinoporin sequences. The complete structures of Or-A (165 aa) and Or-G (173 aa) were elucidated by sequencing the cDNA clones obtained by the rapid amplification of 3'-ends of cDNA. A comparative analysis of the amino acid sequences of the O ulactis actinoporins with those of actinoporins from tropical species revealed considerable differences in the structures of their N -terminal fragments and their membrane-binding sites. We believe that these differences could explain the lower hemolytic activities of Or-A and Or-G compared to those of actinoporins from the tropical species.

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Cited by 5 publications

References 21 publications

Deep-Sea Anemones Are Prospective Source of New Antimicrobial and Cytotoxic Compounds

Deep-Sea Anemones Are Prospective Source of New Antimicrobial and Cytotoxic Compounds

Actinoporins from the Sea of Japan anemone Oulactis orientalis: Isolation and partial characterization

Primary Structures of Actinoporins from Sea Anemone Oulactis orientalis

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