Thim L
Department of Protein Chemistry, Novo Nordisk A/S, Bagsvaerd, Denmark.
Cell Mol Life Sci. 1997 Dec;53(11-12):888-903. doi: 10.1007/s000180050108.
The unique structure in which six cysteine residues in a sequence of 38 or 39 amino acid residues form three disulphide bonds in a 1-5, 2-4 and 3-6 configuration constitutes the basic elements of a trefoil domain. Today three mammalian trefoil factors (TFF1, TFF2 and TFF3) containing one or two trefoil domains are known. Trefoil factors are usually associated with the mucin layer of the gastrointestinal tract. Early studies on trefoil factors concentrated on structure elucidation and sites of expression in health and disease, whereas studies over the last 3-5 years have focused on the mechanism of action and the search for specific receptors. This review summarises our present knowledge of trefoil peptide structures, their sites of expression, and their protection and repair functions, with a focus on the mechanism by which these peptides exert their biological function.
在由38或39个氨基酸残基组成的序列中，六个半胱氨酸残基以1-5、2-4和3-6构型形成三个二硫键的独特结构构成了三叶因子结构域的基本元件。如今已知有三种含有一个或两个三叶因子结构域的哺乳动物三叶因子（TFF1、TFF2和TFF3）。三叶因子通常与胃肠道的黏液层相关。早期对三叶因子的研究集中在结构解析以及在健康和疾病状态下的表达部位，而过去3至5年的研究则聚焦于作用机制以及寻找特异性受体。本综述总结了我们目前对三叶肽结构、其表达部位以及保护和修复功能的认识，重点关注这些肽发挥生物学功能的机制。
