EPIDERMAL TRANSGLUTAMINASES

转谷氨酰胺酶在受体酰胺之间形成异二肽交联物 赖氨酸的谷氨基残基和供体epsilon-NH2基团。 在表皮和其他层状鳞状上皮组织中， 这些酶被认为参与了可能的交联剂 形成不溶于水的细胞膜的蛋白质成分。使用分子 生物学方法，我们发现有3种不同的 正常人和小鼠表皮中谷氨酰胺转氨酶的活性。这些 被称为K(TGase1)、C(TGase2)和E(TGase3)酶。我们有 编码全长Tgase1和Tgase1基因的cDNA克隆的分离和鉴定 Tgase3系统。TGase1的完整基因组结构(14.1kbp) 系统已经完成。基因组结构方面的工作正在进行中 Tgase3基因。TGase1的全长和缺失构建体 酶在大肠杆菌和哺乳动物细胞中都有表达 努力了解这种酶的结构/功能域。 所有这些研究的目的都是为了确定可能的功能 正常表皮中的这些不同活动，以及这些活动是否或如何 可能参与了病理过程。

Transglutaminases form isodipeptide crosslinks between acceptor amide groups of glutaminyl residues and donor epsilon-NH2 groups of lysines. In the epidermis, and other stratified squamous epithelial tissues, these enzymes are thought to be involved in the crosslinking of putative protein components to form the insoluble cell envelope. Using molecular biology approaches, we have found that there are 3 different transglutaminase activities in normal human and mouse epidermis. These are known as the K (TGase1), C (TGase2) and E (Tgase3) enzymes. We have isolated and characterized cDNA clones encoding full-length Tgase1 and Tgase3 systems. The complete genomic structure (14.1kbp) of the TGase1 system has been completed. Work is in progress on the genomic structure of the Tgase3 gene. Full-length and deletion constructs of the TGase1 enzyme have been expressed in E. coli and in mammalian cells in an effort to understand the structural/functional domains of this enzyme. The aim of all of these studies is to determine the likely functions of these different activities in normal epidermis, and whether or how these may be involved in pathology.