谷氨酸受体相互作用蛋白介导AMPA受体兴奋性毒性效应
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摘要
脑卒中是一类常见致死性与致残性疾病，卒中发生时由于脑缺血导致兴奋性谷氨酸递质的大量释放入细胞外间隙，激活离子型谷氨酸受体引发钙内流、兴奋性毒性损伤与易损区神经元丢失是过去二十多年来的研究成果。但至今尚不清楚不同类型钙透性谷氨酸受体在引发神经元丢失的特异性作用以及为什么脑中有些区域如海马CA1锥体细胞、纹状体棘细胞与皮质投射神经元对谷氨酸兴奋性毒性损伤异常敏感。中枢神经系统（CNS）内离子型谷氨酸受体激活引发离子快速内流在介导快速突触传递、突触可塑性改变以及学习与记忆中其重要作用，但在病理状态下如缺氧、缺血，谷氨酸受体过渡激活会导致过多的钙、钠、锌离子内流就会导致神经兴奋性毒性损伤。CNS内离子型谷氨酸受体主要分三类即N-甲基-D-天门冬氨酸（NMDA）受体、α-氨基羟甲基恶唑丙酸（AMPA）受体、海人藻酸（KA）受体。因为所有NMDA受体均透过钙，起初的缺血损伤研究多集中于对该类受体的研究，然而近来已经有越来越多的研究指向钙透型AMPA受体，AMPA受体是一类由GluR1~4亚基以不同聚合形式形成的异源聚体，缺乏GluR2亚基的AMPA受体是透钙与锌离子的，GluR2亚基由于第二次跨膜区存在精氨酸可以阻滞含该亚基的AMPA受体通过钙离子，编码GluR2的基因组DNA是无此密码子的，只是在前mRNA水平在神经元内一种腺嘌呤脱氨酶的作用下，将原编码谷氨酸CAG中的A转化为I导致编码精氨酸，正常状态下脑内几乎100%的GluR2均是经过此加工的，因此绝大多数含GluR2的AMPA受体是不透钙的。以前的研究发现脑缺血可特异性导致CA1区GluR2mRNA与蛋白表达降低，由此形成了“脑缺血GluR2损伤假说”，认为缺血状态下由于GluR2表达降低导致GluR2缺失型AMPA受体生成增多，导致钙透性AMPA受体的增多，从而引发神经元的兴奋性毒性损伤。但该学说有许多未解之谜，如通过CA1区单细胞RT-PCR结合单细胞电生理研究脑缺血并未引发CA1神经元膜上AMPA受体水平与GluR2数目明显降低，Peng等人研究发现只是由于脑缺血引起神经元内2型腺嘌呤脱氨酶酶活性降低，导致非编辑状态GluR2的大量出现，从而导致了钙透性AMPA受体的增多，在CA1区的锥体细胞中GluR2在脑缺血状态下的编辑状态的GluR2在7~98%之间，以前的发现是由于研究者所采用的CA1整体区域细胞的异源性造成的，非编辑状态的GluR2有利于在组成AMPA受体时形成GluR1、GluR2、GluR3同源多聚体，从而形成的AMPA受体都是致钙透性的。
神经细胞内合成的GluR2/3在合成后的膜向转运与树突定向转运依赖一类谷氨酸受体相互作用蛋白即GRIP1（glutamate receptor-interactingprotein GRIP1），及GRIP2（ABP-L）、激酶C反应蛋白（protein interacting withC kinase1, PICK1）等。GRIP1与GRIP2都各有7个PDZ结构域，PDZ结构域在受体的定位、分布及功能上有重要的作用。同样GRIP1与GRIP2能与驱动蛋白（Kinesin）结合，调节神经元树突的物质运输。由于GRIP1与GRIP2不仅能与Kinesin结合影响受体的合成运输，并能与AMPA受体结合调节受体的分布与功能，所以在神经损伤过程当中，GRIP1与GRIP2可能起着重要的作用，搞清楚在损伤过程中GRIP1与GRIP2的功能变化及作用机制，有可能为寻找相应的损伤拮抗剂并及早抑制神经损伤的进一步发展提供可靠的科学依据，具有较高的临床治疗意义。
本研究采用光化学法复制成年大鼠局灶性脑梗塞模型，根据缺血缺氧性脑损伤后的不同时间点将大鼠分为5个组，首先采用免疫组织化学的方法，分别用抗GRIP1与GRIP2抗体对缺血灶局部进行了免疫标记，分析脑缺血后不同时间点缺血半暗带区内两者的表达特征。研究发现：在大鼠脑缺血损伤发生后，损伤灶周围有不同程度的坏死出现，在缺血半暗带区出现GRIP1及GRIP2的阳性标记细胞与神经纤维，损伤后6h和1d组的阳性标记较多，并且紧紧相随于坏死组织前沿，表明在损伤发生后GRIP1与GRIP2表达增强，GRIPs可能参与了脑缺血损伤过程。由于AMPA受体在神经兴奋毒性中的作用以及GRIPs对AMPA受体亚基GluR2与GluR3的调控作用，我们进一步研究了缺血损伤发生后GRIP1、GRIP2与AMPA受体亚基GluR2、GluR3的关系。通过免疫组织化学双标记技术研究，证实了AMPA受体亚基GluR2、GluR3与GRIP1、GRIP2在神经元存在双标记，有明显的共存现象，共存多出现在损伤后6h和1d。进而我们通过蛋白免疫印迹技术对缺血区GRIP1蛋白表达水平与GluR2/3在细胞膜与细胞浆的分布状态进行了研究，研究发现脑缺血导致的GRIP1升高时程与GluR2/3在细胞膜上的含量变化非常吻合，当GRIP1在缺血后6h~12h达最高水平时，GluR2/3在细胞膜上的含量也达最高，表明GRIPs的表达升高可能是致使GluR2/3在胞膜上分布升高的原因。同时我们第一次发现了脑缺血能诱导GRIP1、GRIP2在大脑少突胶质细胞上的表达。这些结果均表明GRIP1、GRIP2在缺血缺氧性脑损伤过程中可能扮演重要角色。
Stroke, because of occlusion or rupture of an artery, is a leading cause ofdeath or infirmity in developed countries. As stroke, lack of blood flow to thebrain (ischemia) results in excessive release of the neurotransmitter glutamateinto the extracellular space. For over two decades, it has been known that theglutamate release activates ionotropic glutamate receptors, causing calciumentry, excitotoxicity, and neuronal death in vulnerable brain regions. Manyaspects are remained yet including the specific role of different types of Ca2+-permeable glutamate receptor in precipitating cell death and why neurons insome regions of the brain,such as hippocampal CA1 pyramidal neurons, striatalspiny neurons, and cortical projection neurons, are more vulnerable to glutamatemediated excitotoxicity. In the central nervous system (CNS), activation ofionotropic glutamate receptors allows a rapid influx of ions across the neuronalmembrane, mediating fast excitatory synaptic transmission. Ionotropicglutamate receptors are also critical for synaptic plasticity , learning andmemory. However, excessive activation of glutamate