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rdf:type |
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lifeskim:mentions |
umls-concept:C0018787,
umls-concept:C0021641,
umls-concept:C0033640,
umls-concept:C0049700,
umls-concept:C0164786,
umls-concept:C0285558,
umls-concept:C0812228,
umls-concept:C1546857,
umls-concept:C1705328,
umls-concept:C1705341,
umls-concept:C1822702,
umls-concept:C1879547
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pubmed:issue |
2
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pubmed:dateCreated |
2010-9-29
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pubmed:abstractText |
On the basis of transfection experiments using a dominant-negative approach, our previous studies suggested that PKB (protein kinase B) was not involved in heart PFK-2 (6-phosphofructo2-kinase) activation by insulin. Therefore we first tested whether SGK3 (serum- and glucocorticoid-induced protein kinase 3) might be involved in this effect. Treatment of recombinant heart PFK-2 with [?-32P]ATP and SGK3 in vitro led to PFK-2 activation and phosphorylation at Ser466 and Ser483. However, in HEK-293T cells [HEK (human embryonic kidney)-293 cells expressing the large T-antigen of SV40 (simian virus 40)] co-transfected with SGK3 siRNA (small interfering RNA) and heart PFK-2, insulin-induced heart PFK-2 activation was unaffected. The involvement of PKB in heart PFK-2 activation by insulin was re-evaluated using different models: (i) hearts from transgenic mice with a muscle/heart-specific mutation in the PDK1 (phosphoinositide-dependent protein kinase 1)-substrate-docking site injected with insulin; (ii) hearts from PKB?-deficient mice injected with insulin; (iii) freshly isolated rat cardiomyocytes and perfused hearts treated with the selective Akti-1/2 PKB inhibitor prior to insulin treatment; and (iv) HEK-293T cells co-transfected with heart PFK-2, and PKB?/? siRNA or PKB? siRNA, incubated with insulin. Together, the results indicated that SGK3 is not required for insulin-induced PFK-2 activation and that this effect is likely mediated by PKB?.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1470-8728
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pubmed:author |
pubmed-author:BertrandLucL,
pubmed-author:DequiedtFranckF,
pubmed-author:GueuningMarie-AgnèsMA,
pubmed-author:HavauxXavierX,
pubmed-author:HemmingsBrian ABA,
pubmed-author:HueLouisL,
pubmed-author:MaisinLilianeL,
pubmed-author:MoutonVéroniqueV,
pubmed-author:RiderMark HMH,
pubmed-author:Sanchez-CanedoCossetteC,
pubmed-author:ToussaintLouiseL,
pubmed-author:VertommenDidierD
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
431
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
267-75
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:20687898-Animals,
pubmed-meshheading:20687898-Binding Sites,
pubmed-meshheading:20687898-Cattle,
pubmed-meshheading:20687898-Cell Line,
pubmed-meshheading:20687898-Enzyme Activation,
pubmed-meshheading:20687898-Humans,
pubmed-meshheading:20687898-Insulin,
pubmed-meshheading:20687898-Male,
pubmed-meshheading:20687898-Mice,
pubmed-meshheading:20687898-Mice, Transgenic,
pubmed-meshheading:20687898-Mutation,
pubmed-meshheading:20687898-Myocardium,
pubmed-meshheading:20687898-Myocytes, Cardiac,
pubmed-meshheading:20687898-Organ Specificity,
pubmed-meshheading:20687898-Phosphofructokinase-2,
pubmed-meshheading:20687898-Protein Kinase Inhibitors,
pubmed-meshheading:20687898-Protein-Serine-Threonine Kinases,
pubmed-meshheading:20687898-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:20687898-Rats,
pubmed-meshheading:20687898-Rats, Wistar,
pubmed-meshheading:20687898-Substrate Specificity
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pubmed:year |
2010
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pubmed:articleTitle |
Heart 6-phosphofructo-2-kinase activation by insulin requires PKB (protein kinase B), but not SGK3 (serum- and glucocorticoid-induced protein kinase 3).
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pubmed:affiliation |
Université catholique de Louvain and de Duve Institute, 75 Avenue Hippocrate, Brussels, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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