Molecular proteomics imaging of tumor interfaces by mass spectrometry

J Proteome Res. 2010 Feb 5;9(2):1157-64. doi: 10.1021/pr900666q.

Abstract

The specific molecular profiles of ovarian cancer interface zones (IZ), the region between tumors and normal tissues, were evaluated using a new method involving matrix-assisted laser desorption/ionization (MALDI)-imaging mass spectrometry (IMS). We analyzed three ovarian serous carcinomas using MALDI-IMS. Principal component analysis (PCA) was used to evaluate the quality of tissue spatial features based on MALDI-IMS, and for analysis of large data sets of MALDI-IMS. Two-dimensional gel electrophoresis and fluorescence microscopy were used to verify interface-specific proteins. Unique profiles were identified for the tumors, the normal zone, and the IZ. Through MALDI analysis, two interface-specific proteins, plastin 2 and peroxiredoxin 1 (PRDX 1), were identified as differentially regulated between zones. Fluorescence microscopy revealed high expression levels of plastin 2 and PRDX 1 along the IZ of ovarian tumors. This comparative proteomics study using tissue MALDI-IMS suggested that the IZ is different from the adjacent tumor and normal zones, and that plastin 2 and PRDX 1 may be interface markers specific to ovarian tumors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electrophoresis, Gel, Two-Dimensional
  • Female
  • Humans
  • Immunohistochemistry
  • Microscopy, Fluorescence
  • Ovarian Neoplasms / chemistry*
  • Principal Component Analysis
  • Proteomics*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*