Amyloid precursor protein is trafficked and secreted via synaptic vesicles.

A large body of evidence has implicated amyloid precursor protein (APP) and its proteolytic derivatives as key players in the physiological context of neuronal synaptogenesis and synapse maintenance, as well as in the pathology of Alzheimer's Disease (AD). Although APP processing and release ar...

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Autores principales: Teja W Groemer, Cora S Thiel, Matthew Holt, Dietmar Riedel, Yunfeng Hua, Jana Hüve, Benjamin G Wilhelm, Jürgen Klingauf
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Publicado: Public Library of Science (PLoS) 2011
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Acceso en línea:https://doaj.org/article/0a96d424466346ceb490fa796332a47d
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spelling oai:doaj.org-article:0a96d424466346ceb490fa796332a47d2021-11-18T06:55:06ZAmyloid precursor protein is trafficked and secreted via synaptic vesicles.1932-620310.1371/journal.pone.0018754https://doaj.org/article/0a96d424466346ceb490fa796332a47d2011-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21556148/?tool=EBIhttps://doaj.org/toc/1932-6203A large body of evidence has implicated amyloid precursor protein (APP) and its proteolytic derivatives as key players in the physiological context of neuronal synaptogenesis and synapse maintenance, as well as in the pathology of Alzheimer's Disease (AD). Although APP processing and release are known to occur in response to neuronal stimulation, the exact mechanism by which APP reaches the neuronal surface is unclear. We now demonstrate that a small but relevant number of synaptic vesicles contain APP, which can be released during neuronal activity, and most likely represent the major exocytic pathway of APP. This novel finding leads us to propose a revised model of presynaptic APP trafficking that reconciles existing knowledge on APP with our present understanding of vesicular release and recycling.Teja W GroemerCora S ThielMatthew HoltDietmar RiedelYunfeng HuaJana HüveBenjamin G WilhelmJürgen KlingaufPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 4, p e18754 (2011)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Teja W Groemer
Cora S Thiel
Matthew Holt
Dietmar Riedel
Yunfeng Hua
Jana Hüve
Benjamin G Wilhelm
Jürgen Klingauf
Amyloid precursor protein is trafficked and secreted via synaptic vesicles.
description A large body of evidence has implicated amyloid precursor protein (APP) and its proteolytic derivatives as key players in the physiological context of neuronal synaptogenesis and synapse maintenance, as well as in the pathology of Alzheimer's Disease (AD). Although APP processing and release are known to occur in response to neuronal stimulation, the exact mechanism by which APP reaches the neuronal surface is unclear. We now demonstrate that a small but relevant number of synaptic vesicles contain APP, which can be released during neuronal activity, and most likely represent the major exocytic pathway of APP. This novel finding leads us to propose a revised model of presynaptic APP trafficking that reconciles existing knowledge on APP with our present understanding of vesicular release and recycling.
format article
author Teja W Groemer
Cora S Thiel
Matthew Holt
Dietmar Riedel
Yunfeng Hua
Jana Hüve
Benjamin G Wilhelm
Jürgen Klingauf
author_facet Teja W Groemer
Cora S Thiel
Matthew Holt
Dietmar Riedel
Yunfeng Hua
Jana Hüve
Benjamin G Wilhelm
Jürgen Klingauf
author_sort Teja W Groemer
title Amyloid precursor protein is trafficked and secreted via synaptic vesicles.
title_short Amyloid precursor protein is trafficked and secreted via synaptic vesicles.
title_full Amyloid precursor protein is trafficked and secreted via synaptic vesicles.
title_fullStr Amyloid precursor protein is trafficked and secreted via synaptic vesicles.
title_full_unstemmed Amyloid precursor protein is trafficked and secreted via synaptic vesicles.
title_sort amyloid precursor protein is trafficked and secreted via synaptic vesicles.
publisher Public Library of Science (PLoS)
publishDate 2011
url https://doaj.org/article/0a96d424466346ceb490fa796332a47d
work_keys_str_mv AT tejawgroemer amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
AT corasthiel amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
AT matthewholt amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
AT dietmarriedel amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
AT yunfenghua amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
AT janahuve amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
AT benjamingwilhelm amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
AT jurgenklingauf amyloidprecursorproteinistraffickedandsecretedviasynapticvesicles
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