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Mol Cells. 2015 Jul;38(7):624-9. doi: 10.14348/molcells.2015.0013. Epub 2015 Jun 10.

Identification of Protein Markers Specific for Papillary Renal Cell Carcinoma Using Imaging Mass Spectrometry.

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Department of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yongin 446-701, Korea.
The Institute of Natural Science, College of Applied Sciences, Kyung Hee University, Yongin 446-701, Korea.
Department of Pathology, Konkuk University School of Medicine, Seoul 143-701, Korea.
National Cancer Center, Goyang, 410-769, Korea.


Since the emergence of proteomics methods, many proteins specific for renal cell carcinoma (RCC) have been identified. Despite their usefulness for the specific diagnosis of RCC, such proteins do not provide spatial information on the diseased tissue. Therefore, the identification of cancer-specific proteins that include information on their specific location is needed. Recently, matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS) based imaging mass spectrometry (IMS) has emerged as a new tool for the analysis of spatial distribution as well as identification of either proteins or small molecules in tissues. In this report, surgical tissue sections of papillary RCC were analyzed using MALDI-IMS. Statistical analysis revealed several discriminative cancer-specific m/z-species between normal and diseased tissues. Among these m/z-species, two particular proteins, S100A11 and ferritin light chain, which are specific for papillary RCC cancer regions, were successfully identified using LC-MS/MS following protein extraction from independent RCC samples. The expressions of S100A11 and ferritin light chain were further validated by immunohistochemistry of human tissues and tissue microarrays (TMAs) of RCC. In conclusion, MALDI-IMS followed by LC-MS/MS analysis in human tissue identified that S100A11 and ferritin light chain are differentially expressed proteins in papillary RCC cancer regions.


LC-MS/MS; MALDI IMS; MALDI TOF; biomarker; papillary renal cell carcinoma; proteomic analysis

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