| Project/Area Number |
06454159
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General pharmacology
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| Research Institution | Mie University |
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Principal Investigator |
TANAKA Toshio Mie University School of Medicine, Department of Molecular and Cellular Pharmacology Professor and Chairman, 医学部, 教授 (00135443)
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| Co-Investigator(Kenkyū-buntansha) |
MUKAI Jun Mie University School of Medicine, Department of Molecular and Cellular Pharmaco, 医学部, 助手 (70263019)
NAKA Michiko Mie University School of Medicine, Department of Molecular and Cellular Pharmaco, 医学部, 助手 (10093139)
松島 聡 三重大学, 医学部, 助手 (50252367)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥6,400,000 (Direct Cost: ¥6,400,000)
Fiscal Year 1995: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1994: ¥5,400,000 (Direct Cost: ¥5,400,000)
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| Keywords | Leucocyte / Eosinophil / Chemotaxis / S100 protein / S100L / PAF / Ca^<2+>-binding protein / Signal transduction |
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| Research Abstract |
It is currently thought that leucocytes play a proinflammatory role in allergic disease or parasitic disease. In addition, it was known that marked leucocytes infiltration occurred in the some kinds of malignant tumor occasionally. Several proteins and biolipids are being considered as important mediators in regulating leucocytes function. Recently, we found that extracts of salting out fraction of bovine lung from ion-exchange chromatography had eosinophil chemotactic activity. The extracts were further purified by sequential purification on hydrophobic chromato graphy and ion-exchange chromatography, so we had 11kDa protein revealed on SDS-polyacry lamide gel electrophoresis. Its partial protein sequence analysis indicated that it was identical with S100L,one of Ca2+-binding S100 protein family. Then, we examined and proved existence of S100L protein in extracellular fluid with cultured LLC-PK1 cells. S100L did not induce chemotaxis of guinea pig neutrophils and monocytes. In this study, we demonstrate that S100L is a novel selective chemotactic factor for eosinophils, and has a most potent chemotactic activity on guinea pig eosinophils of all the chemotactic proteins. The chemotactic activity of S100L on guinea pig eosinophils is observed at 0.1nM of protein concentration, and the effects appear mediated by a novel specific surface receptor. We characterized the receptor for S100L on guinea pig eosinophils. Scatchard analyzes of the data that [125I] S100L bound to S100L recreptor indicate the presence of two receptor populations on eosinophils with Kd value of 3.3x 10-11M and 1.1x 10-9M.Thus, S100L protein has a most potent chemotactic activity on guinea pig eosinophils of all the chemotactic proteins.
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