Linked Life Data

11916906

Source:http://linkedlifedata.com/resource/pubmed/id/11916906

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-3-27
pubmed:abstractText
Mutations of the hepatocyte nuclear factor-4alpha (HNF-4alpha) gene are associated with a subtype of maturity-onset diabetes of the young (MODY1) that is characterized by impaired insulin secretion in response to a glucose load. HNF-4alpha, which is a transcription factor expressed in pancreatic beta-cells, plays an important role in regulating the expression of genes involved in glucose metabolism. Thus, cofactors that interact with HNF-4alpha and modify its transcriptional activity might also play an important role in regulating the metabolic pathways in pancreatic beta-cells, and the genes of such cofactors are plausible candidate genes for MODY. In the present study, we showed, using a yeast two-hybrid screening assay, that thyroid hormone receptor interacting protein 3 (Trip3) interacted with HNF-4alpha, and their interaction was confirmed by the glutathione S-transferase pull-down assay. Human Trip3 cDNA contained an open reading frame for a protein of 155 amino acids, and the gene was expressed in both pancreatic islets and MIN6 cells. Cotransfection experiments indicated that Trip3 could enhance (two- to threefold) the transcription activity of HNF-4alpha in COS-7 cells and MIN6 cells. These results suggest that Trip3 is a coactivator of HNF-4alpha. Mutation screening revealed that variation of the Trip3 gene is not a common cause of MODY/early-onset type 2 diabetes in Japanese individuals. Trip3 may play an important role in glucose metabolism by regulating the transcription activity of HNF-4alpha.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0012-1797
pubmed:author
pubmed:issnType
Print
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
910-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11916906-Animals, pubmed-meshheading:11916906-Base Sequence, pubmed-meshheading:11916906-Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, pubmed-meshheading:11916906-COS Cells, pubmed-meshheading:11916906-Cercopithecus aethiops, pubmed-meshheading:11916906-Cloning, Molecular, pubmed-meshheading:11916906-DNA Primers, pubmed-meshheading:11916906-DNA-Binding Proteins, pubmed-meshheading:11916906-Hepatocyte Nuclear Factor 4, pubmed-meshheading:11916906-Humans, pubmed-meshheading:11916906-Islets of Langerhans, pubmed-meshheading:11916906-Liver, pubmed-meshheading:11916906-Phosphoproteins, pubmed-meshheading:11916906-Recombinant Fusion Proteins, pubmed-meshheading:11916906-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11916906-Transcription Factors, pubmed-meshheading:11916906-Transfection
pubmed:year
2002
pubmed:articleTitle
Thyroid hormone receptor interacting protein 3 (trip3) is a novel coactivator of hepatocyte nuclear factor-4alpha.
pubmed:affiliation
Department of Internal Medicine and Molecular Science, Graduate School of Medicine, Osaka University, Osaka, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't