Hunter G K, Goldberg H A
Faculty of Dentistry, University of Western Ontario, London, Canada.
Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8562-5. doi: 10.1073/pnas.90.18.8562.
Bone sialoprotein (BSP) and osteopontin, the major phosphorylated proteins of mammalian bone, have been proposed to function in the initiation of mineralization. To test this hypothesis, the effects of BSP and osteopontin on hydroxyapatite crystal formation were determined by using a steady-state agarose gel system. At low calcium phosphate concentrations, no accumulation of calcium and phosphate occurred in control gels or gels containing osteopontin. Gels containing BSP at 1-5 micrograms/ml, however, exhibited a visible precipitation band and significantly elevated Ca + PO4 contents. By powder x-ray diffraction, the precipitate formed in the presence of BSP was shown to be hydroxyapatite. These findings suggest that bone sialoprotein may be involved in the nucleation of hydroxyapatite at the mineralization front of bone.
骨唾液蛋白(BSP)和骨桥蛋白是哺乳动物骨骼中的主要磷酸化蛋白,有人提出它们在矿化起始过程中发挥作用。为了验证这一假设,通过使用稳态琼脂糖凝胶系统测定了BSP和骨桥蛋白对羟基磷灰石晶体形成的影响。在低磷酸钙浓度下,对照凝胶或含有骨桥蛋白的凝胶中未出现钙和磷的积累。然而,含有1-5微克/毫升BSP的凝胶呈现出可见的沉淀带,且钙+磷含量显著升高。通过粉末X射线衍射表明,在BSP存在下形成的沉淀为羟基磷灰石。这些发现提示骨唾液蛋白可能参与了骨矿化前沿羟基磷灰石的成核过程。