Temperature- and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines.

@article{Oda1997TemperatureAP,
  title={Temperature- and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines.},
  author={Tatsuya Oda and M Tsuru and Tomomitsu Hatakeyama and Hidetaka Nagatomo and Tsuyoshi Muramatsu and Nobuyuki Yamasaki},
  journal={Journal of biochemistry},
  year={1997},
  volume={121 3},
  pages={
          560-7
        }
}
We investigated the cytotoxicity of CEL-III, one of four Ca2+-dependent galactose/N-acetylgalactosamine (GalNAc)-binding lectins from the marine invertebrate Cucumaria echinata. Among six cell lines tested, MDCK cells showed the highest susceptibility to CEL-III cytotoxicity and its LD50 was estimated to be 53 ng/ml, while no significant cytotoxicity of CEL-III was observed in CHO cells up to 10,000 ng/ml. In the presence of 0.1 M lactose, the cytotoxicity of CEL-III was strongly inhibited. The… Expand
Antibacterial Peptides Derived from the C-Terminal Domain of the Hemolytic Lectin, CEL-III
CEL-III is a Ca2+-dependent, galactose/N-acetylgalactosamine-specific lectin (carbohydrate-binding protein) isolated from a sea cucumber, Cucumaria echinata.In addition to carbohydrate-bindingExpand
Molecular mechanism for pore-formation in lipid membranes by the hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata.
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Channel measurements showed that CEL-III has an ability to form small ion channels in the planar lipid bilayers consisting of diphytanoylphosphatidylcholine and human globoside (Gb4Cer)/LacCer, and the leakage of CF from the DPPC-lactosyl ceramide liposomes was pH-dependent, and it increased with increasing pH. Expand
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Molecular Cloning, Functional Expression, and Characterization of Isolectin Genes of Hemolytic Lectin CEL-III from the Marine Invertebrate Cucumaria echinata
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The results suggest that Tyr36 of CEL-III-L2 is important for the expression of hemolytic activity and oligomerization. Expand
Crystal Structure of the Hemolytic Lectin CEL-III Isolated from the Marine Invertebrate Cucumaria echinata
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The paucity of hydrophobic interactions in the interfaces between the domains and biochemical data suggest that these domains rearrange upon carbohydrate binding in the erythrocyte membrane may be responsible for oligomerization of CEL-III molecules and hemolysis in the cell membrane. Expand
Identification of the amino acid residues involved in the hemolytic activity of the Cucumaria echinata lectin CEL-III.
TLDR
Several amino acid residues, especially basic residues, are found to be involved in the hemolytic activity as well as the oligomerization ability of CEL-III, which is also related to that of bacterial pore-forming toxins. Expand
Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata.
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The results suggest that CEL-I induces NO production in RAW264.7 cells through the protein-cell interaction rather than the binding to the specific carbohydrate chains on the cell surface. Expand
C-type Lectin-like Carbohydrate Recognition of the Hemolytic Lectin CEL-III Containing Ricin-type β-Trefoil Folds*
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The three-dimensional structure of CEL-III/GalNAc and CEL/methyl α-galactoside complexes was solved by x-ray crystallographic analysis and the importance of amino acid residues in the carbohydrate-binding sites was confirmed by the mutational analyses. Expand
HGA-2, a novel galactoside-binding lectin from the sea cucumber Holothuria grisea binds to bacterial cells.
TLDR
A novel lectin isolated from the sea cucumber Holothuria grisea was found to be Ca(2+)-dependent; it was highly toxic against Artemia nauplii and able to recognize and agglutinate cells of Escherichia coli, and Amino acid sequences of tryptic peptides of HGA-2 strongly suggest that it is a member of the C-type lectin family. Expand
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