Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
2001-7-30
pubmed:abstractText
The slow myosin heavy chain 3 gene (slow MyHC3) is restricted in its expression to the atrial chambers of the heart. Understanding its regulation provides a basis for determination of the mechanisms controlling chamber-specific gene expression in heart development. The observed chamber distribution results from repression of slow MyHC3 gene expression in the ventricles. A binding site, the vitamin D response element (VDRE), for a heterodimer of vitamin D receptor (VDR) and retinoic X receptor alpha (RXR alpha) within the slow MyHC3 promoter mediates chamber-specific expression of the gene. Irx4, an Iroquois family homeobox gene whose expression is restricted to the ventricular chambers at all stages of development, inhibits AMHC1, the chick homolog of quail slow MyHC3, gene expression within developing ventricles. Repression of the slow MyHC3 gene in ventricular cardiomyocytes by Irx4 requires the VDRE. Unlike VDR and RXR alpha, Irx4 does not bind directly to the VDRE. Instead two-hybrid and co-immunoprecipitation assays show that Irx4 interacts with the RXR alpha component of the VDR/RXR alpha heterodimer and that the amino terminus of the Irx4 protein is required for its inhibitory action. These observations indicate that the mechanism of atrial chamber-specific expression requires the formation of an inhibitory protein complex composed of VDR, RXR alpha, and Irx4 that binds at the VDRE inhibiting slow MyHC3 expression in the ventricles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/AMHC1 protein, chicken, http://linkedlifedata.com/resource/pubmed/chemical/Atrial Myosins, http://linkedlifedata.com/resource/pubmed/chemical/Avian Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Irx4 protein, Gallus gallus, http://linkedlifedata.com/resource/pubmed/chemical/Myosin Heavy Chains, http://linkedlifedata.com/resource/pubmed/chemical/Myosins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitriol, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
28835-41
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11382777-Animals, pubmed-meshheading:11382777-Atrial Myosins, pubmed-meshheading:11382777-Avian Proteins, pubmed-meshheading:11382777-Binding Sites, pubmed-meshheading:11382777-Cells, Cultured, pubmed-meshheading:11382777-Chick Embryo, pubmed-meshheading:11382777-Cloning, Molecular, pubmed-meshheading:11382777-DNA-Binding Proteins, pubmed-meshheading:11382777-Gene Deletion, pubmed-meshheading:11382777-Gene Expression Regulation, pubmed-meshheading:11382777-Heart Atria, pubmed-meshheading:11382777-Heart Ventricles, pubmed-meshheading:11382777-Homeodomain Proteins, pubmed-meshheading:11382777-Myocardium, pubmed-meshheading:11382777-Myosin Heavy Chains, pubmed-meshheading:11382777-Myosins, pubmed-meshheading:11382777-Polymerase Chain Reaction, pubmed-meshheading:11382777-Promoter Regions, Genetic, pubmed-meshheading:11382777-Protein Biosynthesis, pubmed-meshheading:11382777-Quail, pubmed-meshheading:11382777-Receptors, Calcitriol, pubmed-meshheading:11382777-Receptors, Retinoic Acid, pubmed-meshheading:11382777-Retinoid X Receptors, pubmed-meshheading:11382777-Transcription Factors
pubmed:year
2001
pubmed:articleTitle
Irx4 forms an inhibitory complex with the vitamin D and retinoic X receptors to regulate cardiac chamber-specific slow MyHC3 expression.
pubmed:affiliation
Department of Medicine, Stanford University School of Medicine, Stanford, California 94305-5151, USA.
pubmed:publicationType
Journal Article