| Project/Area Number |
03670107
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General pharmacology
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| Research Institution | Department of Pharmacology 2, Nagasaki University School of Medicine |
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Principal Investigator |
NIWA Masami Nagasaki University School of Medicine, Department of Pharamcology 2 Associate Professor, 医学部, 助教授 (20136641)
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| Co-Investigator(Kenkyū-buntansha) |
SHIGEMATSU Kazuto Nagasaki University School of Medicine, Department of Pathology 2 Assistant Prof, 医学部, 講師 (20154205)
KATAOKA Yasufumi Nagasaki University School of Medicine, Department of Pharmacology 2 Assistant P, 医学部, 講師 (70136513)
TANIYAMA Kohtaro Nagasaki University School of Medicine, Department of Pharmacology 2 Professor, 医学部, 教授 (70030898)
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| Project Period (FY) |
1991 – 1992
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| Project Status |
Completed (Fiscal Year 1992)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1992: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1991: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | endothelin receptors / receptor autoradiography / chemical cross-linking / rat brain / porcine spinal cord / human spinal cord / 定量的受容体オ-トラジオグラフ法 / 受容体活性部位 / エンドセリン |
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| Research Abstract |
Specific binding sites for ^<125>I-endothelin-1 (^<125>I-ET-1) in the spinal cord were investigated using quantitative receptor autoradiographic and chemical cross-linking methods. The binding sites were highly concentrated in porcine and human spinal cord areas corresponding anatomically to the dorsal horn (Rexed's laminae I-III), an area around the central canal (lamina X) and the principal part of the intermediolateral nucleus (IMLp). The localization of the binding sites differed from those of ^<125>I-omega-conotoxin GVIA (^<125>I-CgTx) and ^<125>I-Bolton-Hunter substance P (^<125>I-BH-SP), with the exception that the IMLp shared ^<125>I-ET-1 with ^<125>I-CgTx and ^<125>I-BH-SP binding sites. Specific ^<125>I-ET-1 binding sites in the areas examined were characteristically single and of high affinity. There were no differences between the potencies of unlabeled ET family peptides, ET-1, ET-2, ET-3 and sarafotoxin S6b at inhibiting ^<125>I-ET-1 binding to the areas. Chemical cross-linking studies showed that ^<125>I-ET-1 AND ^<125>I-ET-3 mainly bound to a protein with molecular mass of 43 kDa in the porcine and human thoracic spinal cord membranes. The present finding shows the neuronal significance of this newly discovered peptide in the spinal cord.
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