Presenilin-1/γ-Secretase Controls Glutamate Release, Tyrosine Phosphorylation, and Surface Expression of N-Methyl-d-aspartate Receptor (NMDAR) Subunit GluN2B

التفاصيل البيبلوغرافية
العنوان: Presenilin-1/γ-Secretase Controls Glutamate Release, Tyrosine Phosphorylation, and Surface Expression of N-Methyl-d-aspartate Receptor (NMDAR) Subunit GluN2B
المؤلفون: Anastasios Georgakopoulos, Nikolaos K. Robakis, Jindong Xu, Zhao Xuan, Julien Bruban, Junichi Shioi, Gael Barthet
المصدر: Journal of Biological Chemistry. 288:30495-30501
بيانات النشر: Elsevier BV, 2013.
سنة النشر: 2013
مصطلحات موضوعية: Time Factors, Excitotoxicity, Nerve Tissue Proteins, medicine.disease_cause, Receptors, N-Methyl-D-Aspartate, Biochemistry, Mice, chemistry.chemical_compound, mental disorders, Presenilin-1, medicine, Animals, Glutamate reuptake, Phosphorylation, Neurotransmitter, Molecular Biology, Cells, Cultured, Cerebral Cortex, Mice, Knockout, Neurons, biology, Glutamate receptor, Spectrin, Molecular Bases of Disease, Tyrosine phosphorylation, Calpain, Cell Biology, Molecular biology, Gene Expression Regulation, nervous system, chemistry, biology.protein, Tyrosine, NMDA receptor, Amyloid Precursor Protein Secretases
الوصف: Abnormally high concentrations of extracellular glutamate in the brain may cause neuronal damage via excitotoxicity. Thus, tight regulation of glutamate release is critical to neuronal function and survival. Excitotoxicity is caused mainly by overactivation of the extrasynaptic NMDA receptor (NMDAR) and results in specific cellular changes, including calcium-induced activation of calpain proteases. Here, we report that presenilin-1 (PS1) null mouse cortical neuronal cultures have increased amounts of calpain-dependent spectrin breakdown products (SBDPs) compared with WT cultures. NMDAR antagonists blocked accumulation of SBDPs, suggesting abnormal activation of this receptor in PS1 null cultures. Importantly, an increase in SBDPs was detected in cultures of at least 7 days in vitro but not in younger cultures. Conditioned medium from PS1 null neuronal cultures at 8 days in vitro contained higher levels of glutamate than medium from WT cultures and stimulated production of SBDPs when added to WT cultures. Use of glutamate reuptake inhibitors indicated that accumulation of this neurotransmitter in the media of PS1 null cultures was due to increased rates of release. PS1 null neurons showed decreased cell surface expression and phosphorylation of the GluN2B subunit of NMDAR, indicating decreased amounts of extrasynaptic NMDAR in the absence of PS1. Inhibition of γ-secretase activity in WT neurons caused changes similar to those observed in PS1 null neurons. Together, these data indicate that the PS1/γ-secretase system regulates release of glutamate, tyrosine phosphorylation, and surface expression of GluN2B-containing NMDARs. Background: Presenilin-1/γ-secretase is critical to neuronal function. Results: Inhibition of presenilin-1/γ-secretase increases release of glutamate, stimulating NMDAR and calpain while decreasing phosphorylation and surface expression of neuronal GluN2B. Conclusion: Presenilin-1/γ-secretase regulates glutamate release, NMDAR-dependent calpain activity, and modification of GluN2B. Significance: This study reveals a role for γ-secretase in release of glutamate, a neurotransmitter central to neuronal function, and excitotoxicity, a stress important to neurodegeneration.
تدمد: 0021-9258
DOI: 10.1074/jbc.m113.499004
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9be4f6676702cd2832814839055696ed
https://doi.org/10.1074/jbc.m113.499004
Rights: OPEN
رقم الانضمام: edsair.doi.dedup.....9be4f6676702cd2832814839055696ed
قاعدة البيانات: OpenAIRE
الوصف
تدمد:00219258
DOI:10.1074/jbc.m113.499004