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  1. 医学
  2. 発表論文(医学系)

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/2298/20582
dc851347-1011-41dc-884f-af0971006dff
名前 / ファイル ライセンス アクション
Apoptosis_HIRO Apoptosis_HIRO minor revised paper_r.pdf (601.2 kB)
Item type 学術雑誌論文 / Journal Article(1)
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
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
著者 Nishiura, Hiroshi

× Nishiura, Hiroshi

WEKO 104566

Nishiura, Hiroshi

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Tokita, Kazutaka

× Tokita, Kazutaka

WEKO 104567

Tokita, Kazutaka

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Li, Ying

× Li, Ying

WEKO 104568

Li, Ying

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Harada, Koichi

× Harada, Koichi

WEKO 104569

Harada, Koichi

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Trent, M. Woodruff

× Trent, M. Woodruff

WEKO 104570

Trent, M. Woodruff

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Stephen, M. Taylor

× Stephen, M. Taylor

WEKO 104571

Stephen, M. Taylor

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Tienabe, Kipassa Nsiama

× Tienabe, Kipassa Nsiama

WEKO 104572

Tienabe, Kipassa Nsiama

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Nishino, Norikazu

× Nishino, Norikazu

WEKO 104573

Nishino, Norikazu

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山本, 哲郎

× 山本, 哲郎

WEKO 94588

ja 山本, 哲郎
ISNI

ja-Kana ヤマモト, テツロウ

en Yamamoto, Tetsuro

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別言語の著者 西浦, 弘志

× 西浦, 弘志

WEKO 104580

西浦, 弘志

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斎田, 和孝

× 斎田, 和孝

WEKO 104581

斎田, 和孝

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原田, 幸一

× 原田, 幸一

WEKO 104582

原田, 幸一

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西野, 憲和

× 西野, 憲和

WEKO 104583

西野, 憲和

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山本, 哲郎

× 山本, 哲郎

WEKO 104584

山本, 哲郎

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内容記述
内容記述タイプ Other
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.
書誌情報 Apoptosis

巻 15, 号 8, p. 966-981, 発行年 2010-08
PubMed番号
関連タイプ isVersionOf
識別子タイプ PMID
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
内容記述タイプ Other
内容記述 application/pdf
形態
値 601180 bytes
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
日本十進分類法
主題Scheme NDC
主題 491
出版者
出版者 Springer Netherlands
資源タイプ
内容記述タイプ Other
内容記述 論文(Article)
資源タイプ・ローカル
値 雑誌掲載論文
資源タイプ・NII
値 Journal Article
資源タイプ・DCMI
値 text
資源タイプ・ローカル表示コード
値 01
URL
内容記述タイプ Other
内容記述 http://www.springerlink.com/content/w47x84142mw45723/
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