Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-11-24
pubmed:abstractText
Bone sialoprotein (BSP) and osteopontin (OPN) belong to the small integrin-binding ligand N-linked glycoprotein (SIBLING) family, whose members interact with bone cells and bone mineral. Previously, we showed that BSP knockout (BSP(-/-) ) mice have a higher bone mass than wild type (BSP(+/+) ) littermates, with very low bone-formation activity and reduced osteoclast surfaces and numbers. Here we report that approximately twofold fewer tartrate-resistant acid phosphatase (TRACP)-positive cells and approximately fourfold fewer osteoclasts form in BSP(-/-) compared with BSP(+/+) spleen cell cultures. BSP(-/-) preosteoclast cultures display impaired proliferation and enhanced apoptosis. Addition of RGD-containing proteins restores osteoclast number in BSP(-/-) cultures to BSP(+/+) levels. The expression of osteoclast-associated genes is markedly altered in BSP(-/-) osteoclasts, with reduced expression of cell adhesion and migration genes (?V integrin chain and OPN) and increased expression of resorptive enzymes (TRACP and cathepsin K). The migration of preosteoclasts and mature osteoclasts is impaired in the absence of BSP, but resorption pit assays on dentine slices show no significant difference in pit numbers between BSP(+/+) and BSP(-/-) osteoclasts. However, resorption of mineral-coated slides by BSP(-/-) osteoclasts is markedly impaired but is fully restored by coating the mineral substrate with hrBSP and partly restored by hrOPN coating. In conclusion, lack of BSP affects both osteoclast formation and activity, which is in accordance with in vivo findings. Our results also suggest at least some functional redundancy between BSP and OPN that remains to be clarified.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1523-4681
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 American Society for Bone and Mineral Research.
pubmed:issnType
Electronic
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2669-79
pubmed:dateRevised
2011-4-28
pubmed:meshHeading
pubmed-meshheading:20812227-Animals, pubmed-meshheading:20812227-Apoptosis, pubmed-meshheading:20812227-Biological Markers, pubmed-meshheading:20812227-Bone Resorption, pubmed-meshheading:20812227-Cell Count, pubmed-meshheading:20812227-Cell Differentiation, pubmed-meshheading:20812227-Cell Movement, pubmed-meshheading:20812227-Cell Proliferation, pubmed-meshheading:20812227-Cells, Cultured, pubmed-meshheading:20812227-Dentin, pubmed-meshheading:20812227-Durapatite, pubmed-meshheading:20812227-Gene Expression Profiling, pubmed-meshheading:20812227-Humans, pubmed-meshheading:20812227-Integrin-Binding Sialoprotein, pubmed-meshheading:20812227-Mice, pubmed-meshheading:20812227-Minerals, pubmed-meshheading:20812227-Oligopeptides, pubmed-meshheading:20812227-Osteoclasts, pubmed-meshheading:20812227-Osteogenesis, pubmed-meshheading:20812227-Osteopontin, pubmed-meshheading:20812227-Recombinant Proteins, pubmed-meshheading:20812227-Spleen
pubmed:year
2010
pubmed:articleTitle
Bone sialoprotein deficiency impairs osteoclastogenesis and mineral resorption in vitro.
pubmed:affiliation
Université de Lyon, Saint-Etienne, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't