67LR的结构和功能及其与表没食子儿茶素没食子酸酯的相互作用

67LR—structure,function,and interaction with epigallocatechingallate

相对分子质量为67 000的层粘连蛋白受体(67LR)是一种细胞外基质的非整合素型表面受体,在肿瘤细胞中表达明显高于正常细胞。它是由一种小分子多肽——相对分子质量为37 000的层粘连蛋白受体前体(37LRP)通过脂肪酸乙酰化转变而来。67LR广泛参与肿瘤细胞的生长、转移、侵袭和凋亡过程,不仅是层粘连蛋白的受体,还可作为其他多种病毒和朊蛋白的受体。67LR是表没食子儿茶素没食子酸酯(EGCG)主要的膜表面受体,EGCG通过与67LR相互作用调控Toll样受体、MAPK和NF-κB等信号转导通路,对肿瘤的生长、转移抑制以及促凋亡有显著作用。文章综述了近年来关于67LR及其与EGCG相互作用机制的研究进展。

The laminin receptor （67LR）, relative molecular mass 67 000, is a non-integrin cell surface receptor for the extracellular matrix, with a higher expression in tumor cells than normal ones. The 67LR originates from 37LRP （relative molecular mass 37 000） through fatty acid acylation. It is widely involved in several processes of tumor cells, such as growth, metastasis, invasion, and apoptosis. It is not only a receptor for laminin but for several viruses and prion proteins. As the major surface receptor for epigallocatechingallate （ EGCG）, 67LR can coordinate with EGCG in regulation of several signal pathways and in inhibition of tumor growth and metastasis and promotion of apoptosis. The studies on mechanism of interaction between 67LR and EGCG are reviewed in this article.