A proteomic analysis of human bile.
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 (18)O, 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.
Kristiansen
Troels Zakarias
TZ
McKusick-Nathans Institute of Genetic Medicine and Department of Biological Chemistry, Johns Hopkins University, Baltimore, MD 21205, USA.
Bunkenborg
Jakob
J
Gronborg
Mads
M
Molina
Henrik
H
Thuluvath
Paul J
PJ
Argani
Pedram
P
Goggins
Michael G
MG
Maitra
Anirban
A
Pandey
Akhilesh
A
D000595:Amino Acid Sequence; D001646:Bile / Q000378:metabolism*; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007553:Isotope Labeling; D037102:Lectins / Q000737:chemistry*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D020543:Proteome
D037102:Lectins; D020543:Proteome