his.sePublikasjoner
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
p110 alpha Hot Spot Mutations E545K and H1047R Exert Metabolic Reprogramming Independently of p110 alpha Kinase Activity
Wallenberg Laboratory, Department of Molecular and Clinical Medicine, University of Gothenburg, Sweden.
Wallenberg Laboratory, Department of Molecular and Clinical Medicine, University of Gothenburg, Sweden / Scientific Solutions, Stockholm, Sweden.
Wallenberg Laboratory, Department of Molecular and Clinical Medicine, University of Gothenburg, Sweden.
Department of Medical Chemistry and Cell Biology, University of Gothenburg, Sweden.
Vise andre og tillknytning
2015 (engelsk)Inngår i: Molecular and Cellular Biology, ISSN 0270-7306, Vol. 35, nr 19, s. 3258-3273Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The phosphatidylinositol-4,5-bisphosphate 3-kinase (PI3K) catalytic subunit p110α is the most frequently mutated kinase in human cancer, and the hot spot mutations E542K, E545K, and H1047R are the most common mutations in p110α. Very little is known about the metabolic consequences of the hot spot mutations of p110α in vivo. In this study, we used adenoviral gene transfer in mice to investigate the effects of the E545K and H1047R mutations on hepatic and whole-body glucose metabolism. We show that hepatic expression of these hot spot mutations results in rapid hepatic steatosis, paradoxically accompanied by increased glucose tolerance, and marked glycogen accumulation. In contrast, wild-type p110α expression does not lead to hepatic accumulation of lipids or glycogen despite similar degrees of upregulated glycolysis and expression of lipogenic genes. The reprogrammed metabolism of the E545K and H1047R p110α mutants was surprisingly not dependent on altered p110α lipid kinase activity.

sted, utgiver, år, opplag, sider
American Society for Microbiology , 2015. Vol. 35, nr 19, s. 3258-3273
HSV kategori
Forskningsprogram
Biomedicinsk genetik
Identifikatorer
URN: urn:nbn:se:his:diva-13592DOI: 10.1128/MCB.00471-15ISI: 000365391300001PubMedID: 26169833Scopus ID: 2-s2.0-84941052983OAI: oai:DiVA.org:his-13592DiVA, id: diva2:1098173
Tilgjengelig fra: 2017-05-23 Laget: 2017-05-23 Sist oppdatert: 2020-01-17bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstPubMedScopus

Personposter BETA

Ejeskär, Katarina

Søk i DiVA

Av forfatter/redaktør
Ejeskär, Katarina
Av organisasjonen

Søk utenfor DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 669 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf