VSE knjižnice (vzajemna bibliografsko-kataložna baza podatkov COBIB.SI)
  • C-terminal peptide of ▫$[gama]$▫-enolase impairs amyloid-ß-induced apoptosis through p75$▫^{NTR}▫$ signaling
    Pišlar, Anja ; Kos, Janko, 1959-
    [Gama]-enolase acts as a neurotrophic-like factor promoting growth, differentiation, survival and regeneration of neurons. It is shown in this study to exert a protective effect against ... amyloid-ß-peptide (Aß)-induced neurotoxicity in rat pheochromocytoma PC12 cells. Aß-induced toxicity was abolished in the presence of the active C-terminal peptide of Ž-enolase ([gama]-Eno) as measured by cell viability, lactate dehydrogenase release, sub G-1cell population, intracellular reactive oxygen species, mitochondrial functions and apoptotic morphology. [gama]-eno caused downregulation of the pro-apoptotic protein Bax and upregulation of the anti-apoptotic protein Bcl-2, as well as reduced caspase-3 activation. Exposure to Aß increased surface expression of p75 neurotrophin receptor (p75NTR), and the increase was abolished in the presence of [gama]-eno peptide. Further, pretreatment with [gama]-eno suppressed the activation of mitogen-activated protein kinases p38 and Jun-N-terminal kinase, which are p75NTR downstream effectors in apoptotic signaling. Moreover, AŽ triggered Ž-enolase co-immunoprecipitation with p75NTR as well as their strong association in the perimembrane region as shown by confocal microscopy, which further supports the interaction between these two proteins in cells insulted by Aß peptide. Our results indicate the possible use of [gama]-enolase C-terminal peptide for treating or preventing Alzheimer's disease.
    Vir: Neuromolecular medicine. - ISSN 1535-1084 (Vol. 15, iss. 3, 2013, str. 623-635)
    Vrsta gradiva - članek, sestavni del
    Leto - 2013
    Jezik - angleški
    COBISS.SI-ID - 3492209

    Povezava(-e):

    http://link.springer.com/article/10.1007%2Fs12017-013-8247-9
    DOI

vir: Neuromolecular medicine. - ISSN 1535-1084 (Vol. 15, iss. 3, 2013, str. 623-635)
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