rdf:type |
|
lifeskim:mentions |
umls-concept:C0109317,
umls-concept:C0166417,
umls-concept:C0243192,
umls-concept:C0728938,
umls-concept:C0752312,
umls-concept:C1150579,
umls-concept:C1159884,
umls-concept:C1333340,
umls-concept:C1366882,
umls-concept:C1370600,
umls-concept:C1705767,
umls-concept:C1705791,
umls-concept:C1879547,
umls-concept:C2604987
|
pubmed:issue |
10
|
pubmed:dateCreated |
2009-7-14
|
pubmed:abstractText |
Indenone KR-62776 acts as an agonist of PPAR gamma without inducing obesity in animal models and cells. X-ray crystallography reveals that the indenone occupies the binding pocket in a different manner than rosiglitazone. 2-Dimensional gel-electrophoresis showed that the expression of 42 proteins was altered more than 2.0-fold between KR-62776- or rosiglitazone-treated adipocyte cells and control cells. Rosiglitazone down-regulated the expression of ERK1/2 and suppressed the phosphorylation of ERK1/2 in these cells. However, the expression of ERK1/2 was up-regulated in KR-62776-treated cells. Phosphorylated ERK1/2, activated by indenone, affects the localization of PPAR gamma, suggesting a mechanism for indenone-inhibition of adipogenesis in 3T3-L1 preadipocyte cells. The preadipocyte cells are treated with ERK1/2 inhibitor PD98059, a large amount of the cells are converted to adipocyte cells. These results support the conclusion that the localization of PPAR gamma is one of the key factors explaining the biological responses of the ligands.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
1420-9071
|
pubmed:author |
pubmed-author:CHUS USU,
pubmed-author:CIDJ MJM,
pubmed-author:CheonH GHG,
pubmed-author:ECKH WHW,
pubmed-author:HongS HSH,
pubmed-author:JungS-KSK,
pubmed-author:KimS JSJ,
pubmed-author:KitSS,
pubmed-author:KwonB-MBM,
pubmed-author:LeeJ WJW,
pubmed-author:LeeS YSY,
pubmed-author:WonJ SJS,
pubmed-author:YoonK SKS
|
pubmed:issnType |
Electronic
|
pubmed:volume |
66
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1766-81
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:19347570-3T3-L1 Cells,
pubmed-meshheading:19347570-Adipocytes,
pubmed-meshheading:19347570-Animals,
pubmed-meshheading:19347570-Cell Differentiation,
pubmed-meshheading:19347570-Crystallography, X-Ray,
pubmed-meshheading:19347570-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:19347570-Gene Expression Regulation,
pubmed-meshheading:19347570-Indans,
pubmed-meshheading:19347570-Mice,
pubmed-meshheading:19347570-Models, Molecular,
pubmed-meshheading:19347570-Molecular Structure,
pubmed-meshheading:19347570-Oximes,
pubmed-meshheading:19347570-PPAR gamma,
pubmed-meshheading:19347570-Protein Binding,
pubmed-meshheading:19347570-Protein Structure, Tertiary,
pubmed-meshheading:19347570-Proteome,
pubmed-meshheading:19347570-Thiazolidinediones
|
pubmed:year |
2009
|
pubmed:articleTitle |
PPAR gamma partial agonist, KR-62776, inhibits adipocyte differentiation via activation of ERK.
|
pubmed:affiliation |
Laboratory of Chemical Biology and Genomics, Korea Research Institute of Bioscience and Biotechnology, University of Science and Technology in Korea, 52 Uendong Yoosung, Daejon, 305-600, Korea.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|