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Related Experiment Videos

Quantitative proteomics using mass spectrometry.

Salvatore Sechi1, Yoshiya Oda

  • 1National Institute of Diabetes and Digestive and Kidney Diseases, NIH, DHHS, Bethesda, MD 20892-5460, USA. Salvatore_Sechi@nih.gov

Current Opinion in Chemical Biology
|January 28, 2003
PubMed
Summary

Stable isotopes revolutionize quantitative proteomics by enabling accurate protein measurement. Different labeling strategies, including in vivo and in vitro methods, offer versatility for various sample types.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Stable isotopes are crucial internal standards in mass spectrometry.
  • Quantitative proteomics relies on accurate protein concentration determination.
  • Various labeling strategies exist for proteomic analysis.

Purpose of the Study:

  • To review the advancements in stable isotope labeling for quantitative proteomics.
  • To discuss different labeling methodologies and their applications.
  • To highlight the achievements and future needs in proteomic quantification.

Main Methods:

  • Classification of labeling procedures: in vivo, in vitro pre-digestion, and in vitro post-digestion.
  • Application of mass spectrometry for relative protein quantification.

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  • Quantification of post-translational modifications using mass spectrometry.

    • Main Results:

    • Stable isotope labeling has significantly advanced quantitative proteomics.
    • In vivo labeling offers high accuracy for cultured cells.
    • In vitro labeling methods are versatile for diverse samples like body fluids and biopsies.
    • Mass spectrometry strategies show significant achievements in protein and PTM quantification.

    Conclusions:

    • Stable isotope labeling is a powerful tool in quantitative proteomics.
    • Different labeling approaches cater to specific sample types and research questions.
    • Continued technological development is essential for understanding proteome dynamics.