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Autocrine effects of visfatin on hepatocyte sensitivity to insulin action
V. Škop, K. Kontrová, V. Zídek, M. Pravenec, L. Kazdová, K. Mikulík, J. Sajdok, J. Zídková
Jazyk angličtina Země Česko
Grantová podpora
NR9387
MZ0
CEP - Centrální evidence projektů
NR9359
MZ0
CEP - Centrální evidence projektů
Digitální knihovna NLK
Plný text - Článek
Plný text - Část
Zdroj
Zdroj
Free Medical Journals od 1998
ProQuest Central od 2005-01-01
Medline Complete (EBSCOhost) od 2006-01-01
Nursing & Allied Health Database (ProQuest) od 2005-01-01
Health & Medicine (ProQuest) od 2005-01-01
ROAD: Directory of Open Access Scholarly Resources od 1998
- MeSH
- autokrinní signalizace MeSH
- biologický transport MeSH
- buněčné linie MeSH
- cytokiny genetika metabolismus MeSH
- financování organizované MeSH
- glukosa metabolismus MeSH
- hepatocyty enzymologie MeSH
- inzulin metabolismus MeSH
- inzulinová rezistence MeSH
- krysa rodu rattus MeSH
- messenger RNA metabolismus MeSH
- NAD metabolismus MeSH
- nikotinamidfosforibosyltransferasa genetika metabolismus MeSH
- potkani inbrední WKY MeSH
- regulace genové exprese enzymů MeSH
- RNA interference MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- zvířata MeSH
Visfatin was originally described as an adipokine with insulin mimetic effects. Recently, it was found that visfatin is identical with the Nampt (nicotinamide phosphoribosyltransferase) gene that codes for an intra- and extracellular NAD biosynthetic enzyme and is predominantly expressed outside the adipose tissue. In the current study, we found strong protein and mRNA expression of visfatin in rat heart, liver, kidney, and muscle, while the expression of visfatin in visceral fat was significantly lower and undetectable in subcutaneous fat. The insulin-mimetic effects of visfatin (extracellular form of Nampt or eNampt) are controversial and even less is known about autocrine effects of visfatin (intracellular form of Nampt or iNampt). Since liver plays a major role in glucose metabolism, we studied visfatin effects on insulin-stimulated cellular glucose uptake in Fao rat hepatocytes using RNA interference (RNAi). RNAi-mediated downregulation of visfatin expression in Fao cells was associated with significantly reduced NAD biosynthesis (0.3±0.01 vs. 0.5±0.01 mmol/h/g, P<0.05) and with significantly decreased incremental glucose uptake after stimulation with insulin when compared to controls with normal expression of visfatin (0.6±0.2 vs. 2.2±0.5 nnmol/g/2 h, P=0.02). These results provide evidence that visfatin exhibits important autocrine effects on sensitivity of liver cells to insulin action possibly through its effects on NAD biosynthesis.
Lit.: 11
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- $a Inst. Physiol., Acad. Sci. Czech Rep., Prague
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- $a Visfatin was originally described as an adipokine with insulin mimetic effects. Recently, it was found that visfatin is identical with the Nampt (nicotinamide phosphoribosyltransferase) gene that codes for an intra- and extracellular NAD biosynthetic enzyme and is predominantly expressed outside the adipose tissue. In the current study, we found strong protein and mRNA expression of visfatin in rat heart, liver, kidney, and muscle, while the expression of visfatin in visceral fat was significantly lower and undetectable in subcutaneous fat. The insulin-mimetic effects of visfatin (extracellular form of Nampt or eNampt) are controversial and even less is known about autocrine effects of visfatin (intracellular form of Nampt or iNampt). Since liver plays a major role in glucose metabolism, we studied visfatin effects on insulin-stimulated cellular glucose uptake in Fao rat hepatocytes using RNA interference (RNAi). RNAi-mediated downregulation of visfatin expression in Fao cells was associated with significantly reduced NAD biosynthesis (0.3±0.01 vs. 0.5±0.01 mmol/h/g, P<0.05) and with significantly decreased incremental glucose uptake after stimulation with insulin when compared to controls with normal expression of visfatin (0.6±0.2 vs. 2.2±0.5 nnmol/g/2 h, P=0.02). These results provide evidence that visfatin exhibits important autocrine effects on sensitivity of liver cells to insulin action possibly through its effects on NAD biosynthesis.
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