Item type |
itemtype_ver1(1) |
公開日 |
2021-12-09 |
タイトル |
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タイトル |
Secretion of signal peptides via extracellular vesicles |
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言語 |
en |
著者 |
Ono, Kenji
Niwa, Mikio
Suzuki, Hiromi
Kobayashi, Nahoko Bailey
Yoshida, Tetsuhiko
Sawada, Makoto
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アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
権利 |
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言語 |
en |
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権利情報 |
Signal peptides (SPs) consist of short peptide sequences present at the N-terminal of newly synthesizing proteins and act as a zip code for the translocation of the proteins to the endoplasmic reticulum (ER). It was thought that the SPs are intracellularly degraded after translocation to the ER; however, recent studies showed cleaved SPs have diverse roles for controlling cell functions in auto- and/or intercellular manners. In addition, it still remains obscure how SP fragments translocate away from the site where they are produced. Extracellular vesicles (EV) are important for intercellular communication and can transport functional molecules to specific cells. In this study, we show that SPs are involved in EV from T-REx AspALP cells that were transfected with a human APP SP-inducible expression vector. There was no difference in the average particle size or particle concentration of EV collected from T-REx AspALP cells and T-REx Mock cells. When the SP content in the EV was examined by mass spectrometry, the C-terminal fragment of APP SP was identified in the exosomes (SEV) of T-REx AspALP cells. In our preparation of SEV fractions, no ER-specific proteins were detected; therefore, SPs may be included in SEV but not in the debris of degraded ER. This is the first indication that SPs are secreted from cells via EV. |
キーワード |
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主題Scheme |
Other |
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主題 |
Signal peptide |
キーワード |
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主題Scheme |
Other |
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主題 |
Extracellular vesicles |
キーワード |
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主題Scheme |
Other |
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主題 |
Exosomes |
キーワード |
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主題Scheme |
Other |
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主題 |
Intercellular communication |
内容記述 |
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内容記述 |
Signal peptides (SPs) consist of short peptide sequences present at the N-terminal of newly synthesizing proteins and act as a zip code for the translocation of the proteins to the endoplasmic reticulum (ER). It was thought that the SPs are intracellularly degraded after translocation to the ER; however, recent studies showed cleaved SPs have diverse roles for controlling cell functions in auto- and/or intercellular manners. In addition, it still remains obscure how SP fragments translocate away from the site where they are produced. Extracellular vesicles (EV) are important for intercellular communication and can transport functional molecules to specific cells. In this study, we show that SPs are involved in EV from T-REx AspALP cells that were transfected with a human APP SP-inducible expression vector. There was no difference in the average particle size or particle concentration of EV collected from T-REx AspALP cells and T-REx Mock cells. When the SP content in the EV was examined by mass spectrometry, the C-terminal fragment of APP SP was identified in the exosomes (SEV) of T-REx AspALP cells. In our preparation of SEV fractions, no ER-specific proteins were detected; therefore, SPs may be included in SEV but not in the debris of degraded ER. This is the first indication that SPs are secreted from cells via EV. |
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言語 |
en |
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内容記述タイプ |
Abstract |
出版者 |
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言語 |
en |
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出版者 |
Elsevier |
言語 |
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言語 |
eng |
資源タイプ |
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資源タイプresource |
http://purl.org/coar/resource_type/c_6501 |
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タイプ |
journal article |
出版タイプ |
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出版タイプ |
AM |
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出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
関連情報 |
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関連タイプ |
isVersionOf |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1016/j.bbrc.2021.04.073 |
収録物識別子 |
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収録物識別子タイプ |
PISSN |
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収録物識別子 |
0006-291X |
書誌情報 |
en : Biochemical and Biophysical Research Communications
巻 560,
p. 21-26,
発行日 2021-06-30
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ファイル公開日 |
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日付 |
2022-06-30 |
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日付タイプ |
Available |