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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2007-3-19
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pubmed:abstractText |
Highly purified fractions of bone extracts capable of inducing ectopic bone formation have been reported to contain peptides corresponding to the mature active regions of the TGF-beta-like bone morphogenetic proteins (BMPs) 2-7, and to the prodomain region of the metalloproteinase BMP1. Co-purification of BMPs 2-7 with BMP1 prodomain sequences through the multiple biochemical steps used in these previous reports has suggested the possibility of interactions between the BMP1 prodomain and BMPs 2-7. Here we demonstrate that the BMP1 prodomain binds BMPs 2 and 4 with high specificity and with a KD of approximately 11 nM, in the physiological range. It is further demonstrated that the BMP1 prodomain is capable of modulating signaling by BMPs 2 and 4 in vitro and in vivo, and that endogenous BMP1 prodomain-BMP4 complexes exist in cell culture media and in tissues.
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pubmed:grant |
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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/BMP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BMP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BMP4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 2,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 4,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/bmp4 protein, zebrafish
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9053-62
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17255107-Animals,
pubmed-meshheading:17255107-Bone Morphogenetic Protein 1,
pubmed-meshheading:17255107-Bone Morphogenetic Protein 2,
pubmed-meshheading:17255107-Bone Morphogenetic Protein 4,
pubmed-meshheading:17255107-Bone Morphogenetic Proteins,
pubmed-meshheading:17255107-Cell Membrane,
pubmed-meshheading:17255107-Humans,
pubmed-meshheading:17255107-Kinetics,
pubmed-meshheading:17255107-Metalloendopeptidases,
pubmed-meshheading:17255107-Nucleic Acid Hybridization,
pubmed-meshheading:17255107-Osteoblasts,
pubmed-meshheading:17255107-Phenotype,
pubmed-meshheading:17255107-Protein Binding,
pubmed-meshheading:17255107-Protein Structure, Tertiary,
pubmed-meshheading:17255107-Signal Transduction,
pubmed-meshheading:17255107-Surface Plasmon Resonance,
pubmed-meshheading:17255107-Transforming Growth Factor beta,
pubmed-meshheading:17255107-Zebrafish,
pubmed-meshheading:17255107-Zebrafish Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Bone morphogenetic protein 1 prodomain specifically binds and regulates signaling by bone morphogenetic proteins 2 and 4.
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pubmed:affiliation |
Program in Molecular and Cellular Pharmacology, University of Wisconsin, Madison, Wisconsin 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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