شنبه 29 اردیبهشت 1403
دوره 9، شماره 4 - ( 7-1402 )
جلد 9 شماره 4 صفحات 267-259 |
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R Prabhu R. Phosphorylation Status of GluN2B-Ser1303 Under Glutamate-induced Excitotoxicity in Primary Cortical Neurons: An In Vitro Study. Caspian J Neurol Sci 2023; 9 (4) :259-267
URL: http://cjns.gums.ac.ir/article-1-668-fa.html
URL: http://cjns.gums.ac.ir/article-1-668-fa.html
Phosphorylation Status of GluN2B-Ser1303 Under Glutamate-induced Excitotoxicity in Primary Cortical Neurons: An In Vitro Study. مجله علوم اعصاب کاسپین. 1402; 9 (4) :259-267
چکیده: (380 مشاهده)
Background: Glutamate, an excitatory neurotransmitter, plays a pivotal role in cellular phenomena in neurons,
like synaptic plasticity and excitotoxicity. As the major glutamate receptors, N-methyl-D-aspartate receptors
(NMDARs) undergo phosphorylation at Ser1303 on the GluN2B subunit upon glutamate binding. This effect
results from the influx of calcium and subsequent activation of many known kinases that phosphorylate the
receptor. However, the regulation of this phosphorylation at this site and the involved phosphatases have
remained unknown, especially under excitotoxicity conditions induced by glutamate treatment.
Objectives: This study attempts to investigate the regulation of phosphorylation at GluN2B-Ser1303
under excitotoxic conditions and identify the phosphatase responsible.
Materials & Methods: Primary cortical neurons prepared from embryonic rat brains were treated
with glutamate, thereby inducing excitotoxicity in vitro. Then, the phosphorylation status of
GluN2B-Ser1303 was studied using western blots in the presence of various phosphatase inhibitors.
Finally, the interaction of phosphatase with GluN2B was studied using immunostaining and coimmunoprecipitation
analysis.
Results: The results show that under excitotoxic conditions, there is a reduction in the phosphorylation
of GluN2B-Ser1303, and protein phosphatase 1 (PP1) was the phosphatase responsible. PPI was
found to interact with the receptor.
Conclusion: This study reports for the first time the regulation of phosphorylation at GluN2BSer1303
in vitro under excitotoxic conditions, which PP1 mediates. This site could be a potential drug
target for designing novel compounds which could exacerbate excitotoxicity.
like synaptic plasticity and excitotoxicity. As the major glutamate receptors, N-methyl-D-aspartate receptors
(NMDARs) undergo phosphorylation at Ser1303 on the GluN2B subunit upon glutamate binding. This effect
results from the influx of calcium and subsequent activation of many known kinases that phosphorylate the
receptor. However, the regulation of this phosphorylation at this site and the involved phosphatases have
remained unknown, especially under excitotoxicity conditions induced by glutamate treatment.
Objectives: This study attempts to investigate the regulation of phosphorylation at GluN2B-Ser1303
under excitotoxic conditions and identify the phosphatase responsible.
Materials & Methods: Primary cortical neurons prepared from embryonic rat brains were treated
with glutamate, thereby inducing excitotoxicity in vitro. Then, the phosphorylation status of
GluN2B-Ser1303 was studied using western blots in the presence of various phosphatase inhibitors.
Finally, the interaction of phosphatase with GluN2B was studied using immunostaining and coimmunoprecipitation
analysis.
Results: The results show that under excitotoxic conditions, there is a reduction in the phosphorylation
of GluN2B-Ser1303, and protein phosphatase 1 (PP1) was the phosphatase responsible. PPI was
found to interact with the receptor.
Conclusion: This study reports for the first time the regulation of phosphorylation at GluN2BSer1303
in vitro under excitotoxic conditions, which PP1 mediates. This site could be a potential drug
target for designing novel compounds which could exacerbate excitotoxicity.
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