Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
2005-7-25
pubmed:abstractText
Biochemical and biophysical methods are used to show that BMP-7 is secreted as a stable complex consisting of the processed growth factor dimer noncovalently associated with its two prodomain propeptide chains and that the BMP-7 complex is structurally similar to the small transforming growth factor beta (TGFbeta) complex. Because the prodomain of TGFbeta interacts with latent TGFbeta-binding proteins, a family of molecules homologous to the fibrillins, the prodomain of BMP-7 was tested for binding to fibrillin-1 or to LTBP-1. The BMP-7 prodomain and BMP-7 complex, but not the separated growth factor dimer, interact with N-terminal regions of fibrillin-1. This interaction may target the BMP-7 complex to fibrillin microfibrils in the extracellular matrix. Immunolocalization of BMP-7 in tissues like the kidney capsule and skin reveals co-localization with fibrillin. However, BMP-7 immunolocalization in other tissues known to be active sites for BMP-7 signaling is not apparent, suggesting that immunolocalization of BMP-7 in certain tissues represents specific extracellular storage sites. These studies suggest that the prodomains of TGFbeta-like growth factors are important for positioning and concentrating growth factors in the extracellular matrix. In addition, they raise the possibility that prodomains of other TGFbeta-like growth factors interact with fibrillins and/or LTBPs and are also targeted to the extracellular matrix.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/BMP7 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 7, http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Glucosides, http://linkedlifedata.com/resource/pubmed/chemical/Histidine, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/LTBP1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Latent TGF-beta Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ltbp1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta, http://linkedlifedata.com/resource/pubmed/chemical/fibrillin, http://linkedlifedata.com/resource/pubmed/chemical/octyl-beta-D-glucoside
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27970-80
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15929982-Amino Acid Sequence, pubmed-meshheading:15929982-Animals, pubmed-meshheading:15929982-Binding Sites, pubmed-meshheading:15929982-Bone Morphogenetic Protein 7, pubmed-meshheading:15929982-Bone Morphogenetic Proteins, pubmed-meshheading:15929982-Cell Line, pubmed-meshheading:15929982-DNA, Complementary, pubmed-meshheading:15929982-Dimerization, pubmed-meshheading:15929982-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:15929982-Extracellular Matrix, pubmed-meshheading:15929982-Glucosides, pubmed-meshheading:15929982-Histidine, pubmed-meshheading:15929982-Humans, pubmed-meshheading:15929982-Hydrogen-Ion Concentration, pubmed-meshheading:15929982-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:15929982-Kidney, pubmed-meshheading:15929982-Latent TGF-beta Binding Proteins, pubmed-meshheading:15929982-Light, pubmed-meshheading:15929982-Mice, pubmed-meshheading:15929982-Mice, Inbred BALB C, pubmed-meshheading:15929982-Microfilament Proteins, pubmed-meshheading:15929982-Microscopy, Electron, pubmed-meshheading:15929982-Microscopy, Fluorescence, pubmed-meshheading:15929982-Molecular Sequence Data, pubmed-meshheading:15929982-Protein Binding, pubmed-meshheading:15929982-Protein Structure, Secondary, pubmed-meshheading:15929982-Protein Structure, Tertiary, pubmed-meshheading:15929982-Recombinant Proteins, pubmed-meshheading:15929982-Scattering, Radiation, pubmed-meshheading:15929982-Shadowing (Histology), pubmed-meshheading:15929982-Signal Transduction, pubmed-meshheading:15929982-Transforming Growth Factor beta, pubmed-meshheading:15929982-Ultraviolet Rays
pubmed:year
2005
pubmed:articleTitle
The prodomain of BMP-7 targets the BMP-7 complex to the extracellular matrix.
pubmed:affiliation
Shriners Hospital for Children, Portland, Oregon 97239, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural