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Erlin-2 is associat...
Erlin-2 is associated with active γ-secretase in brain and affects amyloid β-peptide production
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Teranishi, Yasuhiro (author)
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Hur, Ji-Yeun (author)
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- Gu, Gucci Jijuan (author)
- Uppsala universitet,Molekylära verktyg,Science for Life Laboratory, SciLifeLab
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Kihara, Takahiro (author)
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Ishikawa, Taizo (author)
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Nishimura, Takeshi (author)
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- Winblad, Bengt (author)
- Karolinska Institutet
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- Behbahani, Homira (author)
- Karolinska Institutet
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- Kamali-Moghaddam, Masood (author)
- Uppsala universitet,Molekylära verktyg,Science for Life Laboratory, SciLifeLab,landegren
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- Frykman, Susanne (author)
- Karolinska Institutet
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- Tjernberg, Lars O (author)
- Karolinska Institutet
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(creator_code:org_t)
- Elsevier BV, 2012
- 2012
- English.
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In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 424:3, s. 476-481
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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Abstract
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- The transmembrane protease complex γ-secretase is responsible for the generation of the neurotoxic amyloid β-peptide (Aβ) from its precursor (APP). Aβ has a causative role in Alzheimer disease, and thus, γ-secretase is a therapeutic target. However, since there are more than 70 γ-secretase substrates besides APP, selective inhibition of APP processing is required. Recent data indicates the existence of several γ-secretase associated proteins (GSAPs) that affect the selection and processing of substrates. Here, we use a γ-secretase inhibitor for affinity purification of γ-secretase and associated proteins from microsomes and detergent resistant membranes (DRMs) prepared from rat or human brain. By tandem mass spectrometry we identified a novel brain GSAP; erlin-2. This protein was recently reported to reside in DRMs in the ER. A proximity ligation assay, as well as co-immunoprecipitation, confirmed the association of erlin-2 with γ-secretase. We found that a higher proportion of erlin-2 was associated with γ-secretase in DRMs than in soluble membranes. siRNA experiments indicated that reduced levels of erlin-2 resulted in a decreased Aβ production, whereas the effect on Notch processing was limited. In summary, we have found a novel brain GSAP, erlin-2, that resides in DRMs and affects Aβ production.
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- ref (subject category)
- art (subject category)
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- By the author/editor
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Teranishi, Yasuh ...
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Hur, Ji-Yeun
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Gu, Gucci Jijuan
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Kihara, Takahiro
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Ishikawa, Taizo
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Nishimura, Takes ...
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show more...
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Winblad, Bengt
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Behbahani, Homir ...
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Kamali-Moghaddam ...
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Frykman, Susanne
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Tjernberg, Lars ...
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show less...
- Articles in the publication
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Biochemical and ...
- By the university
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Uppsala University
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Karolinska Institutet