Zumbrunn J, Trueb B
M. E. Müller-Institute for Biomechanics, University of Bern, Switzerland.
Eur J Biochem. 1996 Oct 15;241(2):657-63. doi: 10.1111/j.1432-1033.1996.00657.x.
We have cloned the gene for a novel LIM-domain protein from human fibroblasts whose expression is substantially decreased in simian-virus-40-(SV40)-transformed cells. This protein has a calculated molecular mass of 61 kDa and comprises a proline-rich domain followed by three LIM motifs. It appears to be identical to the focal adhesion protein p83 that has recently been isolated and characterized from porcine and human platelets. Hybridization experiments demonstrate a very low degree of evolutionary conservation of its sequence between mammals and birds. It is therefore possible that the novel protein represents the human equivalent of the chicken protein zyxin as the two proteins display a very similar overall structure, although their amino acid sequences diverge markedly from each other. The repression of this zyxin-related protein in virally transformed fibroblasts may explain, at least in part, the dramatic morphological changes that occur at the cell surface and in the cytoskeleton of transformed cells.
我们从人成纤维细胞中克隆了一种新型LIM结构域蛋白的基因，其在猿猴病毒40（SV40）转化的细胞中表达显著降低。该蛋白的计算分子量为61 kDa，包含一个富含脯氨酸的结构域，其后跟着三个LIM基序。它似乎与最近从猪和人血小板中分离并鉴定的粘着斑蛋白p83相同。杂交实验表明，其序列在哺乳动物和鸟类之间的进化保守程度非常低。因此，尽管这两种蛋白的氨基酸序列明显不同，但由于它们具有非常相似的整体结构，这种新型蛋白有可能代表鸡蛋白zyxin的人类等同物。在病毒转化的成纤维细胞中这种zyxin相关蛋白的抑制可能至少部分解释了在转化细胞的细胞表面和细胞骨架中发生的显著形态变化。
