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000136887 0247_ $$2doi$$a10.1002/pmic.201200582
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000136887 041__ $$aEnglish
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000136887 1001_ $$0P:(DE-2719)9000409$$aHogl, Sebastian$$b0$$eFirst author
000136887 245__ $$aLabel-free quantitative analysis of the membrane proteome of Bace1 protease knock-out zebrafish brains.
000136887 260__ $$aWeinheim$$bWiley VCH69157$$c2013
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000136887 520__ $$aThe aspartyl protease BACE1 cleaves neuregulin 1 and is involved in myelination and is a candidate drug target for Alzheimer's disease, where it acts as the β-secretase cleaving the amyloid precursor protein. However, little is known about other substrates in vivo. Here, we provide a proteomic workflow for BACE1 substrate identification from whole brains, combining filter-aided sample preparation, strong-anion exchange fractionation, and label-free quantification. We used bace1-deficient zebrafish and quantified differences in protein levels between wild-type and bace1 -/- zebrafish brains. Over 4500 proteins were identified with at least two unique peptides and quantified in both wild-type and bace1 -/- zebrafish brains. The majority of zebrafish membrane proteins did not show altered protein levels, indicating that Bace1 has a restricted substrate specificity. Twenty-four membrane proteins accumulated in the bace1 -/- brains and thus represent candidate Bace1 substrates. They include several known BACE1 substrates, such as the zebrafish homologs of amyloid precursor protein and the cell adhesion protein L1, which validate the proteomic workflow. Additionally, several candidate substrates with a function in neurite outgrowth and axon guidance, such as plexin A3 and glypican-1 were identified, pointing to a function of Bace1 in neurodevelopment. Taken together, our study provides the first proteomic analysis of knock-out zebrafish tissue and demonstrates that combining gene knock-out models in zebrafish with quantitative proteomics is a powerful approach to address biomedical questions.
000136887 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000136887 542__ $$2Crossref$$i2013-04-02$$uhttp://doi.wiley.com/10.1002/tdm_license_1.1
000136887 542__ $$2Crossref$$i2013-04-02$$uhttp://onlinelibrary.wiley.com/termsAndConditions#vor
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000136887 650_7 $$2NLM Chemicals$$aAmyloid beta-Protein Precursor
000136887 650_7 $$2NLM Chemicals$$aGlypicans
000136887 650_7 $$2NLM Chemicals$$aMembrane Proteins
000136887 650_7 $$2NLM Chemicals$$aPlxna3 protein, zebrafish
000136887 650_7 $$2NLM Chemicals$$aProteome
000136887 650_7 $$2NLM Chemicals$$aReceptors, Cell Surface
000136887 650_7 $$2NLM Chemicals$$aZebrafish Proteins
000136887 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$aAspartic Acid Endopeptidases
000136887 650_2 $$2MeSH$$aAmyloid beta-Protein Precursor: genetics
000136887 650_2 $$2MeSH$$aAmyloid beta-Protein Precursor: metabolism
000136887 650_2 $$2MeSH$$aAnimals
000136887 650_2 $$2MeSH$$aAnimals, Genetically Modified
000136887 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: genetics
000136887 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: metabolism
000136887 650_2 $$2MeSH$$aBrain: metabolism
000136887 650_2 $$2MeSH$$aChemical Fractionation: methods
000136887 650_2 $$2MeSH$$aGlypicans: metabolism
000136887 650_2 $$2MeSH$$aHumans
000136887 650_2 $$2MeSH$$aMembrane Proteins: analysis
000136887 650_2 $$2MeSH$$aMembrane Proteins: genetics
000136887 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000136887 650_2 $$2MeSH$$aProteome: genetics
000136887 650_2 $$2MeSH$$aProteome: metabolism
000136887 650_2 $$2MeSH$$aReceptors, Cell Surface: metabolism
000136887 650_2 $$2MeSH$$aTandem Mass Spectrometry
000136887 650_2 $$2MeSH$$aWorkflow
000136887 650_2 $$2MeSH$$aZebrafish: genetics
000136887 650_2 $$2MeSH$$aZebrafish: metabolism
000136887 650_2 $$2MeSH$$aZebrafish Proteins: analysis
000136887 650_2 $$2MeSH$$aZebrafish Proteins: genetics
000136887 650_2 $$2MeSH$$aZebrafish Proteins: metabolism
000136887 7001_ $$0P:(DE-2719)9000319$$avan Bebber, Frauke$$b1
000136887 7001_ $$0P:(DE-2719)9000408$$aDislich, Bastian$$b2
000136887 7001_ $$0P:(DE-2719)2810327$$aKuhn, Peer-Hendrik$$b3
000136887 7001_ $$0P:(DE-2719)2202037$$aHaass, Christian$$b4
000136887 7001_ $$0P:(DE-2719)2241638$$aSchmid, Bettina$$b5
000136887 7001_ $$0P:(DE-2719)2181459$$aLichtenthaler, Stefan F$$b6$$eLast author
000136887 77318 $$2Crossref$$3journal-article$$a10.1002/pmic.201200582$$b : Wiley, 2013-04-02$$n9$$p1519-1527$$tPROTEOMICS$$v13$$x1615-9853$$y2013
000136887 773__ $$0PERI:(DE-600)2253166-X$$a10.1002/pmic.201200582$$gVol. 13, no. 9, p. 1519 - 1527$$n9$$p1519-1527$$q13:9<1519 - 1527$$tPractical proteomics$$v13$$x1615-9853$$y2013
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