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The role of the ribosomal protein S19 C-terminus in Gi protein-dependent alternative activation of p38 MAP kinase via the C5a receptor in HMC-1 cells
http://hdl.handle.net/2298/20582
http://hdl.handle.net/2298/20582dc851347-1011-41dc-884f-af0971006dff
名前 / ファイル | ライセンス | アクション |
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Apoptosis_HIRO minor revised paper_r.pdf (601.2 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2011-08-01 | |||||
タイトル | ||||||
タイトル | The role of the ribosomal protein S19 C-terminus in Gi protein-dependent alternative activation of p38 MAP kinase via the C5a receptor in HMC-1 cells | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題 | C5a receptor, Gi protein, HMC-1 cells, p38MAPK, PI3K, Ribosomal protein S19 | |||||
資源タイプ | ||||||
資源タイプ | journal article | |||||
著者 |
Nishiura, Hiroshi
× Nishiura, Hiroshi× Tokita, Kazutaka× Li, Ying× Harada, Koichi× Trent, M. Woodruff× Stephen, M. Taylor× Tienabe, Kipassa Nsiama× Nishino, Norikazu× 山本, 哲郎 |
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別言語の著者 |
西浦, 弘志
× 西浦, 弘志× 斎田, 和孝× 原田, 幸一× 西野, 憲和× 山本, 哲郎 |
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内容記述 | ||||||
内容記述 | We have demonstrated that an alternative C5a receptor (C5aR) ligand, the homodimer of ribosomal protein S19 (RP S19), contains a unique C-terminus (I134–H145) that is distinct from the moieties involved in the C5a–C5aR interaction. To examine the role of I134–H145 in the ligand–C5aR interaction, we connected this peptide to the C-terminus of C5a (C5a/RP S19) and found that it endowed the second binding moiety of RP S19 (L131DR) with a relatively higher binding affinity to the C5aR on a human mast cell line, HMC-1. In contrast to the C5aR, the second C5aR C5L2 worked as a decoy receptor. As a result, the mitogen-activated protein kinase (MAPK) downstream of the Gi protein exchanged extracellular-signal regulated kinase for p38MAPK. This alternative p38MAPK activation could be pharmacologically suppressed not only by the downregulation of phosphoinositide 3-kinase (PI3K) by LY294002, but also by the over-activation of protein kinase C by phorbol 12-myristate 13-acetate. The activation was reproduced upon C5a–C5aR interaction by a simultaneous suppression of PI3K and phospholipase C with LY294002 and U73122 at low concentrations. Moreover, p38MAPK phosphorylation upstream of the pertussis toxin-dependent extracellular Ca2+ entry was also suppressed by high concentrations of MgCl2, which blocks melastatin-type transient receptor potential Ca2+ channels (TRPMs). The active conformation of C5aR upon the ligation by C5a, at least on HMC-1 cells, is changed by the additional interaction of the I134–H145 peptide, which seems to guide the alternative activation of p38MAPK. This activation is then amplified by a novel positive feedback loop between p38MAPK and TRPM. Electronic supplementary material The online version of this article (doi:10.1007/s10495-010-0511-y) contains supplementary material, which is available to authorized users. |
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書誌情報 |
Apoptosis 巻 15, 号 8, p. 966-981, 発行年 2010-08 |
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PubMed番号 | ||||||
関連タイプ | isVersionOf | |||||
関連識別子 | 20473571 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
関連識別子 | 10.1007/s10495-010-0511-y | |||||
権利 | ||||||
権利情報 | © Springer Science+Business Media | |||||
情報源(ISSN) | ||||||
関連名称 | 13608185 | |||||
フォーマット | ||||||
内容記述 | application/pdf | |||||
形態 | ||||||
601180 bytes | ||||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
日本十進分類法 | ||||||
主題 | 491 | |||||
出版者 | ||||||
出版者 | Springer Netherlands | |||||
資源タイプ | ||||||
内容記述 | 論文(Article) | |||||
資源タイプ・ローカル | ||||||
雑誌掲載論文 | ||||||
資源タイプ・NII | ||||||
Journal Article | ||||||
資源タイプ・DCMI | ||||||
text | ||||||
資源タイプ・ローカル表示コード | ||||||
01 | ||||||
URL | ||||||
内容記述 | http://www.springerlink.com/content/w47x84142mw45723/ |