Despite the known importance of the endoplasmic reticulum (ER) in protein synthesis and vesicular transport, it is not clear whether neuropeptide and neuromodulator oxytocin can directly affect components of the ER in neuronal cells. Therefore, in the present study, we hypothesize that incubation of hippocampal neuronal cells in a presence of oxytocin 1) plays a role in the regulation of the expression of selected ER chaperone components and molecules involved in unfolded protein response pathway 2) affects distribution of the intracellular fluorescence signal highly selective for the ER. We found that oxytocin (1 μM) after 60 min significantly decreased the gene expression of oxidoreductase Ero1β, chaperone glucose-regulated proteins (Grp) 78 and Grp94. A significant decrease in GRP78 protein levels in response to oxytocin treatment occurred after 30, 60 and 120 min. We also observed a time-dependent increase in calreticulin protein levels with a statistically significant increase observed after 360 min. We found that the dynamics of the ER network changes significantly within 2 h of incubation under the influence of oxytocin. In conclusion we have shown that ER chaperones, oxidoreductases and trafficking molecules in neuronal cells are changing in response to oxytocin treatment in a short-term scenario potentially relevant for growth of dendrites and axons.
Keywords: Chaperone proteins; Endoplasmic reticulum; Neuron; Oxytocin.
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