2. Conclusion

In this article, we reviewed analytical method in MSI analyses of FFPE tissues. This method for protein extraction from FFPE enabled proteomic analysis. With the combination of label-free LC-MS accompanied by precise laser microdissection enabled in situ proteomic analysis, new pathological findings are obtained.

Proteomic studies by MSI have recently been developed extensively for the identification of peptides in tissues [5, 34]. In this study, the application of MSI method leads to a significant improvement in the signal intensity FFPE tissues. The treatment improved the quality of signals obtained from FFPE specimens by swelling of the deparaffinized sample and increasing tissue permeability. For precise diagnosis, FFPE specimens provide more informatic histologic findings than frozen samples. Therefore, establishment of technique for proteomic study using FFPE contributes to the identification of novel diagnostic markers. To obtain specific markers, it is necessary to exclude nonspecific abundant proteins, including collagens, keratins, beta tubulin, and vimentin. Proteomic studies represent a promising approach to the discovery of novel diagnostic markers and understanding of the pathogenesis of cardiac remodeling. MSI may provide information about the histologic diagnosis of AMI, and several sarcomeric proteins may be a promising marker for the diagnosis of AMI. ROI and HCA analyses proved to be useful tools for the analysis of signal distribution patterns of infarcted tissues. When supplemented by these analyses, IMS may be a promising technique for the identification of biomarkers for pathological studies that involve the comparison of diseased and control areas.
