Linked Life Data

15677465

Source:http://linkedlifedata.com/resource/pubmed/id/15677465

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2005-5-9
pubmed:abstractText
Latent transforming growth factor-beta-binding proteins (LTBPs) are extracellular matrix (ECM) glycoproteins that play a major role in the storage of latent TGF beta in the ECM and regulate its availability. Here we show that fibronectin is critical for the incorporation of LTBP1 and transforming growth factor-beta (TGF beta) into the ECM of osteoblasts and fibroblasts. Immunolocalization studies suggested that fibronectin provides an initial scaffold that precedes and patterns LTBP1 deposition but that LTBP1 and fibronectin are later localized in separate fibrillar networks, suggesting that the initial template is lost. Treatment of fetal rat calvarial osteoblasts with a 70-kDa N-terminal fibronectin fragment that inhibits fibronectin assembly impaired incorporation of LTBP1 and TGFbeta into the ECM. Consistent with this, LTBP1 failed to assemble in embryonic fibroblasts that lack the gene for fibronectin. LTBP1 assembly was rescued by full-length fibronectin and superfibronectin, which are capable of assembly into fibronectin fibrils, but not by other fibronectin fragments, including a 160-kDa RGD-containing fragment that activates alpha5beta1 integrins. This suggests that the critical event for LTBP1 assembly is the formation of a fibronectin fibrillar network and that integrin ligation by fibronectin molecules alone is not sufficient. Not only was fibronectin essential for the initial incorporation of LTBP1 into the ECM, but the continued presence of fibronectin was required for the continued assembly of LTBP1. These studies highlight a nonredundant role for fibronectin in LTBP1 assembly into the ECM and suggest a novel role for fibronectin in regulation of TGF beta via LTBP1 interactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18871-80
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15677465-Animals, pubmed-meshheading:15677465-Blotting, Western, pubmed-meshheading:15677465-Cell Line, Tumor, pubmed-meshheading:15677465-Cells, Cultured, pubmed-meshheading:15677465-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:15677465-Extracellular Matrix, pubmed-meshheading:15677465-Fibroblasts, pubmed-meshheading:15677465-Fibronectins, pubmed-meshheading:15677465-Humans, pubmed-meshheading:15677465-Immunohistochemistry, pubmed-meshheading:15677465-Immunoprecipitation, pubmed-meshheading:15677465-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:15677465-Latent TGF-beta Binding Proteins, pubmed-meshheading:15677465-Mice, pubmed-meshheading:15677465-Mice, Transgenic, pubmed-meshheading:15677465-Microscopy, Fluorescence, pubmed-meshheading:15677465-Microscopy, Immunoelectron, pubmed-meshheading:15677465-Osteoblasts, pubmed-meshheading:15677465-Protein Binding, pubmed-meshheading:15677465-Protein Structure, Tertiary, pubmed-meshheading:15677465-Rats, pubmed-meshheading:15677465-Time Factors, pubmed-meshheading:15677465-Transforming Growth Factor beta, pubmed-meshheading:15677465-Transgenes
pubmed:year
2005
pubmed:articleTitle
Fibronectin regulates latent transforming growth factor-beta (TGF beta) by controlling matrix assembly of latent TGF beta-binding protein-1.
pubmed:affiliation
Department of Oral Biology, School of Dentistry, University of Missouri, Kansas City, Missouri 64108, USA. dallass@umkc.edu
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