The peptide mimicking small extracellular loop domain of CD82 inhibits tumor cell migration, adhesion and induces apoptosis by inhibiting integrin mediated signaling
The peptide mimicking small extracellular loop domain of CD82 inhibits tumor cell migration, adhesion and induces apoptosis by inhibiting integrin mediated signaling
复制标题
模拟 CD82 胞外小环结构域的肽通过抑制整合素介导的信号传导来抑制肿瘤细胞迁移、粘附并诱导细胞凋亡
DOI：
10.1016/j.bbrc.2018.06.139
复制
发表时间：
2018-09-18
影响因子：
3.1
通讯作者：
Ma, Keli
中科院分区：
文献类型：
--
作者：
Luan, Mingchun;He, Xin;Ma, Keli
在肿瘤转移抑制因子CD 82的细胞外结构域中，大细胞外环（EC2）受到了广泛的关注，其结构和功能已被详细研究。然而，很少有人注意到小的细胞外环（EC 1结构域）。为了研究EC 1在CD 82转移抑制中的作用，合成了模拟EC 1氨基酸序列的多肽（EC 1-mP），并研究了其对肿瘤细胞行为的影响。本文报道了EC 1-mP在体外对癌细胞迁移有明显的抑制作用，减弱癌细胞与纤维连接蛋白的粘附能力，并诱导癌细胞凋亡。EC 1-mP还能抑制SW 620细胞整合素α 5和β 1的表达，降低FAK的磷酸化和ILK的表达。综上所述，这些结果表明该小肽具有CD 82完整分子的功能作用。这一新的发现将提高我们对CD 82抑制转移机制的理解，并表明EC 1模拟肽可能是开发抗转移药物的有希望的候选者。(C)2018由Elsevier Inc.出版
Within the extracellular domains of metastasis suppressor CD82, the large extracellular loop (EC2) has received much of the attention and its structure and function have been studied in detail. However, little attention has been given to the small extracellular loop (EC1 domain). To investigate the function role of EC1 in metastasis suppression of CD82, the peptide mimicking EC1 amino acid sequence (EC1-mP) was synthesized and its effect on cancer cells behavior was examined. Here, we reported that EC1-mP strongly inhibited cancer cell migration in vitro, attnuated the ability of cancer cells adhesion to fibronectin, and induced the apoptosis. Furthermore, the EC1-mP was showed to supprese the expressions of integrins alpha 5 and beta 1, as well as decreased the phosphorylation of FAK and expression of ILK in SW620 cells. Taken together, these results demonstrate that this small peptide has the functional role of CD82 intact molecule. This novel finding will improve our understanding of the mechanism by which CD82 inhibits metastasis, and suggested that EC1 mimic peptide may be a promising candidate for developing anti-metastasis drugs. (C) 2018 Published by Elsevier Inc.