receptors in pathologicalconditions, such as anoxia or ischemia, precipitates excitotoxic neuronal death in vulnerable neuronal types by allowing an excessive influx of Ca2+, Na+, andZn2+ into neurons. There are three main classes of ionotropic glutamate receptor:NMDA, AMPA, and kainate receptors. Because all NMDA receptors arepermeable to calcium, it is focused on the role of these receptors in ischemicinjury in early studies. More recently, however, the hotspot is gradually shiftedto a critical role played by Ca2+-permeable AMPA receptors. AMPA receptors(AMPARs) are heteromeric assemblies of subunits GluR1– GluR4. AMPARslacking GluR2 subunits are permeable to Ca2+ and Zn2+. Ca2+-impermeability inGluR2-containing receptors is specified by the presence of an arginine (R)residue present in transmembrane domain 2 of this subunit instead of theglutamine residue (Q) in the GluR1, GluR3, and GluR4 subunits. Although thevast majority of GluR2 subunits in the brain contain arginine at this site, thisphenotype is not encoded at the genomic level but is the result of RNA editingof the GluR2 pre-mRNA in the nucleus by the enzyme adenosine deaminase 2(ADAR2), which catalyzes site-selective deamination of adenosine in thegenomic glutamine codon (CAG) to an inosine, giving an arginine codon (CIG)in the mRNA. This position is nearly 100% edited in the brain, so the vastmajority of GluR2-containing AMPARs in the CNS containing GluR2(R) areCa2+-impermeable. In addition, Q/R editing also influences subunit assembly,membrane trafficking, and synaptic targeting of GluR2-containing receptors.The observation that GluR2 expression is specifically attenuated in vulnerableCA1 pyramidal neurons after transient ischemia led to the‘‘GluR2 hypothesis,’’which proposed that decreased availability of Ca2+-impermeable GluR2(R)protein after a neurological insult would result in augmented formation of Ca2+-permeable AMPARs and consequently increased neurotoxic Ca2+ (and possiblyZn2+) influx. Remaining more controversial are the molecular mechanisms that underlie the postischemic downregulation of GluR2(R) protein and, the role ofGluR2 Q/R editing in this process. Peng promoted further understanding ofthe mechanisms that increase AMPAR Ca2+ permeability in vulnerable CA1hippocampal cells after transient forebrain ischemia. By combination ofelectrophysiology and single-cell RT-PCR, the authors correlated GluR2 Q/Rediting efficiency with the Ca2+ permeability of AMPARs in single neuron.Postischemic CA1 pyramidal cells exhibited high levels of heterogeneity in Q/Rediting (7%–98%) compared with sham controls and other less-vulnerablehippocampal cell types (CA3 pyramidal or dentate granule cells), which allexhibited over 95% editing efficiency, suggesting that GluR2Q/R editing inCA1 pyramidal neurons is particularly vulnerable to ischemic insult.Importantly, the impaired GluR2 Q/R editing correlated closely with the Ca2+-permeability of AMPAR channels (assessed from the reversal potential of theAMPAR current) in these cells.Failure to detect alterations in levels of GluR2protein, GluR2 Q/R editing in ischemia in early research may reflect the use ofwhole hippocampal tissue rather than RNA derived from singleelectrophysiologicallycharacterised cells.The postischemic reduction inADAR2-dependent GluR2 Q/R editing results in accumulation of uneditedGluR2 pre-mRNA in the nucleus, which downregulates both GluR2 mRNA andprotein levels, while the remaining GluR2(Q) proteinis preferentially assembledto produce Ca2+-permeable AMPARs that are exported to synapses. Furtherinvestigaton is needed to address these differences.
