Source:http://linkedlifedata.com/resource/pubmed/id/10854066
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2000-7-6
|
pubmed:abstractText |
The myofibroblast is responsible for the generation of contractile force associated with wound contraction and pathological contractures and is characterized by the presence of alpha-smooth muscle (alpha-sm) actin-containing stress fibers, vinculin-containing fibronexus adhesion complexes, and fibronectin fibrils containing the ED-A splice variant. Transforming growth factor-beta1 (TGF-beta1) can promote the expression of alpha-sm actin in myofibroblasts, but the functional significance of this increased expression is unclear. In this study, we demonstrate, using the stress-relaxed collagen lattice contraction assay, that TGF-beta1 promoted a dose-dependent increase in the generation of contractile force in myofibroblasts and a concomitant increase in the expression of alpha-sm actin. We also demonstrate that TGF-beta1 enhanced the formation of the structural elements important in myofibroblast contractile force generation and transmission, including stress fibers, vinculin-containing fibronexus adhesion complexes, and fibronectin fibrils, and that this enhancement occurred prior to, and independent of, alpha-sm actin expression. This differentiated myofibroblast phenotype was not stable. Removal of TGF-beta1 resulted in reduced expression of alpha-sm actin as well as a decreased assembly of stress fibers and vinculin-containing adhesion complexes; however, there was no reduction in fibronectin fibrils. We conclude that TGF-beta1 promotes the morphological and functional differentiation of the myofibroblast by first enhancing the formation of the structural elements characteristic of the myofibroblast followed by increased expression of alpha-sm actin and contractile force generation.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0014-4827
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
257
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
180-9
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10854066-Actins,
pubmed-meshheading:10854066-Cell Differentiation,
pubmed-meshheading:10854066-Cells, Cultured,
pubmed-meshheading:10854066-Dose-Response Relationship, Drug,
pubmed-meshheading:10854066-Fibroblasts,
pubmed-meshheading:10854066-Humans,
pubmed-meshheading:10854066-Transforming Growth Factor beta,
pubmed-meshheading:10854066-Wound Healing
|
pubmed:year |
2000
|
pubmed:articleTitle |
Transforming growth factor-beta1 promotes the morphological and functional differentiation of the myofibroblast.
|
pubmed:affiliation |
Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City 73104, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|