Schlaepfer D D, Haigler H T
Department of Biological Chemistry, University of California, Irvine 92717.
J Cell Biol. 1990 Jul;111(1):229-38. doi: 10.1083/jcb.111.1.229.
Annexins are a structurally related family of Ca2+ binding proteins of undertermined biological function. Annexin I (also called lipocortin 1) is a substrate for the EGF-stimulated tyrosine kinase and is postulated to be involved in mitogenic signal transduction. To investigate further the involvement of lipocortin 1 in cell proliferation, we measured lipocortin 1 levels in normal diploid human foreskin fibroblasts (HFF) to determine whether its expression changed as a function of growth status. For comparison, the expression of annexin V (also called endonexin II) was measured in HFF cells. Endonexin II is a protein with similar Ca2+ and phospholipid binding properties as lipocortin 1, but it is not a substrate for tyrosine kinases. Quiescent HFF cell cultures were induced to proliferate by either subculture to lower cell density, EGF stimulation, or serum stimulation. In all three protocols, proliferating HFF cells contained three- to fourfold higher levels of lipocortin 1 and three- to fourfold lower levels of endonexin II than quiescent HFF cells. In contrast, the expression of annexin II (also called calpactin I) and annexin IV (also called endonexin I) remained relatively unchanged in growing and quiescent HFF cells. Lipocortin 1 synthesis rate was eightfold higher and its turnover rate was 1.5-fold slower in proliferating compared to quiescent HFF cells. Endonexin II synthesis rate remained constant but its turnover rate was 2.2-fold faster in proliferating compared to quiescent HFF cells. In a separate set of experiments, annexin expression levels were measured in cultures of rat PC-12 cells, a pheochromocytoma that ceases proliferation and undergoes reversible differentiation into nondividing neuronlike cells in response to nerve growth factor (NGF). After NGF treatment, PC-12 cells expressed fivefold higher levels of endonexin II and 32-fold higher levels of calpactin 1. Lipocortin 1 and endonexin I were not expressed in PC-12 cells. In summary, lipocortin 1 expression exhibited a positive correlation with cell proliferation in HFF cells. The increased expression of endonexin II in quiescent HFF cells and differentiating PC-12 cells implies that this protein may play a more prominent role in nondividing cells.
膜联蛋白是一类结构相关的钙离子结合蛋白家族,其生物学功能尚不清楚。膜联蛋白I(也称为脂皮质素1)是表皮生长因子(EGF)刺激的酪氨酸激酶的底物,据推测参与有丝分裂信号转导。为了进一步研究脂皮质素1在细胞增殖中的作用,我们检测了正常二倍体人包皮成纤维细胞(HFF)中脂皮质素1的水平,以确定其表达是否随生长状态而变化。作为对照,我们检测了HFF细胞中膜联蛋白V(也称为内毒素II)的表达。内毒素II是一种与脂皮质素1具有相似钙离子和磷脂结合特性的蛋白质,但它不是酪氨酸激酶的底物。通过传代培养至较低细胞密度、EGF刺激或血清刺激,诱导静止的HFF细胞培养物增殖。在所有这三种方案中,增殖的HFF细胞中脂皮质素1的水平比静止的HFF细胞高3至4倍,而内毒素II的水平则低3至4倍。相比之下,在生长和静止的HFF细胞中,膜联蛋白II(也称为凝溶胶蛋白I)和膜联蛋白IV(也称为内毒素I)的表达相对不变。与静止的HFF细胞相比,增殖的HFF细胞中脂皮质素1的合成速率高8倍,其周转率慢1.5倍。内毒素II的合成速率保持不变,但其周转率在增殖的HFF细胞中比静止的细胞快2.2倍。在另一组实验中,我们检测了大鼠嗜铬细胞瘤PC-12细胞培养物中膜联蛋白的表达水平。PC-12细胞在神经生长因子(NGF)的作用下停止增殖,并可逆地分化为不分裂的神经元样细胞。NGF处理后,PC-12细胞中内毒素II的表达水平提高了5倍,凝溶胶蛋白1的表达水平提高了32倍。脂皮质素1和内毒素I在PC-12细胞中不表达。总之,在HFF细胞中,脂皮质素1的表达与细胞增殖呈正相关。静止的HFF细胞和分化的PC-12细胞中内毒素II表达的增加表明,这种蛋白可能在不分裂细胞中发挥更突出的作用。