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Amelogenin binds to both heparan sulfate and bone morphogenetic protein 2 and pharmacologically suppresses the effect of noggin
http://hdl.handle.net/10069/18356
http://hdl.handle.net/10069/18356afe24f86-99e1-4145-b809-2cc96602107b
名前 / ファイル | ライセンス | アクション |
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Bone43_371.pdf (1.0 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2008-07-02 | |||||
タイトル | ||||||
タイトル | Amelogenin binds to both heparan sulfate and bone morphogenetic protein 2 and pharmacologically suppresses the effect of noggin | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Amelogenin | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | BMP | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Heparan sulfate | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Noggin | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Osteoblast | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Saito, Kan
× Saito, Kan× Konishi, Ikuri× Nishiguchi, Miyuki× Hoshino, Tomonori× Fujiwara, Taku |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Enamel matrix derivative (EMD) is widely considered useful to promote tissue regeneration during periodontal treatment. It has been reported that the main constituent of EMD is amelogenin and that the BMP-like and TGF-β-like activity of EMD promotes osteogenesis. However, it remains unclear whether those activities are dependent on amelogenin or another growth factor contained in EMD. We performed two-dimensional SDS-PAGE analysis of EMD, as well as Western blot analyses using anti-amelogenin, anti-BMP2/4, and anti-TGF-β1 antibodies, and amino acid sequencing. Our results revealed that a large number of splicing forms of amelogenin, BMP2/4, and other unknown molecules were involved in EMD, though TGF-β1 was not. In addition, we have evaluated intracellular signaling of ERK1/2 and Smad1/5/8, binding potential and alkaline phosphatase activity and have explored the potential regulatory relationship between amelogenin and BMP. Amelogenin bound to BMP2 as well as heparin/heparan sulfate. Thus, it was suggested that BMP2/4 carried over in EMD during processing promote binding activity and phosphorylate Smad1/5/8 in osteoblasts. On the other hand, amelogenin did not phosphorylate Smad1/5/8, but rather ERK1/2. Further, high-density amelogenin reduced the inhibition of alkaline phosphatase activity by noggin, though amelogenin did not have antagonistic properties against BMP. Together with the above findings, our findings suggest that the BMP2/4 contaminated during the purification process of EMD because of the avidity of amelogenin plays an important role in signaling pathway of calcification. | |||||
書誌情報 |
Bone 巻 43, 号 2, p. 371-376, 発行日 2008-08 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 87563282 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA10506985 | |||||
PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 18515207 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1016/j.bone.2008.03.029 | |||||
権利 | ||||||
権利情報 | Copyright (c) 2008 Elsevier B.V., All rights reserved. | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Bone, 43(2), pp.371-376; 2008 |