TY - JOUR
T1 - Towards a comprehensive proteome of normal and malignant human colon tissue by 2-D-LC-ESI-MS and 2-DE proteomics and identification of S100A12 as potential cancer biomarker
AU - Thierolf, Michael
AU - Hagmann, Marie Luise
AU - Pfeffer, Michael
AU - Berntenis, Nikolaos
AU - Wild, Norbert
AU - Roeßler, Markus
AU - Palme, Stefan
AU - Karl, Johann
AU - Bodenmüller, Heinz
AU - Rüschoff, Josef
AU - Rossol, Siegbert
AU - Rohr, Gerhard
AU - Rösch, Wolfgang
AU - Friess, Helmut
AU - Eickhoff, Axel
AU - Jauch, Karl Walter
AU - Langen, Hanno
AU - Zolg, Werner
AU - Tacke, Michael
PY - 2008/1
Y1 - 2008/1
N2 - The aim of this study was to characterize the proteome of normal and malignant colonic tissue. We previously studied the colon proteome using 2-DE and MALDINS and identified 734 proteins (Roeßler, M., Rollinger, W., Palme S., Hagmann, M.-L., et al., Clin. Cancer Res. 2005, 11, 6550-6557). Here we report the identification of additional colon proteins from the same set of tissue samples using a complementary nano-flow 2-D-LC-ESI-MS. In total, 484 proteins were identified in colon. Of these, 252 had also been identified by the 2-DE/MALDI-MS approach, whereas 232 proteins were unique to the 2-D-LC-ESI-MS analysis. Comparing protein expression in neoplastic and normal colon tissue indicated elevated expression of several proteins in colorectal cancer, among them the well established tumor marker carcinoembryonic antigen, as well as calnexin, 40S ribosomal protein S15a, serpin H1, and S100A12. Overexpression of these proteins was confirmed by immunoblotting. Serum levels of S100A12 were determined by ELISA and were found to be strongly elevated in colorectal cancer patients compared to healthy individuals. We conclude, that 2-D-LC-ESI-MS is a powerful approach to identify and compare protein profiles of tissue samples, that it is complementary to 2-DE/MALDI-MS approaches and has the potential to identify novel biomarkers.
AB - The aim of this study was to characterize the proteome of normal and malignant colonic tissue. We previously studied the colon proteome using 2-DE and MALDINS and identified 734 proteins (Roeßler, M., Rollinger, W., Palme S., Hagmann, M.-L., et al., Clin. Cancer Res. 2005, 11, 6550-6557). Here we report the identification of additional colon proteins from the same set of tissue samples using a complementary nano-flow 2-D-LC-ESI-MS. In total, 484 proteins were identified in colon. Of these, 252 had also been identified by the 2-DE/MALDI-MS approach, whereas 232 proteins were unique to the 2-D-LC-ESI-MS analysis. Comparing protein expression in neoplastic and normal colon tissue indicated elevated expression of several proteins in colorectal cancer, among them the well established tumor marker carcinoembryonic antigen, as well as calnexin, 40S ribosomal protein S15a, serpin H1, and S100A12. Overexpression of these proteins was confirmed by immunoblotting. Serum levels of S100A12 were determined by ELISA and were found to be strongly elevated in colorectal cancer patients compared to healthy individuals. We conclude, that 2-D-LC-ESI-MS is a powerful approach to identify and compare protein profiles of tissue samples, that it is complementary to 2-DE/MALDI-MS approaches and has the potential to identify novel biomarkers.
KW - 2-D-LC-ESI-MS
KW - 2-DE
KW - Biomarker
KW - Colorectal cancer
KW - S100A12
UR - http://www.scopus.com/inward/record.url?scp=38949206401&partnerID=8YFLogxK
U2 - 10.1002/prca.200780046
DO - 10.1002/prca.200780046
M3 - Article
AN - SCOPUS:38949206401
SN - 1862-8346
VL - 2
SP - 11
EP - 22
JO - Proteomics - Clinical Applications
JF - Proteomics - Clinical Applications
IS - 1
ER -
