2000 Fiscal Year Final Research Report Summary
Actin depolymerize agents isolated from marine organism
Project/Area Number |
11556057
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Research Category |
Grant-in-Aid for Scientific Research (B).
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Allocation Type | Single-year Grants |
Section | 展開研究 |
Research Field |
Basic veterinary science/Basic zootechnical science
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Research Institution | THE UNIVERSITY OF TOKYO |
Principal Investigator |
KARAKI Hideaki THE UNIVERSITY OF TOKYO, Guraduate school of Agriculture and Life Sciences, Veterinary Pharmacology, Prof., 大学院・農学生命科学研究科, 教授 (60011912)
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Co-Investigator(Kenkyū-buntansha) |
NAKAYAMA Hiroyuki THE UNIVERSITY OF TOKYO, Guraduate school of Agriculture and Life Sciences, Veterinary Pathology, Assoc. Prof, 大学院・農学生命科学研究科, 助教授 (40155891)
HORI Masatoshi THE UNIVERSITY OF TOKYO, Guraduate school of Agriculture and Life Sciences, Veterinary Pharmacology, Assist. Prof., 大学院・農学生命科学研究科, 助手 (70211547)
OZAKI Hiroshi THE UNIVERSITY OF TOKYO, Guraduate school of Agriculture and Life Sciences, Veterinary Pharmacology, Assoc. Prof., 大学院・農学生命科学研究科, 助教授 (30134505)
MATUNAGA Shigeki THE UNIVERSITY OF TOKYO, Guraduate school of Agriculture and Life Sciences, Marine Biochemistry, Assoc. Prof., 大学院・農学生命科学研究科, 助教授 (60183951)
FUSETANI Nobuhiro THE UNIVERSITY OF TOKYO, Guraduate school of Agriculture and Life Sciences, Marine Biochemistry, Prof., 大学院・農学生命科学研究科, 教授 (70012010)
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Project Period (FY) |
1999 – 2000
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Keywords | actin / depolimerization / biology / pectenotoxin 2 / mycalolide B, and / swinholide A / bisteonellide A |
Research Abstract |
Pectenotoxin-2 (PCTX-2), which is one of the causation of the Diarrhetic Shellfish Poisoning (DSP), is a family of cyclic polyether macrolide toxin isolated from scallop Patinopecten yessoensis. Although PCTX-2 has a potent cytotoxic activities against several cancer cell lines, the biochemical activity of PCTX-2 has not been determined yet. To clarify the biochemical activity of PCTX-2 is the aime in this study. PCTX-2 inhibited the contractions elicited by 72.7 mM KCl or 1 mM phenyrephrine in a concentration dependent manner in the isolated rat aorta. In A10 cells, actin stressfiber in the central portion but not in the periphery of the cell was disrupted by PCTX-2 without any visible change in the cell shape. By monitoring fluorescent intensity of pyrenyl-actin, PCTX-2 was found to inhibit the velocity and the degree of actin polymerization in a concentration dependent manner. In addition, PCTX-2 decreased viscosity of F-actin measured with the falling ball viscometry. Stoichiometric analysis indicated that PCTX-2 forms 1 : 4 complex with G-actin. These results suggest that PCTX-2 is a potent natural actin depolymerizing compound with unique mode of action. We also examined the other marine metabolites, such as mycalolide B, swinholide A and bisteonellide A, and revealed their unique biological activities. In addition, we applied these agents on actin biology.
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Research Products
(8 results)
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[Publications] H.Takahashi, R.Yoshimoto, K.Fuchibe, A.Fujishige, M.Mitsui-Saito, M.Hori, H.Ozaki, H.Yamamura, N.Awata, S.Taniguchi, M.Katsuki, T.Tsuchiya and H.Karaki: "Regulation of shortenning velocity by calponin in intact contracting smooth muscles."Biochem.Biophys.Res.Comm.. 279. 150-157 (2000)
Description
「研究成果報告書概要(欧文)」より
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