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Maier, S.K. ; Hahne, H.* ; Moghaddas Gholami, A.* ; Balluff, B. ; Meding, S. ; Schoene, C. ; Walch, A.K. ; Kuster, B.*

Comprehensive identification of proteins from MALDI imaging.

Mol. Cell. Proteomics 12, 2901-2910 (2013)
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Open Access Green as soon as Postprint is submitted to ZB.
MALDI imaging mass spectrometry (MALDI IMS) is a powerful tool for the visualization of proteins in tissues and has demonstrated considerable diagnostic and prognostic value. One main challenge is that the molecular identity of such potential biomarkers mostly remains unknown. We introduce a generic method that removes this issue by systematically identifying the proteins embedded in the MALDI matrix using a combination of bottom-up and top-down proteomics. The analyses of ten human tissues lead to the identification of 1,400 abundant and soluble proteins constituting the set of proteins detectable by MALDI IMS including >90% of all IMS biomarkers reported in the literature. Top-down analysis of the matrix proteome identified 124 mostly N- and C-terminally fragmented proteins indicating considerable protein processing activity in tissues. All protein identification data from this study as well as the IMS literature has been deposited into MaTisse, a new publically available database which we anticipate will become a valuable resource for the IMS community.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Biomarkers; Imaging; MALDI IMS; Mass Spectrometry; Protein Identification; Tissues; Mass-spectrometry; Tissue-sections; High-resolution; Gastric-cancer; Peptides; Signatures; Fragment; Markers; Samples; Tumors
ISSN (print) / ISBN 1535-9476
e-ISSN 1535-9484
Quellenangaben Volume: 12, Issue: 10, Pages: 2901-2910 Article Number: , Supplement: ,
Publisher American Society for Biochemistry and Molecular Biology
Publishing Place Bethesda
Reviewing status Peer reviewed