Gk. Hunter et Ha. Goldberg, NUCLEATION OF HYDROXYAPATITE BY BONE SIALOPROTEIN, Proceedings of the National Academy of Sciences of the United Statesof America, 90(18), 1993, pp. 8562-8565
Bone sialoprotein (BSP) and osteopontin, the major phosphorylated prot
eins of mammalian bone, have been proposed to function in the initiati
on of mineralization. To test this hypothesis, the effects of BSP and
osteopontin on hydroxyapatite crystal formation were determined by usi
ng a steady-state agarose gel system. At low calcium phosphate concent
rations, no accumulation of calcium and phosphate occurred in control
gels or gels containing osteopontin. Gels containing BSP at 1-5 mug/ml
, however, exhibited a visible precipitation band and significantly el
evated Ca + PO4 contents. By powder x-ray diffraction, the precipitate
formed in the presence of BSP was shown to be hydroxyapatite. These f
indings suggest that bone sialoprotein may be involved in the nucleati
on of hydroxyapatite at the mineralization front of bone.