Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2002-5-6
pubmed:abstractText
The cAMP-response element-binding protein-binding protein (CBP) and p300 are common coactivators for several transcriptional factors. It has been reported that both CBP and p300 are significant for the activation of peroxisome proliferator-activated receptor gamma (PPARgamma), which is a crucial nuclear receptor in adipogenesis. However, it remains unclear whether CBP and/or p300 is physiologically essential to the activation of PPARgamma in adipocytes and adipocyte differentiation. In this study, we investigated the physiological significance of CBP/p300 in NIH3T3 cells transiently expressing PPARgamma and CBP and in 3T3-L1 preadipocytes stably expressing CBP- or p300-specific ribozymes. In PPARgamma-transfected NIH3T3 cells, induction of expression of PPARgamma target genes such as adipocyte fatty acid-binding protein (aP2) and lipoprotein lipase (LPL) by adding thiazolidinedione was enhanced, depending on the amount of a CBP expression plasmid transfected. Expression of aP2 and LPL genes, as well as glycerol-3-phosphate dehydrogenase activity and triacylglyceride accumulation after adipogenic induction, was largely suppressed in 3T3-L1 adipocytes expressing either the CBP- or p300-specific active ribozyme, but not in inactive ribozyme-expressing cells. These data suggest that both CBP and p300 are indispensable for the full activation of PPARgamma and adipocyte differentiation and that CBP and p300 do not mutually complement in the process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/CREB-Binding Protein, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Crebbp protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fabp5 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fabp7 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycerolphosphate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Catalytic, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides, http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP-associated factor
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16906-12
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11884404-3T3 Cells, pubmed-meshheading:11884404-Acetyltransferases, pubmed-meshheading:11884404-Adipocytes, pubmed-meshheading:11884404-Animals, pubmed-meshheading:11884404-CREB-Binding Protein, pubmed-meshheading:11884404-Carrier Proteins, pubmed-meshheading:11884404-Cell Cycle Proteins, pubmed-meshheading:11884404-Cell Differentiation, pubmed-meshheading:11884404-Cell Line, pubmed-meshheading:11884404-Dimerization, pubmed-meshheading:11884404-Dose-Response Relationship, Drug, pubmed-meshheading:11884404-Fatty Acid-Binding Proteins, pubmed-meshheading:11884404-Glycerolphosphate Dehydrogenase, pubmed-meshheading:11884404-Histone Acetyltransferases, pubmed-meshheading:11884404-Immunoblotting, pubmed-meshheading:11884404-Ligands, pubmed-meshheading:11884404-Lipoprotein Lipase, pubmed-meshheading:11884404-Mice, pubmed-meshheading:11884404-Neoplasm Proteins, pubmed-meshheading:11884404-Nerve Tissue Proteins, pubmed-meshheading:11884404-Nuclear Proteins, pubmed-meshheading:11884404-Plasmids, pubmed-meshheading:11884404-Protein Structure, Tertiary, pubmed-meshheading:11884404-RNA, Catalytic, pubmed-meshheading:11884404-RNA, Messenger, pubmed-meshheading:11884404-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:11884404-Recombinant Proteins, pubmed-meshheading:11884404-Time Factors, pubmed-meshheading:11884404-Trans-Activators, pubmed-meshheading:11884404-Transcription Factors, pubmed-meshheading:11884404-Transfection, pubmed-meshheading:11884404-Triglycerides, pubmed-meshheading:11884404-p300-CBP Transcription Factors
pubmed:year
2002
pubmed:articleTitle
Overexpression and ribozyme-mediated targeting of transcriptional coactivators CREB-binding protein and p300 revealed their indispensable roles in adipocyte differentiation through the regulation of peroxisome proliferator-activated receptor gamma.
pubmed:affiliation
Laboratory of Nutrition Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
pubmed:publicationType
Journal Article