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Quantitative proteomic profiling reveals differentially regulated proteins in cystic fibrosis cells

Academic Article
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Overview

authors

  • Rauniyar, N.
  • Gupta, V.
  • Balch, William E.
  • Yates III, John

publication date

  • November 2014

journal

  • Journal of Proteome Research  Journal

abstract

  • The most prevalent cause of cystic fibrosis (CF) is the deletion of a phenylalanine residue at position 508 in CFTR (ΔF508-CFTR) protein. The mutated protein fails to fold properly, is retained in the endoplasmic reticulum via the action of molecular chaperones, and is tagged for degradation. In this study, the differences in protein expression levels in CF cell models were assessed using a systems biology approach aided by the sensitivity of MudPIT proteomics. Analysis of the differential proteome modulation without a priori hypotheses has the potential to identify markers that have not yet been documented. These may also serve as the basis for developing new diagnostic and treatment modalities for CF. Several novel differentially expressed proteins observed in our study are likely to play important roles in the pathogenesis of CF and may serve as a useful resource for the CF scientific community.

subject areas

  • Biomarkers
  • Cystic Fibrosis
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Gene Expression Regulation
  • Humans
  • Proteomics
  • Systems Biology
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Research

keywords

  • CFTR
  • Cystic Fibrosis
  • MudPIT
  • NSAF
  • cystic fibrosis transmembrane conductance regulator
  • label free
  • mass spectrometry
  • proteomics
  • spectral count
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Identity

PubMed Central ID

  • PMC4224989

International Standard Serial Number (ISSN)

  • 1535-3893

Digital Object Identifier (DOI)

  • 10.1021/pr500370g

PubMed ID

  • 24818864
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Additional Document Info

start page

  • 4668

end page

  • 4675

volume

  • 13

issue

  • 11

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