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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-1-29
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pubmed:abstractText |
Members of the transforming growth factor superfamily are known to transduce signals via the activation of Smad proteins. Ligand binding to transmembrane cell surface receptors triggers the phosphorylation of pathway-specific Smads. These Smads then complex with Smad 4 and are translocated to the nucleus where they effect gene transcription. Smads 1 and 4 were recently demonstrated to mediate BMP activation of the OPN promoter by inhibiting the interaction of Hoxc-8 protein with a Hox-binding element. While previous studies have indicated that specific DNA sequences are recognized by Smad complexes in several promoters, the role of Smad-binding elements (SBEs) in activation of the OPN promoter by members of the TGFbeta superfamily has not been previously evaluated. In this study we tested the hypothesis that a putative Smad-binding region containing the sequence AGACTGTCTGGAC is involved in the activation of the OPN promoter by members of the TGFbeta superfamily. Functional analyses demonstrated that the both the HBE- and Smad-binding region were involved in BMP-2-induced activation of the promoter, whereas, the HBE appeared to be the primary region involved in activation by TGFbeta. Deletion of the first 9 bases in the Smad-binding region substantially reduced BMP-2-mediated activation of the promoter. These results strongly suggest that both the Hox- and the Smad-binding regions play a role in BMP-2-induced activation of the OPN promoter.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bmp2 protein, mouse,
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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HOXC8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hoxc8 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Osteopontin,
http://linkedlifedata.com/resource/pubmed/chemical/SPP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Smad Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Smad4 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Smad4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Spp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-4827
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
69-74
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11120606-3T3 Cells,
pubmed-meshheading:11120606-Animals,
pubmed-meshheading:11120606-Bone Morphogenetic Protein 2,
pubmed-meshheading:11120606-Bone Morphogenetic Proteins,
pubmed-meshheading:11120606-DNA-Binding Proteins,
pubmed-meshheading:11120606-Homeodomain Proteins,
pubmed-meshheading:11120606-Mice,
pubmed-meshheading:11120606-Osteopontin,
pubmed-meshheading:11120606-Promoter Regions, Genetic,
pubmed-meshheading:11120606-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:11120606-Sialoglycoproteins,
pubmed-meshheading:11120606-Smad Proteins,
pubmed-meshheading:11120606-Smad4 Protein,
pubmed-meshheading:11120606-Trans-Activators,
pubmed-meshheading:11120606-Transcriptional Activation,
pubmed-meshheading:11120606-Transforming Growth Factor beta
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pubmed:year |
2001
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pubmed:articleTitle |
TGFbeta and BMP-2 activation of the OPN promoter: roles of smad- and hox-binding elements.
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pubmed:affiliation |
Cardiovascular Therapeutics, Pfizer Inc., Ann Arbor, Michigan, 48105, USA.
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pubmed:publicationType |
Journal Article
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