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Cellular Biochemistry Laboratory, Graduate school of Pharmaceutical Sciences, Nagoya University

Transglutaminase Expression Database  [2020 ver. 4]
タンパク質架橋化酵素トランスグルタミナーゼの網羅的な基質(発現)解析データベース


広範なヒト疾患に関わるタンパク質架橋酵素(Transglutaminase: TGase)の役割を理解するためには、各TGaseアイソザイム(哺乳類において8種存在)のmRNAとタンパク質の発現量や局在の理解はもとより、細胞や組織レベルでの活性化量および活性局在性を把握すること、各TGaseアイソザイムにより架橋される標的基質タンパク質を網羅的に理解することが重要である。

私たちはこれまでに、各TGaseアイソザイム選択的な基質となり架橋されるGln残基を含むペプチド配列を同定し、これらのペプチドおよびLys残基を模倣した標識一級アミンを用いて、各種生理的現象(細胞分化や皮膚形成)、病態組織(肝・腎・肺の細胞死や炎症、線維化)において、各TGaseアイソザイムの活性化の程度や局在、基質タンパク質の同定を行ってきた。

In order to understand the role of protein crosslinking enzyme (TGases) in a wide range of human diseases, it is nessesary to evaluate the expression and localization of each TGase isozyme (there are eight species in mammals) in mRNA and protein levels as well as the enzymatic activity. It is also important to comprehensively understand the target substrate proteins cross-linked by each TGase isozyme. So far, we have identified peptide sequences containing Gln residues that are specifically used for crosslinking reaction by TGase in their isozyme-specific manner, and have used these peptides and labeled primary amines that mimic Lys residues to investigate the level and localization of enzymetic activities, as well as globally identify substrate protein for each TGase isozyme in various physiological (cell differentiation and skin formation) and pathological tissues (cell death, inflammation, and fibrosis in the liver, kidney, and lung).











Hideki TATSUKAWA, PhD. Assistant Professor
E-mail: htatsukawa(at)ps.nagoya-u.ac.jp (replace (at) to @)

Kiyotaka HITOMI, PhD. Professor
Graduate School of Pharmaceutical Sciences, Nagoya University,
Tokai National Higher Education and Research System
E-mail: hitomi(at)ps.nagoya-u.ac.jp (replace (at) to @)


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