Absolute quantification of protein and post-translational modification abundance with stable isotope-labeled synthetic peptides

Nat Protoc. 2011 Feb;6(2):175-86. doi: 10.1038/nprot.2010.196. Epub 2011 Jan 27.

Abstract

In the analysis of biological systems, it is of interest to identify the components of the system and to monitor their changes in abundance under different conditions. The AQUA (for 'absolute quantification') method allows sensitive and specific targeted quantification of protein and post-translational modifications in complex protein mixtures using stable isotope-labeled peptides as internal standards. Each AQUA experiment is composed of two stages: method development and application to a biological scenario. In the method development stage, peptides from the protein of interest are chosen and then synthesized with stable isotopes such as (13)C, (2)H or (15)N. The abundance of these internal standards and their endogenous counterparts can be measured by mass spectrometry with selected reaction monitoring or selected ion monitoring methods. Once an AQUA method is established, it can be rapidly applied to a wide range of biological samples, from tissue culture cells to human plasma and tissue. After AQUA peptide synthesis, the development, optimization and application of AQUA analyses to a specific biological problem can be achieved in ~1 week. Here we demonstrate the usefulness of this method by monitoring both Polo-like kinase 1 (Plk1) protein abundance in multiple lung cancer cell lines and the extent of Plk1 activation loop phosphorylation (pThr-210) during release from S phase.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Isotopes
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • Deuterium
  • Humans
  • Isotope Labeling
  • Mass Spectrometry
  • Nitrogen Isotopes
  • Polo-Like Kinase 1
  • Protein Processing, Post-Translational*
  • Protein Serine-Threonine Kinases / chemistry
  • Protein Serine-Threonine Kinases / metabolism*
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / metabolism*

Substances

  • Carbon Isotopes
  • Cell Cycle Proteins
  • Nitrogen Isotopes
  • Proto-Oncogene Proteins
  • Deuterium
  • Protein Serine-Threonine Kinases