Linked Life Data

10666419

Source:http://linkedlifedata.com/resource/pubmed/id/10666419

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-2-24
pubmed:abstractText
Previous studies have shown that multiple serum response factor (SRF)-binding CArG elements were required for smooth muscle cell (SMC)-specific regulation of smooth muscle (SM) alpha-actin expression. However, a critical question remains as to the mechanisms whereby a ubiquitously expressed transcription factor such as SRF might contribute to SMC-specific expression. The goal of the present study was to investigate the hypothesis that SMC-selective expression of SM alpha-actin is due at least in part to (1) unique CArG flanking sequences that distinguish the SM alpha-actin CArGs from other ubiquitously expressed CArG-dependent genes such as c-fos, (2) cooperative interactions between CArG elements, and (3) SRF-dependent binding of SMC-selective proteins to the CArG-containing regions of the promoter. Results demonstrated that specific sequences flanking CArG B were important for promoter activity in SMCs but not in bovine aortic endothelial cells. We also provided evidence indicating that the structural orientation between CArGs A and B was an important determinant of promoter function. Electrophoretic mobility shift assays and methylation interference footprinting demonstrated that a unique SRF-containing complex formed that was selective for SMCs and, furthermore, that this complex was probably stabilized by protein-protein interactions and not by specific interactions with CArG flanking sequences. Taken together, the results of these studies provide evidence that SM alpha-actin expression in SMCs is complex and may involve the formation of a unique multiprotein initiation complex that is coordinated by SRF complexes bound to multiple CArG elements.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1524-4571
pubmed:author
pubmed:issnType
Electronic
pubmed:day
4
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-32
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10666419-Actins, pubmed-meshheading:10666419-Animals, pubmed-meshheading:10666419-Aorta, pubmed-meshheading:10666419-Cattle, pubmed-meshheading:10666419-Cells, Cultured, pubmed-meshheading:10666419-DNA Footprinting, pubmed-meshheading:10666419-DNA Methylation, pubmed-meshheading:10666419-DNA-Binding Proteins, pubmed-meshheading:10666419-Endothelium, Vascular, pubmed-meshheading:10666419-Erythroid-Specific DNA-Binding Factors, pubmed-meshheading:10666419-Gene Expression Regulation, pubmed-meshheading:10666419-Muscle, Smooth, Vascular, pubmed-meshheading:10666419-Mutagenesis, pubmed-meshheading:10666419-Nuclear Proteins, pubmed-meshheading:10666419-Nucleic Acid Conformation, pubmed-meshheading:10666419-Promoter Regions, Genetic, pubmed-meshheading:10666419-Protein Binding, pubmed-meshheading:10666419-Proto-Oncogene Proteins, pubmed-meshheading:10666419-Rats, pubmed-meshheading:10666419-Serum Response Factor, pubmed-meshheading:10666419-Transcription, Genetic, pubmed-meshheading:10666419-Transcription Factors, pubmed-meshheading:10666419-ets-Domain Protein Elk-1, pubmed-meshheading:10666419-ets-Domain Protein Elk-4
pubmed:year
2000
pubmed:articleTitle
Smooth muscle alpha-actin CArG elements coordinate formation of a smooth muscle cell-selective, serum response factor-containing activation complex.
pubmed:affiliation
Department of Molecular Physiology and Biological Physics, University of Virginia Medical School, Charlottesville, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't