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

Profilaggrin N-末端(proFLG-N)由两个不同的结构域组成，一个类似S100的A结构域和一个B结构域。在NHK的生长期转导proFLG-N后，只有表达proFLG-N的细胞出现DNA降解。因此，proFLG-N中的A-结构域与DNA降解有关。这些结果表明，proFlg-N在角质形成细胞的终末分化过程中起重要作用，尤其是在去核过程中。另一方面，我们发现了新的S100融合蛋白，丝状蛋白-2(Flaggrin-2，Flg2)和类毛羽蛋白1(Trichohyalin-like Protein，TCHHL1)。FlG2的结构特征和表达谱与profilaggrin相似。TCHHL1的推导氨基酸序列含有一个跨膜结构域。TCHHL1蛋白在基底层有表达。

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.