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

前丝聚蛋白N-末端（proFLG-N）由两个不同的结构域组成，S100样A结构域和B结构域。在NHK的生长期转染proFLG-N后，仅表达proFLG-N的细胞表现出DNA降解。因此，proFLG-N中的A结构域负责DNA降解。这些结果表明proFLG-N在角质形成细胞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，我们确定了新的S100融合型蛋白，聚丝蛋白-2（FLG 2）和透明质蛋白样蛋白1（TCHHL 1）。FLG 2的结构特征和表达谱与原丝聚蛋白相似。TCHHL 1的氨基酸序列含有一个跨膜结构域。TCHHL 1蛋白在基底层表达。

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.