Systematic analysis of cornification related molecules and development of new treatments for skin disorders.
Project/Area Number |
21791066
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Single-year Grants |
Research Field |
Dermatology
|
Research Institution | University of Toyama |
Principal Investigator |
MAKINO Teruhiko 富山大学, 大学院・医学薬学研究部(医学), 准教授 (90359711)
|
Project Period (FY) |
2009 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2011: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2010: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2009: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | 皮膚生理学 / 皮膚 / 表皮角化細胞 / profilaggrin / TUNEL / TCHHL1 / FLG2 / hornerin / 角化 / ケラチノサイト / フィラグリン / ホルネリン |
Research Abstract |
The Profilaggrin N-terminal(proFLG-N) consists of two distinct domains, an S100-like A-domain and B domain. After proFLG-N transfection at a growing phase of NHK, only proFLG-N expressing cells exhibited DNA degradation. Therefore, A-domain in proFLG-N is responsible for DNA degradation. These results indicate that proFLG-N play an important role in the keratinocyte terminal differentiation, especially in the denucleation process. On the other hand, we identified novel S100 fused-type proteins, filaggrin-2(FLG2) and trichohyalin-like protein 1(TCHHL1). The structural features and expression profile of FLG2 were similar to those of profilaggrin. The deduced amino acid sequence of TCHHL1 contains one trans-membrane domain. The TCHHL1 protein was expressed in the basal layer.
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Report
(4 results)
Research Products
(39 results)