@misc{oai:repo.qst.go.jp:00067653,
 author = {Michikawa, Yuichi and Umetsu, Atsushi and Kouda, Masakazu and Kawai, Seiko and Saegusa, Kumiko and Ban, Sadayuki and Iwakawa, Mayumi and Harada, Yoshinobu and Imai, Takashi and 道川 祐市 and 梅津 篤 and 神田 将和 and 川井 聖子 and 三枝 公美子 and 伴 貞幸 and 岩川 眞由美 and 原田 良信 and 今井 高志},
 month = {Oct},
 note = {It is important to know physiological properties of cancer cells for effective radiation therapy of patients.  We decided to develop a convenient proteomic approach to investigate molecules corresponding to the physiological properties of individual cancer cell lines.  The protein molecules we focused for this purpose were those with modification of side chain amino acid, since in many cases the modification is reversible and is utilized for regulation of the function of protein.  The overall profile of modified proteins should have substantial potential in reflecting cellular physiological properties.
The proteomic approach we are currently developing contains 1D SDS-PAGE of total cell lysate followed by quantitative Western blotting using anti-modified amino acid antibody.  Thus, the profile contains one-dimensional list of the molecular weight of modified protein and its fluorescence signal intensity detected after ECL reaction.  To perform the Western blotting analysis quantitatively, which is the key point of this work, we have made several improvements.  The most important one is triplicated standard and sample data acquisition on single membrane, which is difficult and laborious to perform by 2D PAGE analysis, for the collection of accurate and reliable data.  The profiling data of different cell lines will be further processed by band matching then statistical analysis to create hierarchical trees among them.
As an initial analysis we are planning to investigate tyrosine-phosphorylated protein profile of 35 individual human cell lines (32 cancer cell lines and 3 normal fibroblasts) whose X-ray radiation sensitivity have been known., 第76回日本生化学会大会},
 title = {Convenient clustering method of cancer cell lines by their one-dimensional protein modification profiles},
 year = {2003}
}