TY - JOUR
T1 - MALDI imaging mass spectrometry reveals COX7A2, TAGLN2 and S100-A10 as novel prognostic markers in Barrett's adenocarcinoma
AU - Elsner, Mareike
AU - Rauser, Sandra
AU - Maier, Stefan
AU - Schöne, Cédrik
AU - Balluff, Benjamin
AU - Meding, Stephan
AU - Jung, Gerhard
AU - Nipp, Martin
AU - Sarioglu, Hakan
AU - Maccarrone, Giuseppina
AU - Aichler, Michaela
AU - Feuchtinger, Annette
AU - Langer, Rupert
AU - Jütting, Uta
AU - Feith, Marcus
AU - Küster, Bernhard
AU - Ueffing, Marius
AU - Zitzelsberger, Horst
AU - Höfler, Heinz
AU - Walch, Axel
N1 - Funding Information:
A. Walch gratefully acknowledges the financial support of the Federal Ministry of Education and Research (BMBF) Germany (Grant no. 01EZ0803 , no. 0315508A and no. 01IB10004E ) and the Deutsche Forschungsgemeinschaft ( SFB 824 TP B1 , SFB 824 TP Z2 , and WA 1656/3-1 ). The authors thank Ulrike Buchholz, Claudia-Mareike Pflüger and Andreas Voss for the excellent technical assistance.
PY - 2012/8/3
Y1 - 2012/8/3
N2 - To characterize proteomic changes found in Barrett's adenocarcinoma and its premalignant stages, the proteomic profiles of histologically defined precursor and invasive carcinoma lesions were analyzed by MALDI imaging MS. For a primary proteomic screening, a discovery cohort of 38 fresh frozen Barrett's adenocarcinoma patient tissue samples was used. The goal was to find proteins that might be used as markers for monitoring cancer development as well as for predicting regional lymph node metastasis and disease outcome. Using mass spectrometry for protein identification and validating the results by immunohistochemistry on an independent validation set, we could identify two of 60 differentially expressed m/z species between Barrett's adenocarcinoma and the precursor lesion: COX7A2 and S100-A10. Furthermore, among 22. m/z species that are differentially expressed in Barrett's adenocarcinoma cases with and without regional lymph node metastasis, one was identified as TAGLN2. In the validation set, we found a correlation of the expression levels of COX7A2 and TAGLN2 with a poor prognosis while S100-A10 was confirmed by multivariate analysis as a novel independent prognostic factor in Barrett's adenocarcinoma. Our results underscore the high potential of MALDI imaging for revealing new biologically significant molecular details from cancer tissues which might have potential for clinical application. This article is part of a Special Issue entitled: Translational Proteomics.
AB - To characterize proteomic changes found in Barrett's adenocarcinoma and its premalignant stages, the proteomic profiles of histologically defined precursor and invasive carcinoma lesions were analyzed by MALDI imaging MS. For a primary proteomic screening, a discovery cohort of 38 fresh frozen Barrett's adenocarcinoma patient tissue samples was used. The goal was to find proteins that might be used as markers for monitoring cancer development as well as for predicting regional lymph node metastasis and disease outcome. Using mass spectrometry for protein identification and validating the results by immunohistochemistry on an independent validation set, we could identify two of 60 differentially expressed m/z species between Barrett's adenocarcinoma and the precursor lesion: COX7A2 and S100-A10. Furthermore, among 22. m/z species that are differentially expressed in Barrett's adenocarcinoma cases with and without regional lymph node metastasis, one was identified as TAGLN2. In the validation set, we found a correlation of the expression levels of COX7A2 and TAGLN2 with a poor prognosis while S100-A10 was confirmed by multivariate analysis as a novel independent prognostic factor in Barrett's adenocarcinoma. Our results underscore the high potential of MALDI imaging for revealing new biologically significant molecular details from cancer tissues which might have potential for clinical application. This article is part of a Special Issue entitled: Translational Proteomics.
KW - Barrett's adenocarcinoma
KW - COX7A2
KW - Carcinogenesis
KW - MALDI imaging mass spectrometry
KW - S100-A10
KW - TAGLN2
UR - http://www.scopus.com/inward/record.url?scp=84864092193&partnerID=8YFLogxK
U2 - 10.1016/j.jprot.2012.02.012
DO - 10.1016/j.jprot.2012.02.012
M3 - Article
C2 - 22365974
AN - SCOPUS:84864092193
SN - 1874-3919
VL - 75
SP - 4693
EP - 4704
JO - Journal of Proteomics
JF - Journal of Proteomics
IS - 15
ER -