Background Protein kinase C (PKC) regulates a variety of neural functions including neurotransmitter release. synaptic inputs to the skeletal muscle mass significantly increased the amount of nPKCε isoform as well as its phosphorylated form in the synaptic membrane and muscle mass contraction is necessary for these nPKCε expression changes. The results also demonstrate that synaptic activity-induced muscle mass contraction promotes changes in presynaptic nPKCε through the brain-derived neurotrophic factor (BDNF)-mediated tyrosine Tenapanor kinase receptor B (TrkB) signaling. Moreover nPKCε activity results in phosphorylation of the substrate MARCKS involved in actin cytoskeleton remodeling and related with neurotransmission. Finally blocking nPKCε with a nPKCε-specific translocation inhibitor peptide (εV1-2) strongly reduces phorbol ester-induced ACh release potentiation which further indicates Tenapanor that nPKCε is usually involved in neurotransmission. Conclusions Together these results provide a mechanistic insight into how synaptic activity-induced muscle mass contraction could regulate the presynaptic Rabbit polyclonal to EPHA4. action of the nPKCε isoform and suggest that muscle mass contraction is an important regulatory step in TrkB signaling at the NMJ. test or test (Mann-Whitney) and the normality of the distributions was tested with the Kolmogorov-Smirnov test. The criterion for statistical significance was p?