Source:http://linkedlifedata.com/resource/pubmed/id/10699973
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-3-29
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pubmed:abstractText |
Bone morphogenetic protein-2 (BMP-2) stimulates the differentiation of osteoblastic cells. However, the mechanisms involved in this effect are not well characterized. In this study, we determined the role of the cell-cell adhesion molecules N-cadherin and E-cadherin in the promotion of osteoblast differentiation by BMP-2 in immortalized human neonatal calvaria (IHNC) cells. In cells cultured in aggregates, recombinant human BMP-2 (rhBMP-2) increased messenger RNA levels for alkaline phosphatase (ALP), the osteoblast specific transcription factor Osf2/Cbfa1 and osteocalcin, and enhanced in vitro osteogenesis in long-term culture. RT-PCR, immunocytochemical, and Western blot analyses showed that IHNC cells express E-cadherin, N-cadherin, and neural cell adhesion molecule (N-CAM) mRNA and protein. Treatment with rhBMP-2 induced a rapid and transient increase in N-cadherin and E-cadherin but not N-CAM, mRNA, and protein levels. Incubation with the RNA polymerase II inhibitor 5, 6-dichloro-1-beta-D-ribofuranosyl benzimidazole prevented the upregulation of N- and E-cadherins induced by rhBMP-2, suggesting that transcription is necessary for this effect. N- and E-cadherins were functional because rhBMP-2 increased cell-cell adhesion in a cell aggregation assay, and this effect was largely blocked by N-cadherin- and E-cadherin-neutralizing antibodies. In addition, N- and E-cadherin antibodies decreased the basal ALP activity and completely suppressed the rhBMP-2-induced increase in ALP activity and mRNA levels. Furthermore, anti-N-cadherin or anti-E-cadherin antibodies markedly decreased Osf2/Cbfa1 mRNA levels and abolished the rhBMP-2-induced increased Osf2/Cbfa1 expression, and reduced the increased osteocalcin mRNA levels induced by rhBMP-2. We conclude that rhBMP-2 rapidly and transiently increases N- and E-cadherin expression, and this effect mediates the rhBMP-2-induced early promotion of cell-cell adhesion and osteoblast marker gene expression in human calvaria cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BMP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 2,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/recombinant human bone...
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9541
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:volume |
183
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
117-28
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10699973-Bone Morphogenetic Protein 2,
pubmed-meshheading:10699973-Bone Morphogenetic Proteins,
pubmed-meshheading:10699973-Cadherins,
pubmed-meshheading:10699973-Cell Adhesion,
pubmed-meshheading:10699973-Cell Differentiation,
pubmed-meshheading:10699973-Cell Division,
pubmed-meshheading:10699973-Cells, Cultured,
pubmed-meshheading:10699973-Gene Expression Regulation,
pubmed-meshheading:10699973-Humans,
pubmed-meshheading:10699973-Infant, Newborn,
pubmed-meshheading:10699973-Kinetics,
pubmed-meshheading:10699973-Osteoblasts,
pubmed-meshheading:10699973-Osteogenesis,
pubmed-meshheading:10699973-Recombinant Proteins,
pubmed-meshheading:10699973-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10699973-Skull,
pubmed-meshheading:10699973-Time Factors,
pubmed-meshheading:10699973-Transforming Growth Factor beta
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pubmed:year |
2000
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pubmed:articleTitle |
N- and E-cadherin mediate early human calvaria osteoblast differentiation promoted by bone morphogenetic protein-2.
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pubmed:affiliation |
INSERM U 349, Affiliated CNRS, Cell and Molecular Biology of Bone and Cartilage, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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