Zhou H Y, Takita H, Fujisawa R, Mizuno M, Kuboki Y
Department of Biochemistry, School of Dentistry, Hokkaido University, Sapporo, Japan.
Calcif Tissue Int. 1995 May;56(5):403-7. doi: 10.1007/BF00301610.
Bone sialoprotein (BSP) containing an Arg-Gly-Asp cell-binding sequence was purified from bovine bone 4 M guanidine-HCl extract after HCl demineralization by a series of chromatographic procedures. When this protein was coated on culture dishes in the presence of type I collagen, it increased both DNA content and alkaline phosphatase (ALP) activity in osteoblast-like MC3T3-E1 cells, and stimulated calcification in the cells, whereas fibronectin, another cell-binding protein, showed a marked increase in the DNA content but had little effect on the ALP activity. These findings suggest that BSP is mitogenic for preosteoblasts and differentiating the cells into osteoblasts, thereby stimulating bone calcification.
通过一系列色谱方法,从经盐酸脱矿质处理的牛骨4M盐酸胍提取物中纯化出含有精氨酸 - 甘氨酸 - 天冬氨酸细胞结合序列的骨唾液蛋白(BSP)。当这种蛋白质在I型胶原蛋白存在的情况下包被在培养皿上时,它增加了成骨样MC3T3 - E1细胞中的DNA含量和碱性磷酸酶(ALP)活性,并刺激细胞钙化,而另一种细胞结合蛋白纤连蛋白虽使DNA含量显著增加,但对ALP活性影响很小。这些发现表明,BSP对前成骨细胞具有促有丝分裂作用,并使细胞分化为成骨细胞,从而刺激骨钙化。