A proteomic analysis of human bile

Troels Zakarias, Jakob Bunkenborg, Mads Gronborg, Henrik Molina, Paul J. Thuluvath, Pedram Argani, Michael G. Goggins, Anirban Maitra, Akhilesh Pandey

Research output: Contribution to journalReview article

124 Scopus citations

Abstract

We have carried out a comprehensive characterization of human bile to define the bile proteome. Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry. Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown. A large majority of the identified proteins have not been previously described in bile. Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by 18O, we have identified a total of 33 glycosylation sites. The strategy described in this study should be generally applicable for a detailed proteomic analysis of most body fluids. In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.

Original languageEnglish (US)
Pages (from-to)715-728
Number of pages14
JournalMolecular and Cellular Proteomics
Volume3
Issue number7
DOIs
StatePublished - Jul 1 2004

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Molecular Biology

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    Zakarias, T., Bunkenborg, J., Gronborg, M., Molina, H., Thuluvath, P. J., Argani, P., Goggins, M. G., Maitra, A., & Pandey, A. (2004). A proteomic analysis of human bile. Molecular and Cellular Proteomics, 3(7), 715-728. https://doi.org/10.1074/mcp.M400015-MCP200