Systematic analysis of cornification related molecules and development of new treatments for skin disorders.

  • 牧野, 輝彦 (Principal Investigator)

Project Details

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.
StatusFinished
Effective start/end date2009/01/012011/12/31

Funding

  • Japan Society for the Promotion of Science: ¥4,160,000.00

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