Comprehensive proteomic analysis of human pancreatic juice

J Proteome Res. Sep-Oct 2004;3(5):1042-55. doi: 10.1021/pr0499085.

Abstract

Proteomic technologies provide an excellent means for analysis of body fluids for cataloging protein constituents and identifying biomarkers for early detection of cancers. The biomarkers currently available for pancreatic cancer, such as CA19-9, lack adequate sensitivity and specificity contributing to late diagnosis of this deadly disease. In this study, we carried out a comprehensive characterization of the "pancreatic juice proteome" in patients with pancreatic adenocarcinoma. Pancreatic juice was first fractionated by 1-dimensional gel electrophoresis and subsequently analyzed by liquid chromatography tandem mass spectrometry (LC-MS/MS). A total of 170 unique proteins were identified including known pancreatic cancer tumor markers (e.g., CEA, MUC1) and proteins overexpressed in pancreatic cancers (e.g., hepatocarcinoma-intestine-pancreas/pancreatitis-associated protein (HIP/PAP) and lipocalin 2). In addition, we identified a number of proteins that have not been previously described in pancreatic juice (e.g., tumor rejection antigen (pg96) and azurocidin). Interestingly, a novel protein that is 85% identical to HIP/PAP was identified, which we have designated as PAP-2. The proteins identified in this study could be directly assessed for their potential as biomarkers for pancreatic cancer by quantitative proteomics methods or immunoassays.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Agglutinins / analysis
  • Agglutinins / genetics
  • Agglutinins / metabolism
  • Amino Acid Sequence
  • Antigens, Neoplasm / analysis
  • Antigens, Neoplasm / genetics
  • Antigens, Neoplasm / metabolism
  • Antimicrobial Cationic Peptides
  • Biomarkers, Tumor / analysis
  • Biomarkers, Tumor / genetics
  • Biomarkers, Tumor / metabolism
  • Blood Proteins / analysis
  • Blood Proteins / metabolism
  • Calcium-Binding Proteins / genetics
  • Carrier Proteins / analysis
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Cell Adhesion Molecules / analysis
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism
  • Chromatography, Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression / genetics
  • Glycoproteins / genetics
  • Humans
  • Lectins, C-Type / analysis
  • Lectins, C-Type / genetics
  • Lectins, C-Type / metabolism
  • Lithostathine
  • Mass Spectrometry
  • Membrane Proteins / analysis
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Pancreatic Juice / chemistry*
  • Pancreatic Juice / metabolism
  • Pancreatic Neoplasms / metabolism*
  • Pancreatitis-Associated Proteins
  • Peptide Fragments / analysis
  • Phylogeny
  • Proteome / analysis*
  • Proteome / classification
  • Proteome / genetics
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Receptors, Cell Surface / analysis
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Trypsin / metabolism
  • alpha-Defensins / analysis
  • alpha-Defensins / genetics
  • alpha-Defensins / metabolism

Substances

  • Agglutinins
  • Antigens, Neoplasm
  • Antimicrobial Cationic Peptides
  • Biomarkers, Tumor
  • Blood Proteins
  • Calcium-Binding Proteins
  • Carrier Proteins
  • Cell Adhesion Molecules
  • DMBT1 protein, human
  • Glycoproteins
  • Lectins, C-Type
  • Lithostathine
  • Membrane Proteins
  • Pancreatitis-Associated Proteins
  • Peptide Fragments
  • Proteome
  • REG1A protein, human
  • REG3A protein, human
  • REG4 protein, human
  • RNA, Messenger
  • Receptors, Cell Surface
  • Reg3a protein, rat
  • Reg3b protein, rat
  • Sycn protein, rat
  • alpha-Defensins
  • cationic antimicrobial protein CAP 37, human
  • human neutrophil peptide 3
  • Trypsin