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Restriction mechanism of bone morphogenetic protein in the early development of Xenopus Laevis
https://ir.soken.ac.jp/records/1362
https://ir.soken.ac.jp/records/13625e8aae79-1267-4866-acf1-6977908b8168
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
要旨・審査要旨 / Abstract, Screening Result (192.9 kB)
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| Item type | 学位論文 / Thesis or Dissertation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2010-02-22 | |||||
| タイトル | ||||||
| タイトル | Restriction mechanism of bone morphogenetic protein in the early development of Xenopus Laevis | |||||
| タイトル | ||||||
| タイトル | Restriction mechanism of bone morphogenetic protein in the early development of Xenopus Laevis | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_46ec | |||||
| 資源タイプ | thesis | |||||
| 著者名 |
大河原, 美静
× 大河原, 美静 |
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| フリガナ |
オオカワラ, ビセイ
× オオカワラ, ビセイ |
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| 著者 |
OHKAWARA, Bisei
× OHKAWARA, Bisei |
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| 学位授与機関 | ||||||
| 学位授与機関名 | 総合研究大学院大学 | |||||
| 学位名 | ||||||
| 学位名 | 博士（理学） | |||||
| 学位記番号 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 総研大甲第610号 | |||||
| 研究科 | ||||||
| 値 | 生命科学研究科 | |||||
| 専攻 | ||||||
| 値 | X2 分子生物機構論専攻 | |||||
| 学位授与年月日 | ||||||
| 学位授与年月日 | 2002-03-22 | |||||
| 学位授与年度 | ||||||
| 値 | 2001 | |||||
| 要旨 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | During early development, cells receive positional information from neighboring cells that direct how they should differentiate to form tissue patterns from initially uniform germ layers.Ligands of the transforming growth factor (TGF-β) superfamily are known to participate in this pattern formation. In particular, activin has been shown to act as a long-range signal to establish a concentration gradient in X enopus ectoderm.In contrast, the action of BMP-2 and BMP-4, both of which also belong to this superfamily, appears to be restricted to the ventral ectoderm where they induce the epidermal fate in a tightly localized manner.This raises a question as to how the action of BMP is tightly restricted to within and around the cells that produce it.<br />To investigate this question, I noticed that some of the BMP subfamily ligands contain a unique core of basic amino acids in their N-terminus.Then cDNA encoding BMP-4 variants, lacking basic amino acids core in their N-terminal region, were constructed.To analyze their action ranges in Xenopus embryo, the experiments using presumptive ectoderm and whole embryo were preformed.Results are, first, that a basic core of only three amino acids in the N-terminal region of BMP-4 is required not for its biological activity but for its restriction to the non-neural ectoderm and to the ventral tissue. Second, I demonstrated that heparan sulfate proteoglycans (HSPGs) bind to this basic core and WTBMP-4 could act as long-range siganl molecules where HSPGs are absent in vivo.<br />These observations suggest that the basic amino acids in the N-terminal region of BMP-4 and particularly the basic core play an essential role in conferring to BMP-4 a short-range action in vivo.And I demonstrated that at least one of the molecules trapping WTBMP-4 on the surface of animal cap cells is HSPGs in vivo.The present work first identifies the critical domain of BMP for the restriction of its diffusion through the interaction with extracellular environments in vivo． | |||||
| 所蔵 | ||||||
| 値 | 有 | |||||
