Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2003-10-27
pubmed:abstractText
Although the FGF and TGF-beta families are known to play an important role in regulating vascular endothelial and smooth muscle cell behavior, the influence of these matrix-binding growth factors on microvascular pericyte morphogenesis is not well understood. The current study was undertaken to examine the molecular mechanisms that mediate the effects of the endothelium-produced growth regulators FGF-2 and TGF-beta1 on retinal pericyte proliferation and contractile phenotype.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2, http://linkedlifedata.com/resource/pubmed/chemical/Heparin, http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Myogenic Regulatory Factor 5, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Smad Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta, http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta1
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0146-0404
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4994-5005
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:14578427-Actins, pubmed-meshheading:14578427-Animals, pubmed-meshheading:14578427-Blotting, Northern, pubmed-meshheading:14578427-Cattle, pubmed-meshheading:14578427-Cell Division, pubmed-meshheading:14578427-Cells, Cultured, pubmed-meshheading:14578427-DNA Primers, pubmed-meshheading:14578427-DNA-Binding Proteins, pubmed-meshheading:14578427-Electrophoretic Mobility Shift Assay, pubmed-meshheading:14578427-Fibroblast Growth Factor 2, pubmed-meshheading:14578427-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:14578427-Heparin, pubmed-meshheading:14578427-Muscle Proteins, pubmed-meshheading:14578427-Myogenic Regulatory Factor 5, pubmed-meshheading:14578427-Pericytes, pubmed-meshheading:14578427-Precipitin Tests, pubmed-meshheading:14578427-RNA, Messenger, pubmed-meshheading:14578427-Rabbits, pubmed-meshheading:14578427-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:14578427-Signal Transduction, pubmed-meshheading:14578427-Smad Proteins, pubmed-meshheading:14578427-Trans-Activators, pubmed-meshheading:14578427-Transcription Factors, pubmed-meshheading:14578427-Transforming Growth Factor beta, pubmed-meshheading:14578427-Transforming Growth Factor beta1
pubmed:year
2003
pubmed:articleTitle
FGF-2 antagonizes the TGF-beta1-mediated induction of pericyte alpha-smooth muscle actin expression: a role for myf-5 and Smad-mediated signaling pathways.
pubmed:affiliation
Program in Cellular and Molecular Physiology, Department of Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.