Activation of a mouse in vitro neuromuscular synapse produces a reduction in synaptic efficacy which is greater for nonactivated than for activated inputs to the myotubes. This has been shown to require thrombin and thrombin receptor activation and to involve a protein kinase C (PKC)-mediated step.
Glutamate receptors localize postsynaptically at neuromuscular junctions in mice
β Scribed by Tessily A. Mays; Jamie L. Sanford; Toshihiko Hanada; Athar H. Chishti; Jill A. Rafael-Fortney
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 766 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0148-639X
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Dlg (Discs Large) is a multidomain protein that interacts with glutamate receptors and potassium channels at Drosophila neuromuscular junctions (NMJs) and at mammalian central nervous system synapses. Dlg also localizes postsynaptically at cholinergic mammalian NMJs. We show here that Ξ±βaminoβ3βhydroxyβ5βmethylisoxazoleβ4βproprionate (AMPA) receptor subunits, together with glutamate, are present at the mammalian NMJ. Both AMPA and NMDA (NβmethylβDβaspartate) glutamate receptor subunits display overlapping postsynaptic localization patterns with Dlg at all NMJs examined in normal mice. Kir2 potassium channels also localize with Dlg and glutamate receptors at this synapse. Localization of the components of a glutamatergic system suggests novel mechanisms at mammalian neuromuscular synapses. Muscle Nerve 39: 343β349, 2009
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