A streamlined platform for high-content functional proteomics of primary human specimens

Nat Methods. 2005 Sep;2(9):691-7. doi: 10.1038/nmeth778.

Abstract

Achieving information content of satisfactory breadth and depth remains a formidable challenge for proteomics. This problem is particularly relevant to the study of primary human specimens, such as tumor biopsies, which are heterogeneous and of finite quantity. Here we present a functional proteomics strategy that unites the activity-based protein profiling and multidimensional protein identification technologies (ABPP-MudPIT) for the streamlined analysis of human samples. This convergent platform involves a rapid initial phase, in which enzyme activity signatures are generated for functional classification of samples, followed by in-depth analysis of representative members from each class. Using this two-tiered approach, we identified more than 50 enzyme activities in human breast tumors, nearly a third of which represent previously uncharacterized proteins. Comparison with cDNA microarrays revealed enzymes whose activity, but not mRNA expression, depicted tumor class, underscoring the power of ABPP-MudPIT for the discovery of new markers of human disease that may evade detection by other molecular profiling methods.

Publication types

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

MeSH terms

  • Biomarkers, Tumor / analysis
  • Biomarkers, Tumor / metabolism*
  • Breast Neoplasms / diagnosis
  • Breast Neoplasms / enzymology*
  • Equipment Design
  • Equipment Failure Analysis
  • Female
  • Gene Expression Profiling / methods*
  • Humans
  • Neoplasm Proteins / analysis
  • Neoplasm Proteins / metabolism*
  • Proteome / analysis
  • Proteome / metabolism*
  • Proteomics / instrumentation*
  • Proteomics / methods
  • Tumor Cells, Cultured

Substances

  • Biomarkers, Tumor
  • Neoplasm Proteins
  • Proteome