Abstract
Osteopontin is one of a family of phosphorylated sialoproteins found in the extracellular matrices of mineralized connective tissues. Solution studies from a variety of laboratories have shown that while some of these proteins (e.g., osteopontin, dentin sialoprotein) inhibit calcium phosphate production, others, such as bone sialoprotein, can act as a nucleator of calcium phosphate formation. The differences in the behaviors of these proteins can be related to their interactions with mineral crystal nuclei and crystal growth sites. The specificity of these interactions, in turn, can be related to differences in the primary structures of the sialoproteins and to the extent to which they are phosphorylated. In vitro systems for the study of osteopontins and osteopontin-related protein effects on mineral deposition are described, along with mechanisms explaining the contrasting abilities of the polyglutamate-containing bone sialoprotein to act as a nucleator, while the polyaspartate-containing osteopontin and dentin sialoproteins inhibit calcium phosphate formation and growth.