|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1-4
|
|
pubmed:dateCreated |
2008-9-4
|
|
pubmed:abstractText |
GLUT4, the main insulin-responsive glucose transporter, plays a critical role in maintaining systemic glucose homeostasis and is subject to complicated metabolic regulation. GLUT4 expression disorder might cause insulin resistance, and over-expression of GLUT4 has been confirmed to ameliorate diabetes. Here, we reported that farnesoid X receptor (FXR) and its agonist chenodeoxycholic acid (CDCA) could induce GLUT4 transcription in 3T3-L1 and HepG2 cells. Furthermore, CDCA could increase the GLUT4 protein amount in C57BL/6J mice sex-dependently. The following progressive 5'-deletion analysis and site-mutation investigation further suggested that FXR could induce GLUT4 expression through FXR response element (FXRE) in the GLUT4 promoter. EMSA and knock-down of retinoid X receptor (RXR) indicated that FXR binds to the GLUT4-FXRE as a monomer and RXR does not participate in the FXR stimulation of GLUT4 expression. In addition, we demonstrated that FXR does not interfere with insulin-induced GLUT4 translocation to plasma membrane. All these data thereby implied that FXR is a new transcription factor of GLUT4, further elucidating the potential role for FXR in glucose metabolism.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chenodeoxycholic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/PPAR gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/farnesoid X-activated receptor
|
|
pubmed:status |
MEDLINE
|
|
pubmed:issn |
1421-9778
|
|
pubmed:author |
|
|
pubmed:copyrightInfo |
Copyright 2008 S. Karger AG, Basel.
|
|
pubmed:issnType |
Electronic
|
|
pubmed:volume |
22
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1-14
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:18769028-3T3-L1 Cells,
pubmed-meshheading:18769028-Animals,
pubmed-meshheading:18769028-Base Sequence,
pubmed-meshheading:18769028-Binding Sites,
pubmed-meshheading:18769028-Cell Line, Tumor,
pubmed-meshheading:18769028-Cell Membrane,
pubmed-meshheading:18769028-Chenodeoxycholic Acid,
pubmed-meshheading:18769028-DNA-Binding Proteins,
pubmed-meshheading:18769028-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:18769028-Female,
pubmed-meshheading:18769028-Gene Expression Regulation,
pubmed-meshheading:18769028-Glucose Transporter Type 4,
pubmed-meshheading:18769028-Humans,
pubmed-meshheading:18769028-Insulin,
pubmed-meshheading:18769028-Male,
pubmed-meshheading:18769028-Mice,
pubmed-meshheading:18769028-Mice, Inbred C57BL,
pubmed-meshheading:18769028-Molecular Sequence Data,
pubmed-meshheading:18769028-PPAR gamma,
pubmed-meshheading:18769028-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:18769028-Protein Binding,
pubmed-meshheading:18769028-Protein Conformation,
pubmed-meshheading:18769028-Protein Transport,
pubmed-meshheading:18769028-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:18769028-Response Elements,
pubmed-meshheading:18769028-Retinoid X Receptors,
pubmed-meshheading:18769028-Sex Characteristics,
pubmed-meshheading:18769028-Transcription Factors
|
|
pubmed:year |
2008
|
|
pubmed:articleTitle |
Farnesoid X receptor induces GLUT4 expression through FXR response element in the GLUT4 promoter.
|
|
pubmed:affiliation |
Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, China.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
