211
Views
24
CrossRef citations to date
0
Altmetric
Research Article

Recent Studies on the Pathological Effects of Purified Sea Urchin Toxins

, , , , &
Pages 633-649 | Published online: 12 Nov 2003

References

  • Alender C. B. A biologically active substance from the spines of two diadematid sea urchins. Animal Toxins, F. E. Russll, P. R. Saunders. Pergamon Press, Oxford 1967; 145–155
  • Alender C. B., Feigen G. A., Tomita J. T. Isolation and characterization of sea urchin toxin. Toxicon 1965; 3: 9–17
  • Anraku M., Kihara H., Hashimura S. A new sea urchin toxin and its effect on spontaneous transmitter release at frog neuromuscular junctions. Jpn. J. Physiol. 1984; 34: 839–847
  • Barondes S. H. Soluble lectins. A new class of extracellular proteins. Science 1984; 223: 1259–1264
  • Barondes S. H., Cooper D. N.W., Gitt M. A. Galectins. Structure and function of a large family of animals lectins. J. Biol. Chem. 1994; 269: 20807–20810
  • Belogortseva N. I., Molchanova V. I., Kurika A. V., Skobun A. S., Glazkova V. E. Isolation and characterization of new GalNAc/Gal‐specific lectin from the sea mussel Crenomytilus grayanus. Comp. Biochem. Physiol. 1998; 119C: 45–50
  • De Waard A., Hickmans S., Kornfeld S. Isolation and properties of β‐galactoside binding lectins of calf heart and lung. J. Biol. Chem. 1976; 251: 7581–7587
  • Drickamer K. Two distinct classes of carbohydrate‐recognition domains in animal lectins. J. Biol. Chem. 1988; 263: 9557–9560
  • Feigen G. A., Sanz E., Alender C. B. Studies on the mode of action of sea urchin toxin‐I. Conditions affecting release of histamine and other agents from isolated tissues. Toxicon 1966; 4: 161–175
  • Feigen G. A., Hadji L., Cushing J. E. Mode of action and identities of protein constituents in sea uurchin toxin. Bioactive Compounds from the Sea, H. J. Humm, C. E. Lane. Marcel Dekker, New York 1974; 38–97
  • Fleming W. J., Howden M. E.H. Partial purification and characterization of a lethal protein from Tripneustes gratilla. Toxicon 1974; 12: 447–448
  • Fujiwara T. On the poisonous pedicellariae of Toxopneustes pileolus (Lamark). Annot. Zool. Jpn. 1935; 15: 62–69
  • Giga Y., Ikai A., Takahashi K. The complete amino acid seqence of a lectin from the coelomic fluid of the sea urchin Anthrocidaris crassispina: homologies with mammalian and insect lectins. J. Biol. Chem. 1987; 262: 6197–6203
  • Hatakeyama T., Nagatomo H., Yamasaki N. Interaction of the hemolytic lectin CEL‐III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane. J. Biol. Chem. 1995; 270: 3560–3564
  • Hirabayashi J., Satoh M., Kasai K. Evidence that Caenorhabditis elegans 32‐kDa β‐galactoside‐binding protein is homologous to vertebrates β‐galactoside‐binding lectins. J. Biol. Chem. 1992; 267: 15485–15490
  • Hosono M., Ishikawa K., Mineki R., Murayama K., Numata C., Ogawa Y., Takayanagi Y., Nitta K. Tandem repeat structure of rhamnose‐binding lectin from catfish (Silurus asotus) eggs. Biochim. Biophys. Acta 1999; 1472: 668–675
  • Kasai K., Hirabayashi J. A family of animal lectins that decipher glycocodes. J. Biochem. 1996; 119: 1–6
  • Kawagishi H., Yamawaki H., Isobe S., Usui T., Kimura A., Chiba S. Two lectins from the marine sponge Halichondria okadai. J. Biol. Chem. 1994; 269: 1375–1379
  • Kimura A., Nakagawa H. Action of an extract from the sea urchin Toxopneustes pileolus on isolated smooth muscle. Toxicon 1980; 18: 689–693
  • Kimura A., Hayashi H., Kuramoto M. Studies of urchi‐toxins: separation, purification and pharmacological actions of toxinic substances. Jpn. J. Pharmacol. 1975; 25: 109–120
  • Kuwabara S. Purification and properties of peditoxin and the structure of its prosthetic group, pedoxin, from the sea urchin Toxopneustes pileolus (Lamarck). J. Biol. Chem. 1994; 269: 26734–26738
  • Mebs D. A toxin from the sea urchin Tripneustes gratilla. Toxicon 1984; 22: 306–307
  • Mikheyskaya L. V., Evtushenko E. V., Ovoova R. G., Belogortserva N. I., Ovodov Y. S. Isolation and characterization of a new β‐galactose‐specific lectin from the sea worm Chaetopterus varieopedatus. Carbohydr. Res. 1995; 275: 193–200
  • Muramoto K., Kamiya H. The amino acid sequence of a lectin from the acron barnacle Megabalanus rose. Biochim. Biophys. Acta 1986; 874: 285–295
  • Nakagawa H., Kimura A., Takei M., Endo K. Histamine release from rat mast cells induced by an extract from the sea urchin Toxopneustes pileolus. Toxicon 1982; 20: 1095–1097
  • Nakagawa H., Tu A. T., Kimura A. Purification and characterization of Contractin A from the pedicellarial venom of sea urchin, Toxopneustes pileolus. Arch. Biochem. Biophys. 1991; 284: 279–284
  • Nakagawa H., Yanagihara N., Izumi F., Wad A., Kimura A. Inhibition of nicotinic acethlcholine receptors‐mediated secretion and synthesis of catecholamines by sea urchin toxin in cultured bovine adrenal medullary cells. Biochem. Pharamacol. 1992; 44: 1779–1785
  • Nakagawa H., Tomihara Y., Araki Y., Hayashi H. Preliminary studies on venom proteins in the pedicellariae of the toxopneustid sea urchins, Toxopneustes pileolus and Tripneustes gratilla. J. Nat. Toxins 1994; 3: 25–34
  • Nakagawa H., Hashimoto T., Hayashi H., Shinohara M., Ohura K., Tachikawa E., Kashimoto T. Isolation of a novel lectin from the globiferous pedicellariae of the sea urchin Toxopneustes pileolus. Adv. Exp. Med. Biol. 1996; 391: 213–223
  • Nakagawa H., Yamaguchi C., Hayashi H. Biologically active substances from sea urchins. J. Nat. Toxins 1997; 6: 193–202
  • Nakagawa H., Yamaguchi C., Sakai H., Hayashi H., Kanemaru K., Hayashi H. Biological and physiological proterties of pedicellarial lectins from the toxopneustid sea urchins. J. Nat. Toxins 1999a; 8: 297–308
  • Nakagawa H., Yamaguchi C., Tomiyoshi F., Hayashi H. A novel mitogenic lectin from the globiferous pedicellariae of sea urchin, Toxopneustes pileolus. J. Chem. Soc. Pak. 1999b; 21: 305–310
  • Okada K., Hashimoto T., Miyauchi Y. A preliminary report on the poisonous effect of Toxopneustes toxin upon the heart of oyster. Bull. Mar. Biol. Asamushi 1955; 7: 133–140
  • Ozeki Y., Matsui T., Suzuki M., Titani K. Amino acid sequence and molecular characterization of a D‐galactose‐specific lectin purified from sea urchin (Anthrocidaris crassispina) eggs. Biochemistry 1991; 30: 2391–2394
  • Ozeki Y., Tazawa E., Matsui T. D‐galactoside‐specific lectins from the body wall of an echiuroid (Urechis unicincus) and two annelids (Neanthes japonica and Marphysa sanguinea). Comp. Biochem. Physiol. 1997; 118B: 1–6
