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EN
Glutamate is the predominant excitatory neurotransmitter in the central nervous system (CNS) and glutamatergic transmission is critical for controlling neuronal activity. Glutamate is stored in synaptic vesicles and released upon stimulation. The homeostasis of glutamatergic system is maintained by a set of transporters present in plasma membrane and in the membrane of synaptic vesicles. The family of vesicular glutamate transporters in mammals is comprised of three highly homologous proteins: VGLUT1-3. The expression of particular VGLUTs is largely complementary with limited overlap and so far they are most specific markers for neurons that use glutamate as neurotransmitter. VGLUTs are regulated developmentally and determine functionally distinct populations of glutamatergic neurons. Controlling the activity of these proteins could potentially modulate the efficiency of excitatory neurotransmission. This review summarizes the recent knowledge concerning molecular and functional characteristic of vesicular glutamate transporters, their development, contribution to synaptic plasticity and their involvement in pathology of the nervous system.
EN
Synapsins are a family of proteins associated with synaptic vesicles that are widely used as markers of synaptic terminals. We decided to investigate synapsin I expression in the mouse primary somatosensory cortex (SI). Immunostaining experiments using a polyclonal antibody against C-terminal domain of synapsin Ia/b (anti-SynI-C) showed an unusual pattern in the SI cortex compared to other regions of the neocortex. The staining delineated the cells located in barrel hollows. The immunoreactive product was located on the perikarya and proximal dendrites of gabaergic neurons found in layer IV and VI of the SI cortex. Other anti-synapsin antibodies did not reveal this pattern within the SI cortex, although in the hippocampus all antibodies examined produced a similar pattern of immunostaining. Deglycosylation of sections resulted in complete loss of immunodecoration on the cell perikarya. We suggest that the anti-SynI-C recognizes a saccharide surface epitope, possibly an element of perineuronal nets that is specific for the primary somatosensory cortex.
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