Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-12-12
pubmed:abstractText
We show that tyrosine phosphorylation of FAK was increased as precartilage condensation occurred, followed by a subsequent decrease in proliferation of in vitro micromass culture of wing bud mesenchymal cells. FAK was associated with fibronectin and paxillin, which were maximal at day 3 of culture. FAK was also associated with signaling molecules such as PLC-gamma and PI3-kinase through c-Src. The beta1 integrin antibody and several inhibitors of signaling molecules such as herbimycin A, U73122, LY294002, as well as cytochalasin D, an actin depolymerizing agent, remarkably decreased tyrosine phosphorylation of FAK and its association with fibronectin and paxillin during condensation. resulting in a marked inhibition of condensation and chondrogenesis. Taken together, our findings suggest that beta1 integrin-mediated interaction of mesenchymal cells and fibronectin signals to accelerate the precartilage condensation through tyrosine phosphorylation of FAK and its association with paxillin. This signaling pathway is required for precartilage condensation and subsequent cartilage nodule formation in chondrogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29, http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin D, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins, http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Protein-Tyrosine..., http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Paxillin, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C gamma, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta, http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
522-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11095944-Animals, pubmed-meshheading:11095944-Antigens, CD29, pubmed-meshheading:11095944-Cartilage, pubmed-meshheading:11095944-Cell Differentiation, pubmed-meshheading:11095944-Cell Division, pubmed-meshheading:11095944-Cells, Cultured, pubmed-meshheading:11095944-Chick Embryo, pubmed-meshheading:11095944-Cytochalasin D, pubmed-meshheading:11095944-Cytoskeletal Proteins, pubmed-meshheading:11095944-Enzyme Inhibitors, pubmed-meshheading:11095944-Fibronectins, pubmed-meshheading:11095944-Focal Adhesion Protein-Tyrosine Kinases, pubmed-meshheading:11095944-Insulin, pubmed-meshheading:11095944-Isoenzymes, pubmed-meshheading:11095944-Mesoderm, pubmed-meshheading:11095944-Paxillin, pubmed-meshheading:11095944-Phosphatidylinositol 3-Kinases, pubmed-meshheading:11095944-Phospholipase C gamma, pubmed-meshheading:11095944-Phosphoproteins, pubmed-meshheading:11095944-Phosphorylation, pubmed-meshheading:11095944-Protein-Tyrosine Kinases, pubmed-meshheading:11095944-Signal Transduction, pubmed-meshheading:11095944-Transforming Growth Factor beta, pubmed-meshheading:11095944-Type C Phospholipases, pubmed-meshheading:11095944-src-Family Kinases
pubmed:year
2000
pubmed:articleTitle
Association of focal adhesion kinase with fibronectin and paxillin is required for precartilage condensation of chick mesenchymal cells.
pubmed:affiliation
Department of Biology, College of Natural Sciences, Taegu, 702-701, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't