Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)
Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)
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DOI：
10.1006/bbrc.2001.5517
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发表时间：
2001-09-07
影响因子：
3.1
通讯作者：
Barraclough, R
中科院分区：
文献类型：
--
作者：
Chen, HL;Fernig, DG;Barraclough, R
实验中S100A4水平的升高在体内诱导良性乳腺肿瘤细胞的转移表型。在人类中，乳腺癌细胞中S100A4的存在与患者存活率的降低密切相关。现在已经使用光学生物传感器检测了S100A4的潜在相互作用结合伙伴。S100A4与非肌球蛋白和P53有显著的相互作用，而与肌动蛋白、原肌球蛋白和微管蛋白无明显相互作用。结果提示，肌球蛋白和P53可能是S100A4的细胞内靶点。S100A4对野生型或突变型Arg-175-His P53的亲和力大于对非肌球蛋白的亲和力。结果提示，S100A4可能通过影响P53的功能及其与肌球蛋白的相互作用而诱导肿瘤转移，其机制与P53的突变状态无关。(C)2001年学术出版社。
Experimentally elevated levels of S100A4 induce a metastatic phenotype in benign mammary tumour cells in vivo. In humans, the presence of S100A4 in breast cancer cells correlates strongly with reduced patient survival. Potential interacting binding partners for S100A4 have now been examined using an optical biosensor. There was significant interaction of S100A4 with non-muscle myosin and p53, but not with actin, tropomyosin or tubulin. The results suggest that myosin and p53 are likely to be intracellular targets of S100A4. S100A4 had a greater affinity for wild-type or mutant arg-175-his p53 than for non-muscle myosin. The results suggest that S100A4 might induce metastasis by influencing the function of p53 as well as through its interaction with myosin and that any mechanism is independent of the mutational status of p53. (C) 2001 Academic Press.