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rdf:type |
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lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0027819,
umls-concept:C0028778,
umls-concept:C0041491,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0332206,
umls-concept:C0441712,
umls-concept:C0442805,
umls-concept:C0527443,
umls-concept:C1704256,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
2002-12-6
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pubmed:abstractText |
Human neuroblastoma SH-SY5Y cells were used to study the effects of transforming growth factor beta1 (TGF-beta1) and bone morphogenetic protein 2 (BMP-2) on neuronal differentiation and acquisition of a catecholaminergic phenotype. SH-SY5Y cells express the intracellular factors activated through the receptors of the TGFbeta superfamily members, Smad1 and Smad4, as in basal conditions or after differentiation with 12-O-tetradecanoyl-phorbol-13-acetate (TPA) or retinoic acid (RA). TGF-beta1 and BMP-2 induce differentiation in SH-SY5Y cells by different pathways: the effect of TGF-beta1 is potentiated by TPA and the effect of BMP-2 is blocked by RA. Cell differentiation due to TGF-beta1 treatment is accompanied by an increase in tyrosine hydroxylase (TH) expression, more pronounced in the presence of TPA or RA and counteracted by BMP-2. BMP-2 and RA both induce noncatecholaminergic cell differentiation, and together they may induce choline acetyltransferase expression in serum-cultured cells. In conclusion, our results suggest that TGF-beta1 and BMP-2 may contribute, in opposite ways, to regulation of the neuronal catecholaminergic phenotype.
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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/BMP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 2,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Catecholamines,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ID1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Inhibitor of Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMAD1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SMAD4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Smad Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Smad1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Smad4 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/TGFB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Plasminogen Activator,
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,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-8993
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2002 Elsevier Science B.V.
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
958
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
152-60
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12468040-Bone Morphogenetic Protein 2,
pubmed-meshheading:12468040-Bone Morphogenetic Proteins,
pubmed-meshheading:12468040-Catecholamines,
pubmed-meshheading:12468040-Cell Differentiation,
pubmed-meshheading:12468040-Cell Size,
pubmed-meshheading:12468040-Central Nervous System,
pubmed-meshheading:12468040-Culture Media, Serum-Free,
pubmed-meshheading:12468040-DNA-Binding Proteins,
pubmed-meshheading:12468040-Humans,
pubmed-meshheading:12468040-Inhibitor of Differentiation Protein 1,
pubmed-meshheading:12468040-Neuroblastoma,
pubmed-meshheading:12468040-Neurons,
pubmed-meshheading:12468040-Phenotype,
pubmed-meshheading:12468040-Repressor Proteins,
pubmed-meshheading:12468040-Smad Proteins,
pubmed-meshheading:12468040-Smad1 Protein,
pubmed-meshheading:12468040-Smad4 Protein,
pubmed-meshheading:12468040-Sympathetic Nervous System,
pubmed-meshheading:12468040-Tissue Plasminogen Activator,
pubmed-meshheading:12468040-Trans-Activators,
pubmed-meshheading:12468040-Transcription Factors,
pubmed-meshheading:12468040-Transforming Growth Factor beta,
pubmed-meshheading:12468040-Transforming Growth Factor beta1,
pubmed-meshheading:12468040-Tretinoin,
pubmed-meshheading:12468040-Tumor Cells, Cultured,
pubmed-meshheading:12468040-Tyrosine 3-Monooxygenase,
pubmed-meshheading:12468040-Up-Regulation
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pubmed:year |
2002
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pubmed:articleTitle |
TGF-beta1 increases tyrosine hydroxylase expression by a mechanism blocked by BMP-2 in human neuroblastoma SH-SY5Y cells.
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pubmed:affiliation |
Unitat de Bioquímica, Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, c/Feixa Llarga s/n, E-08907-Hospitalet del Llobregat, Barcelona, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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