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Amino acid-coded tagging approaches in quantitative proteomics.

Xian Chen1, Liwei Sun, Yanbao Yu

  • 1Institutes of Biomedical Sciences, Fudan University, 138 Yixueyuan Road, Shanghai, 20003, China. xian_chen@med.unc.edu

Expert Review of Proteomics
|February 10, 2007
PubMed
Summary
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Mass spectrometry quantitative proteomics uses amino acid-coded mass tagging for efficient protein analysis. This review covers key methods like iTRAQ for high-throughput identification of differentially expressed proteins and interactions.

Area of Science:

  • Proteomics
  • Biochemistry
  • Molecular Biology

Background:

  • Mass spectrometry-based quantitative proteomics aims to improve efficiency, accuracy, and throughput.
  • In vitro and in vivo tagging methods are crucial for global-scale comparative studies of proteins and modifications.

Purpose of the Study:

  • To review and summarize major amino acid-coded mass tagging-based quantitative proteomics approaches.
  • To evaluate the strengths and weaknesses of these methods in identifying differentially expressed or post-translational modified proteins.

Main Methods:

  • Amino acid-coded mass tagging introduces pair-wise isotope signals for peptides containing tagged amino acids.
  • Methods discussed include isotope-coded affinity tag, isobaric tags for relative and absolute quantification (iTRAQ), and stable isotope labeling by amino acids in cell culture.

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Main Results:

  • These gel-free, in-spectra quantitative mechanisms enable high-throughput identification of proteins regulated by cellular stress.
  • Exploration of these methods facilitates the identification and characterization of large-scale protein-protein interactions.

Conclusions:

  • Quantitative proteome changes provide insights into molecular mechanisms.
  • Identification of interconnected protein relationships can reveal novel targets for diagnosis and therapeutic intervention.