rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2003-10-27
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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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
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0146-0404
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4994-5005
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pubmed:dateRevised |
2007-11-14
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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
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pubmed:year |
2003
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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.
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pubmed:affiliation |
Program in Cellular and Molecular Physiology, Department of Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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