Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology, 3 Pasteur St, 02-093 Warsaw, Poland.
J Cell Biochem. 2010 Feb 15;109(3):576-84. doi: 10.1002/jcb.22434.
S100A6 (calcyclin) is a calcium binding protein with two EF-hand structures expressed mostly in fibroblasts and epithelial cells. We have established a NIH 3T3 fibroblast cell line stably transfected with siRNA against S100A6 to examine the effect of S100A6 deficiency on non-transformed cell physiology. We found that NIH 3T3 fibroblasts with decreased level of S100A6 manifested altered cell morphology and proliferated at a much slower pace than the control cells. Cell cycle analysis showed that a large population of these cells lost the ability to respond to serum and persisted in the G0/G1 phase. Furthermore, fibroblasts with diminished S100A6 level exhibited morphological changes and biochemical features of cellular senescence as revealed by beta-galactosidase and gelatinase assays. Also, S100A6 deficiency induced changes in the actin cytoskeleton and had a profound impact on cell adhesion and migration. Thus, we have shown that the S100A6 protein is involved in multiple aspects of fibroblast physiology and that its presence ensures normal fibroblast proliferation and function.
S100A6（钙粒蛋白）是一种钙结合蛋白，具有两个 EF 手结构，主要在成纤维细胞和上皮细胞中表达。我们建立了稳定转染针对 S100A6 的 siRNA 的 NIH 3T3 成纤维细胞系，以研究 S100A6 缺乏对非转化细胞生理学的影响。我们发现，S100A6 水平降低的 NIH 3T3 成纤维细胞表现出改变的细胞形态，并且比对照细胞增殖得慢得多。细胞周期分析表明，这些细胞中的很大一部分失去了对血清的反应能力，并持续处于 G0/G1 期。此外，S100A6 水平降低的成纤维细胞表现出细胞衰老的形态变化和生化特征，如β-半乳糖苷酶和明胶酶测定所示。此外，S100A6 缺乏诱导肌动蛋白细胞骨架的变化，并对细胞黏附和迁移有深远影响。因此，我们已经表明，S100A6 蛋白参与成纤维细胞生理学的多个方面，并且其存在确保了正常的成纤维细胞增殖和功能。
