Stimulation by bone sialoprotein of calcification in osteoblast-like MC3T3-E1 cells.
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.
Zhou
H Y
HY
Department of Biochemistry, School of Dentistry, Hokkaido University, Sapporo, Japan.
Takita
H
H
Fujisawa
R
R
Mizuno
M
M
Kuboki
Y
Y
D016475:3T3 Cells; D000469:Alkaline Phosphatase / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002113:Calcification, Physiologic / Q000187:drug effects*; D004247:DNA / Q000378:metabolism; D058574:Integrin-Binding Sialoprotein; D051379:Mice; D008969:Molecular Sequence Data; D010006:Osteoblasts / Q000166:cytology / Q000187:drug effects / Q000502:physiology*; D012795:Sialoglycoproteins / Q000302:isolation & purification / Q000494:pharmacology*
C546872:Ibsp protein, mouse; D058574:Integrin-Binding Sialoprotein; D012795:Sialoglycoproteins; D004247:DNA; D000469:Alkaline Phosphatase