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  • Gormand, AmelieLund University,Lunds universitet,Molekylär endokrinologi,Forskargrupper vid Lunds universitet,Molecular Endocrinology,Lund University Research Groups (författare)

Regulation of AMP-activated protein kinase by LKB1 and CaMKK in adipocytes.

  • Artikel/kapitelEngelska2011

Förlag, utgivningsår, omfång ...

  • 2011-04-01
  • Wiley,2011

Nummerbeteckningar

  • LIBRIS-ID:oai:lup.lub.lu.se:4e69ecd9-fb9f-4a72-b2c7-5868b4e06433
  • https://lup.lub.lu.se/record/1831942URI
  • https://doi.org/10.1002/jcb.23053DOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:art swepub-publicationtype
  • Ämneskategori:ref swepub-contenttype

Anmärkningar

  • AMP-activated protein kinase (AMPK) is a serine/threonine kinase that regulates cellular and whole body energy homeostasis. In adipose tissue, activation of AMPK has been demonstrated in response to a variety of extracellular stimuli. However, the upstream kinase that activates AMPK in adipocytes remains elusive. Previous studies have identified LKB1 as a major AMPK kinase in muscle, liver and other tissues. In certain cell types, Ca(2+) /Calmodulin-dependent protein kinase kinase (CaMKK) β has been shown to activate AMPK in response to increase of intracellular Ca(2+) levels. Our aim was to investigate if LKB1 and/or CaMKK function as AMPK kinases in adipocytes. We used adipose tissue and isolated adipocytes from mice in which the expression of LKB1 was reduced to 10-20% of that of wild-type (LKB1 hypomorphic mice). We show that adipocytes from LKB1 hypomorphic mice display a 40% decrease in basal AMPK activity and a decrease of AMPK activity in the presence of the AMPK activator phenformin. We also demonstrate that stimulation of 3T3L1 adipocytes with intracellular [Ca(2+) ]-raising agents results in an activation of the AMPK pathway. The inhibition of CaMKK isoforms, particularly CaMKKβ, by the inhibitor STO-609 or by siRNAs, blocked Ca(2+) -, but not phenformin-, AICAR or forskolin-induced activation of AMPK, indicating that CaMKK activated AMPK in response to Ca(2+) . Collectively, we show that LKB1 is required to maintain normal AMPK-signalling in non-stimulated adipocytes and in the presence of phenformin. In addition, we demonstrate the existence of a Ca(2+) /CaMKK signalling pathway that can also regulate the activity of AMPK in adipocytes. J. Cell. Biochem. © 2011 Wiley-Liss, Inc.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Henriksson, EmmaLund University,Lunds universitet,Proteinfosforylering,Forskargrupper vid Lunds universitet,Protein Phosphorylation,Lund University Research Groups(Swepub:lu)med-ehr (författare)
  • Ström, KristofferLund University,Lunds universitet,Molekylär endokrinologi,Forskargrupper vid Lunds universitet,Molecular Endocrinology,Lund University Research Groups(Swepub:lu)medk-kst (författare)
  • Jensen, Thomas Elbenhardt (författare)
  • Sakamoto, Kei (författare)
  • Göransson, OlgaLund University,Lunds universitet,Proteinfosforylering,Forskargrupper vid Lunds universitet,Signaltransduktionsforskning,Protein Phosphorylation,Lund University Research Groups,Insulin Signal Transduction(Swepub:lu)medk-ogo (författare)
  • Molekylär endokrinologiForskargrupper vid Lunds universitet (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Journal of Cellular Biochemistry: Wiley112, s. 1364-13750730-2312

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