  • Perillo N. L., Pace K. E., Seilhamer J. J., Baum L. G. Apoptosis of T cells mediated by galectin‐1. Nature 1995; 378: 736–739
  • Pfeifer K., Haasemann M., Gamulin V., Bretting H., Fahrenholz F., Muller W. E.G. S‐type lectins occur also in vertebrates: high conservation of carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium. Glycobiology 1993; 3: 179–184
  • Sanford G. L., Harris‐Hooker S. Stimulation of vascular cell proliferation by β‐galactoside specific lectins. FASEB J. 1990; 4: 2912–2918
  • Satoh F., Nakagawa H., Yamada H., Nagasaka K., Nagasaka T., Araki Y., Tomihara Y., Nozaki M., Sakuraba H., Ohshima T., Hatakeyama T., Aoyagi H. Fishing for bioactive substances from scorpionfish and some sea urchins. J. Nat. Toxins 2002; 11: 297–304
  • Suzuki T., Takagi T., Furukohori T., Kawamura K., Nakauchi M. A calcium‐dependent galactose‐binding lectin from the tunicate Polyandrocarpa misakiensis. J. Biol. Chem. 1990; 265: 1274–1281
  • Suzuki‐Nishimura T., Nakagawa H., Uchida M. K. D‐galactose‐specific sea urchin lectin sugar‐specifically inhibited histamine release induced by Datura stramonium agglutinin: differences between sugar‐specific effects of sea urchin lectin and those of D‐galactose‐ or L‐fucose‐specific palnt lectins. Jpn. J. Pharmacol. 2001; 85: 443–452
  • Takasaki C., Yutani F., Kajiyashiki T. Amino acid sequences of eight phospholipase A2 from the venom of australian king brown snake, Pseudechis australis. Toxicon 1990; 28: 329–339
  • Takei M., Nakagawa H., Eno K. Mast cell activation by pedicellarial toxin of sea urchin, Toxopneustes pileolus. FEBS Lett. 1993; 328: 59–62
  • Tanigawa T., Elwood N., Metcalf D., Cary D., Deluca E., Nicola N. A., Begley C. G. The SCL gene product is regulated by and differentially regulates cytokine responses during myeloid leukemia cell differentiation. Proc. Natl. Acad. Sci. U. S. A. 1993; 90: 7864–7868
  • Tanigawa T., Nicola N. A., McArthur G. A., Strasser A., Begley C. G. Differential regulation of macrophage differentiation in response to leukemia inhibitory factor/oncostatin‐M/interleukin‐6: the effect of enforced expression of the SCL transcription factor. Blood 1995; 85: 379–390
  • Tateno H., Saneyoshi A., Ogawa T., Muramoto K., Kamiya H., Saneyoshi M. Isolation and characterization of rhamnose‐binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily. J. Biol. Chem. 1999; 273: 19190–19197
  • Yamaoka A., Kuwabara I., Frigeri L. C., Liu F.‐T. A human lectin, galectin‐3 (ϵbp/Mac‐2), stimulates superoxide production by neutrophils. J. Immunol. 1995; 154: 3479–3487
  • Yokosawa H., Harada K., Igarashi K., Abe Y., Takahashi K., Ishii S. Galactose‐specific lectin in the hemolymph of solitary ascidian, Halocynthia Roretzi. Molecular, binding and functional properties. Biochim. Biophys. Acta 1986; 870: 242–247
  • Zhang Y. A., Abe J., Siddiq A., Nakagawa H., Honda S., Wada T., Ichida S. UT841 purified from sea urchin (Toxopneustes pilelolus) venom inhibits time‐dependent 45Ca2 + uptake in crude synaptosome fraction from chick brain. Toxicon 2001; 39: 1223–1229

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.