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Quantitative proteomic profiling reveals novel region‐specific markers in the adult mouse brain

Despite major advances in neuroscience, a comprehensive understanding of the structural and functional components of the adult brain compartments remains to be fully elucidated at a quantitative molecular level. Indeed, over half of the soluble‐ and membrane‐annotated proteins are currently unmapped... Full description

Journal Title: PROTEOMICS February 2014, Vol.14(2-3), pp.241-261
Main Author: Dagley, Laura F.
Other Authors: White, Carl A. , Liao, Yang , Shi, Wei , Smyth, Gordon K. , Orian, Jacqueline M. , Emili, Andrew , Purcell, Anthony W.
Format: Electronic Article Electronic Article
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Subjects:
Ms
ID: ISSN: 1615-9853 ; E-ISSN: 1615-9861 ; DOI: 10.1002/pmic.201300196
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recordid: wj10.1002/pmic.201300196
title: Quantitative proteomic profiling reveals novel region‐specific markers in the adult mouse brain
format: Article
creator:
  • Dagley, Laura F.
  • White, Carl A.
  • Liao, Yang
  • Shi, Wei
  • Smyth, Gordon K.
  • Orian, Jacqueline M.
  • Emili, Andrew
  • Purcell, Anthony W.
subjects:
  • Membrane Proteins
  • Ms
  • Myelin Interactome
  • O‐Based Stable Isotope Labeling
  • Quantitative Proteomics
ispartof: PROTEOMICS, February 2014, Vol.14(2-3), pp.241-261
description: Despite major advances in neuroscience, a comprehensive understanding of the structural and functional components of the adult brain compartments remains to be fully elucidated at a quantitative molecular level. Indeed, over half of the soluble‐ and membrane‐annotated proteins are currently unmapped within online digital brain atlases. In this study, two complementary approaches were used to assess the unique repertoire of proteins enriched within select regions of the adult mouse , including the brain stem, cerebellum, and remaining brain hemispheres. Of the 1200 proteins visualized by 2‐, approximately 150 (including cytosolic and membrane proteins) were found to exhibit statistically significant changes in relative abundance thus representing putative region‐specific brain markers. In addition to using a high‐precision ‐labeling strategy for the quantitative ‐/ mapping of membrane proteins isolated from myelin‐enriched fractions, we have identified over 1000 proteins that have yet to be described in any other mammalian myelin proteome. A comparison of our myelin proteome was made to an existing transcriptome database containing m abundance profiles during oligodendrocyte differentiation and has confirmed statistically significant abundance changes for ∼500 of these newly mapped proteins, thus revealing new roles in oligodendrocyte and myelin biology. These data offer a resource for the neuroscience community studying the molecular basis for specialized neuronal activities in the and myelin‐related disorders. The proteomics data associated with this manuscript have been deposited to the roteomechange onsortium with the dataset identifier 000327 ().
language:
source:
identifier: ISSN: 1615-9853 ; E-ISSN: 1615-9861 ; DOI: 10.1002/pmic.201300196
fulltext: fulltext
issn:
  • 1615-9853
  • 16159853
  • 1615-9861
  • 16159861
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titleQuantitative proteomic profiling reveals novel region‐specific markers in the adult mouse brain
creatorDagley, Laura F. ; White, Carl A. ; Liao, Yang ; Shi, Wei ; Smyth, Gordon K. ; Orian, Jacqueline M. ; Emili, Andrew ; Purcell, Anthony W.
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subjectMembrane Proteins ; Ms ; Myelin Interactome ; O‐Based Stable Isotope Labeling ; Quantitative Proteomics
descriptionDespite major advances in neuroscience, a comprehensive understanding of the structural and functional components of the adult brain compartments remains to be fully elucidated at a quantitative molecular level. Indeed, over half of the soluble‐ and membrane‐annotated proteins are currently unmapped within online digital brain atlases. In this study, two complementary approaches were used to assess the unique repertoire of proteins enriched within select regions of the adult mouse , including the brain stem, cerebellum, and remaining brain hemispheres. Of the 1200 proteins visualized by 2‐, approximately 150 (including cytosolic and membrane proteins) were found to exhibit statistically significant changes in relative abundance thus representing putative region‐specific brain markers. In addition to using a high‐precision ‐labeling strategy for the quantitative ‐/ mapping of membrane proteins isolated from myelin‐enriched fractions, we have identified over 1000 proteins that have yet to be described in any other mammalian myelin proteome. A comparison of our myelin proteome was made to an existing transcriptome database containing m abundance profiles during oligodendrocyte differentiation and has confirmed statistically significant abundance changes for ∼500 of these newly mapped proteins, thus revealing new roles in oligodendrocyte and myelin biology. These data offer a resource for the neuroscience community studying the molecular basis for specialized neuronal activities in the and myelin‐related disorders. The proteomics data associated with this manuscript have been deposited to the roteomechange onsortium with the dataset identifier 000327 ().
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abstractDespite major advances in neuroscience, a comprehensive understanding of the structural and functional components of the adult brain compartments remains to be fully elucidated at a quantitative molecular level. Indeed, over half of the soluble‐ and membrane‐annotated proteins are currently unmapped within online digital brain atlases. In this study, two complementary approaches were used to assess the unique repertoire of proteins enriched within select regions of the adult mouse , including the brain stem, cerebellum, and remaining brain hemispheres. Of the 1200 proteins visualized by 2‐, approximately 150 (including cytosolic and membrane proteins) were found to exhibit statistically significant changes in relative abundance thus representing putative region‐specific brain markers. In addition to using a high‐precision ‐labeling strategy for the quantitative ‐/ mapping of membrane proteins isolated from myelin‐enriched fractions, we have identified over 1000 proteins that have yet to be described in any other mammalian myelin proteome. A comparison of our myelin proteome was made to an existing transcriptome database containing m abundance profiles during oligodendrocyte differentiation and has confirmed statistically significant abundance changes for ∼500 of these newly mapped proteins, thus revealing new roles in oligodendrocyte and myelin biology. These data offer a resource for the neuroscience community studying the molecular basis for specialized neuronal activities in the and myelin‐related disorders. The proteomics data associated with this manuscript have been deposited to the roteomechange onsortium with the dataset identifier 000327 ().
doi10.1002/pmic.201300196
pages241-261
date2014-02