Principal Investigator_H.Hirano
Development of mass spectrometry and related techniques for analysis of protein post-translational modifications
Hisashi Hirano
Professor, Proteomics,
researchmap
Our Aim
Our aim is to develop novel techniques for proteomic analysis using mainly mass spectrometry and the related techniques, and to identify disease-associated proteins such as ovarian cancer-, prostate-, lung cancer-, and Kawasaki disease-associated proteins using these techniques. Also, we aim determining the function of them to develop biomarkers and drug targets.
Background
Conventional analytical techniques were useless for effective comprehensive analysis of post-translational modifications (PTMs). However, mass spectrometer, the related techniques, protein databases, and computer software have been rapidly developed to analyze PTMs efficiently and effectively.
Research Overview
We develop more sensitive, accurate and high-throughput techniques suitable for analysis of post-translationally modified proteins associated with diseases. Using these techniques, we identify disease-associated proteins such as ovarian clear cell adenocarcinoma (CCA)-associated proteins, imatinib resistance-associated proteins in gastrointestinal stromal tumor, androgen-independent cell associated proteins in prostate cancer, adverse prognosis associated proteins in lung cancer.
Achievements
We have developed techniques, for example, to identify 3,000 plasma proteins and 2,000 phosphoproteins in each experiment, to analyze proteins from formalin fixed paraffin embedded tissues, to monitor phosphoproteins using phosphoprotein-affinity electrophoresis, and to identify proteins using membrane chip. By use of these techniques, we have identified ~10,000 phosphorylation sites in various cancer cells and tissues, and we found ~240 phosphoproteins of which expression is specific to the cancer cells and tissues. Among them, we found proteins having the possibility to use as drug targets or biomarkers.