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en: Analysis of cereal extracts as conditioning solutes to suppress the initial attachment of Escherichia coli to abiotic surfaces

en: European Food Research and Technology

ja: European Food Research and Technology


en: Carbohydrate recognition by the rhamnose-binding lectin SUL-I with a novel three-domain structure isolated from the venom of globiferous pedicellariae of the flower sea urchin Toxopneustes pileolus

en: The globiferous pedicellariae of the venomous sea urchin Toxopneustes pileolus contains several biologically active proteins. We have cloned the cDNA of one of the toxin components, SUL-I, which is a rhamnose-binding lectin (RBL) that acts as a mitogen through binding to carbohydrate chains on target cells. Recombinant SUL-I (rSUL-I) was produced in Escherichia coli cells, and its carbohydrate-binding specificity was examined with the glycoconjugate microarray analysis, which suggested that potential target carbohydrate structures are galactose-terminated N-glycans. rSUL-I exhibited mitogenic activity for murine splenocyte cells and toxicity against Vero cells. The three-dimensional structure of the rSUL-I/l-rhamnose complex was determined by X-ray crystallographic analysis at a 1.8 Å resolution. The overall structure of rSUL-I is composed of three distinctive domains with a folding structure similar to those of CSL3, a RBL from chum salmon (Oncorhynchus keta) eggs. The bound l-rhamnose molecules are mainly recognized by rSUL-I through hydrogen bonds between its 2-, 3-, and 4-hydroxy groups and Asp, Asn, and Glu residues in the binding sites, while Tyr and Ser residues participate in the recognition mechanism. It was also inferred that SUL-I may form a dimer in solution based on the molecular size estimated via dynamic light scattering as well as possible contact regions in its crystal structure.

en: Protein Science

ja: Protein Science


en: Isolation of a novel lectin from the dorsal spines of the devil stinger, Inimicus japonicus

en: International Aquatic Research

ja: International Aquatic Research


en: Isolation and partial characterization of a L-rhamnose-binding lectin from the globiferous pedicellariae of the toxopneustid sea urchin, Toxopneustes pileolus


en: Immunomodulatory activity of a pedicellarial venom lectin from the toxopneustid sea urchin, Toxopneustes pileolus

en: Toxin Reviews

ja: Toxin Reviews


en: A novel cytotoxic protein, Karatoxin, from the dorsal spines of the the redfin velvetfihi, Hypodytes rubripinnis


en: Possible use of quercetin, an antioxidant, for protection of cells suffering from overload of intracellular Ca2+: A model experiment

en: Quercetin is known to protect the cells suffering from oxidative stress. However, the oxidative stress elevates intracellular Ca2+ concentration, one of phenomena responsible for cell death. Therefore, we hypothesized that quercetin would protect the cells suffering from overload of intracellular Ca2+. To test the hypothesis, the effects of quercetin on the cells suffering from oxidative stress and intracellular Ca2+ overload were examined by using a flow cytometer with appropriate fluorescence probes (propidium iodide, fluo-3-AM, and annexin V-FITC) and rat thymocytes. The concentrations (1-30 µM) of quercetin to protect the cells suffering from intracellular Ca2+ overload by A23187, a calcium ionophore, were similar to those to do so the cells from oxidative stress by H2O2. The cell death respectively induced by H2O2 and A23187 was significantly suppressed by removal of external Ca2+. Furthermore, quercetin greatly delayed the process of Ca2+-dependent cell death although it did not significantly affect the elevation of intracellular Ca2+ concentration by H2O2 and A23187, respectively. It is concluded that quercetin can protect the cells from oxidative injury in spite of increased concentration of intracellular Ca2+. Results suggest that quercetin is also used for protection of cells suffering from overload of intracellular Ca2+.

en: Life Sciences

ja: Life Sciences


en: Biological activities of multiple lectins from the toxopneustid sea urchins

en: ラッパウニ科のラッパウニおよびシラヒゲウニの毒棘のタンパク画分をゲル濾過，アフィニティークロマトグラフィーおよびHPLCにより精製し，レクチンを単離し，それらの生物活性を比較検討した．ラッパウニから精製された32 kDa のSUL-I は多様な生物活性を示したが，SUL-II はほとんど細胞増殖活性などの生理活性を示さなかった．一方，シラヒゲウニから精製された23 kDa のヘパリン結合性のレクチン，TGL-I も細胞増殖活性は示さなかった．SUL-I とSUL-II は部分アミノ酸配列において殆ど相同性は認められなかった．

en: Recent Advances in Marine Science and Technology 2002


en: Cytokinesis arrest and nuclear fission in low density populations of Trichomonad Protozoan

en: Cell growth of anaerobic protozoan Tritrichomonas foetus was analyzed. This protozoan usually proliferates in extremely high density, but protozoan parasites were dispersed uniformly in F-bouillon medium and cell division stopped temporarily. However, nuclear fission continued and giant polynucleated cells formed. Later, cell division resumed and cells returned to normal form. In conditioned medium, cytokinesis of the dispersed parasites did not stop. Results indicated that T. foetus cells secreted an extracellular factor that influenced cytokinesis.

en: Zoological Science

ja: Zoological Science


en: Cytotoxic effects of methanol, formaldehyde, and formate on dissociate rat thymocytes: a possibility of aspartame toxicity

en: Cell Biology and Toxicology

ja: Cell Biology and Toxicology


en: Tri-n-butyltin-induced decrease in cellular level of glutathione in rat thymocytes: a flow cytometric study using 5-chloromethylfluorescein diacetate

en: Toxicology Letters

ja: Toxicology Letters


en: Biochemical and physiological properties of pedicellarial lectins from the toxopneustid sea urchins

en: Pedicellarial lectins (SUL-I, SUL-II, and TGL-I) were purified from the toxopneustid sea urchins, Toxopneustes pileolus and Tripneustes gratilla using gel filtration chromatography, affinity chromatography, and reverse-phase HPLC. SUL-I (Nakagawa et al., 1996) and SUL-II from the large globiferous pedicellariae of T. pileolus are D-galactose-binding lectins with molecular masses of 32 kDa and 23 kDa, respectively; while TGL-I from the globiferous pedicellariae of T. gratilla is a Ca(2+)-independent heparin-binding lectin with a molecular mass of 23 kDa. SUL-I induced mitogenic stimulation on murine splenocytes but TGL-I did not. At higher dose ranges SUL-I exhibited inhibitory effects on the cells. The dual response to SUL-I was effectively inhibited by D-galactose. SUL-I enhanced norepinephrine-induced contraction of isolated rat mesenteric artery with endothelium. When endothelium was removed from the artery, acetylcholine did not relax the norepinephrine-induced contraction. In the same artery the enhancing effect of the contraction by SUL-I was abolished, suggesting that SUL-I acts on the endothelium of mesenteric artery, and may release prostanoids. The present results suggest an extracellular function for SUL-I that may have wide-ranging effects in physiological processes. The primary role of pedicellarial lectins from T. pileolus and T. gratilla might be defense against a foreign body.

ja: ラッパウニの大型叉棘からゲル濾過，アフィニティークロマトグラフィー及びHPLCを用いて，D-ガラクトース特異的レクチン (SUL-I とSUL-II)ならびにシラヒゲウニの叉棘からヘパリン結合性レクチン(TGL-I)をそれぞれ単離した．SUL-I は強いマイトジェン活性を示し，ラットの血管内皮細胞に対してプロスタノイドの遊離を示唆した．TGL-I はマイトジェン活性を示さなかった．

en: Journal of Natural Toxins

ja: Journal of Natural Toxins