| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2006: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2005: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Research Abstract |
Transglutaminase (TGase) is a family of enzymes that catalyzes cross-linking reaction between two or identical proteins. In formation of skin epidermis, several structural proteins are cross-linked by TGase during differentiation. These reaction products are essential for cornification of the mature keratinocytes. For this cross-linking reaction, the mechanisms that TGase isozymes (TGase 1, TGase 3, and TGase 5) are activated in differentiated keratinocytes remained unclarified. Furthermore, how target substrate proteins are catalyzed by each enzyme is unknown. In this study, I searched the responsible enzyme for activation of TGase 3, a main cross-linking enzyme located in cytoplasm, using recombinant protein expressed in baculovirus-infected insect cells. As a result, two lysosome-proteases, cathepsins S and L appeared as activating protease (Chen et al. J.Biol.Chem., 2006). Since this activation is confirmed as in vitro reaction, in vivo mechanism for activation is necessary as future works. However, the acknowledgements contribute to identify substrate proteins for TGase 3. Additionally, I established the system to identify the substrate sequence by TGase (Sugimura et al. J.Biol.Chem., 2006). For establishment of the system, TGase 2 (tissue-type) and Factor XIII (TGase for blood coagulation) were used as target TGase. I successfully identified the motifs for each preferred substrate sequence. This system enables to provide information of substrate proteins that cross-linked by each TGase isozyme.
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