Yamanishi K, Liew F M, Konishi K, Yasuno H, Doi H, Hirano J, Fukushima S
Department of Dermatology, Kyoto Prefectural University of Medicine, Japan.
Biochem Biophys Res Commun. 1991 Mar 29;175(3):906-13. doi: 10.1016/0006-291x(91)91651-r.
We have isolated a cDNA encoding human epidermal transglutaminase, a key enzyme of terminal differentiation of keratinocytes. A cDNA library from cultured human keratinocytes was screened by a PCR-amplified partial cDNA fragment of the enzyme with oligonucleotide primers based on the homology of the transglutaminase family. The cDNA is 2734 bp coding a protein of 817 amino acids. The several regions including the active site cysteine residue are highly conserved among the transglutaminase family. However, the charged N-terminal domain is unique to the epidermal transglutaminse, suggesting that the region is involved in the function of the enzyme in keratinocytes.
我们已经分离出一种编码人表皮转谷氨酰胺酶的cDNA，它是角质形成细胞终末分化的关键酶。利用基于转谷氨酰胺酶家族同源性设计的寡核苷酸引物，通过该酶的PCR扩增部分cDNA片段筛选来自培养的人角质形成细胞的cDNA文库。该cDNA为2734bp，编码一个含817个氨基酸的蛋白质。包括活性位点半胱氨酸残基在内的几个区域在转谷氨酰胺酶家族中高度保守。然而，带电荷的N端结构域是表皮转谷氨酰胺酶所特有的，这表明该区域参与了该酶在角质形成细胞中的功能。