The AMPA receptor subunits GluR2/3 can bind specifically to a kind ofPDZ proteins, termed as glutamate receptor-interacting protein (GRIP), AMPAreceptor-binding protein (ABP), and protein interacting with C kinase 1 (PICK1).Both GRIP1 and GRIP2 contain seven PDZ domains without other recognizable motif, ABP resembles GRIP in primary sequence; it differs from GRIP mostnotably in lacking the C-terminal seventh PDZ domain. GRIP1 also binds akinesin that functions in transport of dendritic vesicles along microtubules indendrites, showing that the scaffolding protein determines the direction oftransport .When the kinesin was bound to a member of the JIP group of scaffoldproteins, JSAP, it moved toward the axon, while when it was bound to GRIP1, itmoved toward the dendrite.GRIP1 can directly interact and steer kinesin heavychains to dendrites of neurons as a motor for AMPA receptors.So GRIP1 andGRIP2 may play important role on exporting GluR2/3 to synapses during anoxiaand ischemia.To clarify the mechanisms of the GRIP1 and GRIP2 for exportingGluR2/3 to synapses during anoxia and ischemia will facilitate to find effectiveantagonist to anoxia and ischemia.
In this study, focal cerebral infarction model of adult rat were establishedbased on the principle of photochemical initiation of thrombosis, the rats weredivided into 5 groups according to the timecourse after cerebral local ischemia.Anti GRIP1 and GRIP2 antibodies were used via immunohistochemistry toanalysis the differences between the normal and the injury cerebral and thedifferences among every time point after ischemia.The results show that necrosishappened around the focus of injury region.And we can also find the GRIP1 andGRIP2 labeled neurons and immunoreactive nerve fibers in the ischemicpenumbra. Neurons in the cerebral of 6h and 1d groups are more heavily labeledthan others, cells labeled by GRIP1 and GRIP2 antibodys were coincide with theischemic penumbra. It suggests that the expression of GRIP1 and GRIP2increased after irradiation, GRIPs may be play a role on the mechanisms ofischemia injury. Because of the excitotoxicity of AMPA receptors and theinteraction between GRIP1/2 and AMPA receptors, the relationship between GRIP1/2 and AMPA receptors was further investigated next. Double-labelimmunocytochemistry was used demonstrating that the GluR2、GluR3 werecolocalized with GRIP1/2 in cerebral neuron, specially in the ischemicpenumbra and V pyramidal cells, and the colocalization happeded more at 6h and1d after the irradiation. Furthermore, using Western blotting, we study therelationship the levels of GRIP1 in ischemic penumbra and the levels ofmembrane GluR2/3, we found that the elevated levels of GRIP1 was coincidewith the accumulating of GluR2/3 after rat brain ischemia.When the levels ofGRIP1 were highest during 6h~12h after rat brain ischemia, the levels ofmembrane GluR2/3 reached the highest level suggesting that the accumulatingof membrane GluR2/3 may be induced by GRIPs. We demonstrated for the firsttime that ischemia can induce the expression of GRIP1 and GRIP2 on theoligendendrocytes in corpus callosum implying an important role of GRIP1 andGRIP2 in brain ischemia.
