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Univerzitetna knjižnica Maribor (UKM)
Knjižnica je med tednom odprta od 8. do 19. ure, ob sobotah od 9. do 13. ure. Čitalnica ČUK je odprta od ponedeljka do sobote od 12. do 24. ure, ob nedeljah od 18. do 24. ure. Informacije: 02 25 07 431, ukm@um.si
  • Studies of Munc18 Proteins Mediating Insulin Exocytosis
    Mandic, SA ...
    Our aim is to identify novel Cyclin-dependent kinase 5, Cdk5, phosphorylation substrates by which Cdk5 together with its activators p35 or p39 promotes insulin exocytosis. Currently we are focusing ... on the Sec1/Munc18 (SM) protein family that appears to be essential for both membrane trafficking and insulin exocytosis in pancreatic â-cells. RT-PCR and semi-quantitative RT-PCR demonstrated that both splice variants of Munc18-1, Munc18-1a and Munc18-1b, as well as Munc18-2 are expressed in mouse â-cells. Glucose stimulation of MIN6 cells recruited cytosolic wt Munc18-1 protein to the plasma membrane where as Munc18-2 protein remained in soluble fractions. During unstimulated conditions, phosphorylation mutants of Munc18-1 sequestered in the plasma membrane, differently from the wt Munc18-1 protein. Transient overexpression of wt Munc18-1 or wt Munc18-2 into INS-1E cells resulted in increased glucose-stimulated secretion, as measured with the human growth hormone (hGH) assay. Thus, our results suggest that different Munc18 proteins localize to different cellular compartments in â-cells, phosphorylation of the Munc18 proteins regulate their subcellular distribution and transient overexpression of both wt Munc18-1 or wt Munc18-2 protein augments glucose-stimulated secretion.
    Vir: Pancreatic beta-cell: birth, life and death [[Elektronski vir]] : 3-4 December 2007 King's College London School of Medicine, St Thomas' Hospital Campus, London, UK : poster abstracts (Str. [20])
    Vrsta gradiva - prispevek na konferenci
    Leto - 2007
    Jezik - angleški
    COBISS.SI-ID - 66519297

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