A proteomic analysis of human bile

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

Research output: Contribution to journalArticle

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 2004

Fingerprint

Bile
Proteomics
Affinity chromatography
Body fluids
Body Fluids
Affinity Chromatography
Lectins
Proteins
Glycosylation
Asparagine
Liquid chromatography
Proteome
Tumor Biomarkers
Fractionation
Tandem Mass Spectrometry
Electrophoresis
Liquid Chromatography
Labeling
Mass spectrometry
Polysaccharides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Zakarias, T., Bunkenborg, J., Gronborg, M., Molina, H., Thuluvath, P. J., Argani, P., ... 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

A proteomic analysis of human bile. / Zakarias, Troels; Bunkenborg, Jakob; Gronborg, Mads; Molina, Henrik; Thuluvath, Paul J.; Argani, Pedram; Goggins, Michael S; Maitra, Anirban; Pandey, Akhilesh.

In: Molecular and Cellular Proteomics, Vol. 3, No. 7, 07.2004, p. 715-728.

Research output: Contribution to journalArticle

Zakarias, T, Bunkenborg, J, Gronborg, M, Molina, H, Thuluvath, PJ, Argani, P, Goggins, MS, Maitra, A & Pandey, A 2004, 'A proteomic analysis of human bile', Molecular and Cellular Proteomics, vol. 3, no. 7, pp. 715-728. https://doi.org/10.1074/mcp.M400015-MCP200
Zakarias T, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P et al. A proteomic analysis of human bile. Molecular and Cellular Proteomics. 2004 Jul;3(7):715-728. https://doi.org/10.1074/mcp.M400015-MCP200
Zakarias, Troels ; Bunkenborg, Jakob ; Gronborg, Mads ; Molina, Henrik ; Thuluvath, Paul J. ; Argani, Pedram ; Goggins, Michael S ; Maitra, Anirban ; Pandey, Akhilesh. / A proteomic analysis of human bile. In: Molecular and Cellular Proteomics. 2004 ; Vol. 3, No. 7. pp. 715-728.
@article{109ff1abc5c54d9594b3aee198eb7049,
title = "A proteomic analysis of human bile",
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.",
author = "Troels Zakarias and Jakob Bunkenborg and Mads Gronborg and Henrik Molina and Thuluvath, {Paul J.} and Pedram Argani and Goggins, {Michael S} and Anirban Maitra and Akhilesh Pandey",
year = "2004",
month = "7",
doi = "10.1074/mcp.M400015-MCP200",
language = "English (US)",
volume = "3",
pages = "715--728",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "7",

}

TY - JOUR

T1 - A proteomic analysis of human bile

AU - Zakarias, Troels

AU - Bunkenborg, Jakob

AU - Gronborg, Mads

AU - Molina, Henrik

AU - Thuluvath, Paul J.

AU - Argani, Pedram

AU - Goggins, Michael S

AU - Maitra, Anirban

AU - Pandey, Akhilesh

PY - 2004/7

Y1 - 2004/7

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=4043094860&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4043094860&partnerID=8YFLogxK

U2 - 10.1074/mcp.M400015-MCP200

DO - 10.1074/mcp.M400015-MCP200

M3 - Article

VL - 3

SP - 715

EP - 728

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 7

ER -