National Repository of Grey Literature 3 records found  Search took 0.00 seconds. 
The in vitro study of the new lipidized analogs of prolactin-releasing peptide
Šatrová, Lucie ; Maletínská, Lenka (advisor) ; Tichá, Anežka (referee)
Bakalářská práce se zabývá neuropeptidy ovlivňujícími příjem potravy anorexigenním účinkem (snižujícím příjem potravy), které jsou potenciálními Mezi tyto neuropeptidy se řadí peptid uvolňující prolaktin (PrRP), který se váže s itou ke svému receptoru GPR10, a také k afinitou jen o řád nižší než laboratoři RNDr. Lenky Maletínské, CSc. byly navrženy a syntetizovány nové lipidované analogy PrRP, které mají podobnou afini receptorům GPR10 i NPFF2 přirozený PrRP a snižují příjem potravy po periferním podání. Na základě skutečnosti, že GPR10 má vysoko jedním receptorem označovaným jako Y1 a receptor Y1 je homologický s dalšími íněných peptidů Y2 a Y5, byla této bakalářské práci stanovena afinita přirozeného a jeho dvou palmitovaných analogů k receptorům Na buňkách U2OS s transfekovanými pomocí saturačních vazeb . Ty sloužily k výpočtu kompetitivních vazebných experimentech, kde přirozený a jeho dva palmitoylované měly velmi nízkou buňkám U2OS s transfekovanými receptory Y1 nebo Y2. Na druhé straně přirozený PrRP vázal buňkám transfekovaným receptorem řádu 10 a jeho palmitoylované analogy s až stokrát nižší Součástí bakalářské práce byla i optimaliz a přítomnosti inhibitorů proteáz stanovení K buněčn sfekovaným NPFF2 Stanovená K řádu 10 mol/l podobná hodnotám pro přirozené ligandy receptorů Zkoumání vazby...
New analogues of prolactin-releasing peptide with prolonged effect on food intake
Tichá, Anežka ; Ryšlavá, Helena (advisor) ; Konvalinka, Jan (referee)
Prolactin-releasing peptide (PrRP) is a member of the family of RF-amide peptides. These peptides have typical C-terminal sequence -Arg-Phe-NH2 and similar biological effects. PrRP was discovered as an endogenous ligand of an orphan receptor GPR10 while searching for a factor responsible for a prolactin secretion. This effect was not later confirmed and nowadays, PrRP is mainly considered as an anorexigenic peptide. This is supported by a fact that PrRP and GPR10 deficient mice suffer from hyperphagia and late-onset obesity. Besides GPR10, PrRP is bound to NPFF2 receptor whose endogenous ligand is neuropeptide FF (NPFF). In this study, the PrRP's analogues modified at the N-terminus with fatty acids of different lenghts were tested in vitro on binding and activation MAPK/ERK1/2 signalling pathway. In in vivo experiments on food intake, the central anorexigenic effects of lipidized PrRP-analogues were tested provided their crossing blood brain barrier. Binding studies showed that all analogues bound to rat pituitary RC-4B/C cells with high affinity, analogues containing fatty acid with Ki of one order of magnitude lower than native PrRP. High affinity was also confirmed for binding to cells overexpressing GPR10 receptor and cell membranes with overexpressed NPFF2 receptor. All tested analogues...
Effects of PrRP (prolactin-releasing peptide) and NPFF (neuropeptide FF) analogs in vitro and in vivo
Tichá, Anežka ; Ryšlavá, Helena (advisor) ; Železná, Blanka (referee)
Prolactin-releasing peptide (PrRP) and neuropeptide FF (NPFF) belong to the RF-amide family. These peptides have identical C-terminal amino acid sequence (R-F-NH2) and similar biological activities. PrRP was identified as an endogenous ligand of an orphan receptor GPR10 able to stimulate PRL-secretion in vitro and in vivo, but soon it was discoverd that this is not the primary function of this peptide. PrRP is thought to be an anorexigenic peptide as PrRP and GPR10 are found in several parts of the brain responsible for food intake regulation and because both GPR10 and PrRP deficient mice suffer from hyperphagia and late-onset obesity. In this study, relationship between PrRP and NPFF was studied using both in vitro binding and sell signaling and in vivo food intake and analgesia test in mice. In vitro experiments showed that PrRP bound to rat pituitary RC-4B/C cells containing GPR10 receptor with high affinity and NPFF, its stable analog 1DMe and its antagonist RF9 up to 10-5 M concentration did not bind to GPR10. NPFF, 1DMe and PrRP were bound to cell membranes with transfected NPFF2 receptor with high affinity, but RF9 with low affinity in a range of 10-7 M, in contrast to published literature. In vivo experiments with fasted mice confirmed that centrally injected PrRP and NPFF significantly...

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