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重组 N-甲基-D-天冬氨酸受体的钙依赖性失活具有 NR2 亚基特异性。

Calcium-dependent inactivation of recombinant N-methyl-D-aspartate receptors is NR2 subunit specific.

作者信息

Krupp J J, Vissel B, Heinemann S F, Westbrook G L

机构信息

Vollum Institute, Oregon Health Sciences University, Portland 97201, USA.

出版信息

Mol Pharmacol. 1996 Dec;50(6):1680-8.

PMID:8967993
Abstract

Intracellular Ca2+ can reversibly reduce the activity of native N-methyl-D-aspartate (NMDA) receptors in hippocampal neurons, a phenomenon termed Ca2+-dependent inactivation. We examined inactivation in heteromeric NMDA receptors expressed in human embryonic kidney (HEK) 293 cells using whole-cell recording. NR1-1a/2A heteromers showed reversible inactivation that was very similar to native NMDA receptors in cultured hippocampal neurons. Inactivation was dependent on the extracellular Ca2+ concentration and the degree of intracellular Ca2+ buffering. In 2 mM extracellular Ca2+, inactivation resulted in a 46.1 +/- 12.6% reduction in the whole-cell current during a 5-sec agonist application. Inactivation of NR1-1a/2A heteromers was unaffected by calcineurin inhibitors, staurosporine, or phalloidin. NR1-1a/2D heteromers also showed a similar degree of inactivation. In contrast, NR1-1a/2B and NR1-1a/2C heteromers showed no significant inactivation. At saturating concentrations of NMDA (1 mM), NR1-1a/2A heteromers also showed Ca- and glycine-independent desensitization, as seen in native hippocampal neurons. Ca(2+)- and glycine-independent desensitization was less pronounced in NR1-1a/2B heteromers and absent in NR1-1a/2C heteromers. Activation of NR1-1a/2C heteromers triggered intracellular Ca2+ transients similar to NR1-1a/2A heteromers as verified by combined Ca2+ imaging and whole-cell recording. Thus differences in Ca2+ permeability were not responsible for the lack of inactivation in NR1-1a/2C heteromers. Our results show that inactivation of recombinant NMDA receptors requires either the NR2A or NR2D subunit, whereas both inactivation and desensitization were absent in NR2C-containing receptors. The gating of inactivating NMDA receptors is more likely to be influenced by ongoing NMDA receptor activity and Ca2+ transients, perhaps consistent with the prominent expression of NR2A in hippocampus and cerebral cortex.

摘要

细胞内钙离子(Ca2+)可使海马神经元中天然N-甲基-D-天冬氨酸(NMDA)受体的活性发生可逆性降低,这一现象被称为Ca2+依赖性失活。我们采用全细胞记录法,研究了在人胚肾(HEK)293细胞中表达的异聚体NMDA受体的失活情况。NR1-1a/2A异聚体表现出可逆性失活,这与培养的海马神经元中的天然NMDA受体非常相似。失活取决于细胞外Ca2+浓度和细胞内Ca2+缓冲程度。在细胞外Ca2+浓度为2 mM时,在5秒的激动剂应用期间,失活导致全细胞电流降低了46.1±12.6%。NR1-1a/2A异聚体的失活不受钙调神经磷酸酶抑制剂、星形孢菌素或鬼笔环肽的影响。NR1-1a/2D异聚体也表现出相似程度的失活。相比之下,NR1-1a/2B和NR1-1a/2C异聚体未表现出明显的失活。在NMDA饱和浓度(1 mM)下,NR1-1a/2A异聚体也表现出与天然海马神经元中所见类似的Ca2+和甘氨酸非依赖性脱敏。Ca2+和甘氨酸非依赖性脱敏在NR1-1a/2B异聚体中不太明显,而在NR1-1a/2C异聚体中不存在。通过联合Ca2+成像和全细胞记录证实,NR1-1a/2C异聚体的激活引发的细胞内Ca2+瞬变与NR1-1a/2A异聚体相似。因此,Ca2+通透性的差异并非NR1-1a/2C异聚体缺乏失活的原因。我们的结果表明,重组NMDA受体的失活需要NR2A或NR2D亚基,而含NR2C的受体既不存在失活也不存在脱敏。失活性NMDA受体的门控更可能受到持续的NMDA受体活性和Ca2+瞬变的影响,这可能与NR2A在海马体和大脑皮层中的显著表达一致。

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