Isolation of Inhibin Receptor and Siginal Transuduction In TGF-β Superfamily
| Project/Area Number |
15380195
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied animal science
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| Research Institution | Kitasato University |
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Principal Investigator |
HASEGAWA Yoshihisa Kitasato University, School of Veterinary Medicine and Animal Siences, Professor, 獣医畜産学部, 教授 (40092001)
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| Co-Investigator(Kenkyū-buntansha) |
HASHIMOTO Osamu Kitasato University, School of Veterinary Medicine and Animal Siences, Assistant Professor, 獣医畜産学部, 講師 (90317058)
星 信彦 北里大学, 獣医畜産学部, 助教授 (10209223)
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| Project Period (FY) |
2003 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥15,400,000 (Direct Cost: ¥15,400,000)
Fiscal Year 2005: ¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 2004: ¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 2003: ¥7,600,000 (Direct Cost: ¥7,600,000)
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| Keywords | Inhibin / Activin / Receptor / TGF-β Superfamily / Pituitary Cell / Signal Transduction / Smad / K562細胞 / インヒビン結合蛋白質 / K562 / リコンビナントIBP / 下垂体 / TGF-β |
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| Research Abstract |
Inhibin is a disulfide-linked, dimeric glycoprotein composed of an α subunit and β subunits. Activin is disulfide-linked dimeric protein comprised of inhibin β subunits. Although the activity of activin is modified by activin binding protein, follistatin, little is known about the physiological binding proteins of inhibin.
Using biotinylated inhibin as the probe of ligand blotting of inhibin-inhibin binding protein complexes, 43 kDa inhibin binding protein was identified in bovine follicular fluid by sequential chromatographic purification by immunoaffinity chromatography against inhibin α subunit, Sephacryl S 200 pg gel permeation chromatography, and RP-HPLC.
NH2-terminal amino acid sequencing of the protein was identical to a part of the precursor sequence of human inhibin/activin βA subunit. The binding ability of the purified protein was studied with solid phase binding assay using Eu-labeled inhibin and activin as ligands. The binding affinity of Eu labeled inhibin to 43 kDa protein was about four times stronger than that to any follistatins studied ; porcine follistatin 288, porcine follistatin 303, porcine follistatin 315, or recombinant human follistatin 288. The maximal-binding of 43 kDa protein to activin was identical to follistatin and the affinity of 43 kDa protein to activin was about a half of 288 follistatin. The effect of 43 kDa protein on FSH release in pituitary cell culture and hemoglobin biosynthesis in K562 cells was studied. 43 kDa protein showed almost the same suppression curve with pFS288 on the FSH release in rat anterior pituitary cell culture. FSH release was stimulated by the addition of activin in the culture, and the stimulated release of FSH was suppressed by 43 kDa protein dose dependently. In the study of hemoglobin biosynthesis of K562 cells, activin stimulated hemoglobin biosynthesis and 43 kDa protein showed dose dependent suppression of hemoglobin biosynthesis stimulated by activins.
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Report
(4 results)
Research Products
(43 results)