神经细胞内合成的GluR2/3在合成后的膜向转运与树突定向转运依赖一类谷氨酸受体相互作用蛋白即GRIP1（glutamate receptor-interactingprotein GRIP1），及GRIP2（ABP-L）、激酶C反应蛋白（protein interacting withC kinase1, PICK1）等。GRIP1与GRIP2都各有7个PDZ结构域，PDZ结构域在受体的定位、分布及功能上有重要的作用。同样GRIP1与GRIP2能与驱动蛋白（Kinesin）结合，调节神经元树突的物质运输。由于GRIP1与GRIP2不仅能与Kinesin结合影响受体的合成运输，并能与AMPA受体结合调节受体的分布与功能，所以在神经损伤过程当中，GRIP1与GRIP2可能起着重要的作用，搞清楚在损伤过程中GRIP1与GRIP2的功能变化及作用机制，有可能为寻找相应的损伤拮抗剂并及早抑制神经损伤的进一步发展提供可靠的科学依据，具有较高的临床治疗意义。
本研究采用光化学法复制成年大鼠局灶性脑梗塞模型，根据缺血缺氧性脑损伤后的不同时间点将大鼠分为5个组，首先采用免疫组织化学的方法，分别用抗GRIP1与GRIP2抗体对缺血灶局部进行了免疫标记，分析脑缺血后不同时间点缺血半暗带区内两者的表达特征。研究发现：在大鼠脑缺血损伤发生后，损伤灶周围有不同程度的坏死出现，在缺血半暗带区出现GRIP1及GRIP2的阳性标记细胞与神经纤维，损伤后6h和1d组的阳性标记较多，并且紧紧相随于坏死组织前沿，表明在损伤发生后GRIP1与GRIP2表达增强，GRIPs可能参与了脑缺血损伤过程。由于AMPA受体在神经兴奋毒性中的作用以及GRIPs对AMPA受体亚基GluR2与GluR3的调控作用，我们进一步研究了缺血损伤发生后GRIP1、GRIP2与AMPA受体亚基GluR2、GluR3的关系。通过免疫组织化学双标记技术研究，证实了AMPA受体亚基GluR2、GluR3与GRIP1、GRIP2在神经元存在双标记，有明显的共存现象，共存多出现在损伤后6h和1d。进而我们通过蛋白免疫印迹技术对缺血区GRIP1蛋白表达水平与GluR2/3在细胞膜与细胞浆的分布状态进行了研究，研究发现脑缺血导致的GRIP1升高时程与GluR2/3在细胞膜上的含量变化非常吻合，当GRIP1在缺血后6h~12h达最高水平时，GluR2/3在细胞膜上的含量也达最高，表明GRIPs的表达升高可能是致使GluR2/3在胞膜上分布升高的原因。同时我们第一次发现了脑缺血能诱导GRIP1、GRIP2在大脑少突胶质细胞上的表达。这些结果均表明GRIP1、GRIP2在缺血缺氧性脑损伤过程中可能扮演重要角色。
Stroke, because of occlusion or rupture of an artery, is a leading cause ofdeath or infirmity in developed countries. As stroke, lack of blood flow to thebrain (ischemia) results in excessive release of the neurotransmitter glutamateinto the extracellular space. For over two decades, it has been known that theglutamate release activates ionotropic glutamate receptors, causing calciumentry, excitotoxicity, and neuronal death in vulnerable brain regions. Manyaspects are remained yet including the specific role of different types of Ca2+-permeable glutamate receptor in precipitating cell death and why neurons insome regions of the brain,such as hippocampal CA1 pyramidal neurons, striatalspiny neurons, and cortical projection neurons, are more vulnerable to glutamatemediated excitotoxicity. In the central nervous system (CNS), activation ofionotropic glutamate receptors allows a rapid influx of ions across the neuronalmembrane, mediating fast excitatory synaptic transmission. Ionotropicglutamate receptors are also critical for synaptic plasticity , learning andmemory. However, excessive activation of glutamate receptors in pathologicalconditions, such as anoxia or ischemia, precipitates excitotoxic neuronal death in vulnerable neuronal types by allowing an excessive influx of Ca2+, Na+, andZn2+ into neurons. There are three main classes of ionotropic glutamate receptor:NMDA, AMPA, and kainate receptors. Because all NMDA receptors arepermeable to calcium, it is focused on the role of these receptors in ischemicinjury in early studies. More recently, however, the hotspot is gradually shiftedto a critical role played by Ca2+-permeable AMPA receptors. AMPA receptors(AMPARs) are heteromeric assemblies of subunits GluR1– GluR4. AMPARslacking GluR2 subunits are permeable to Ca2+ and Zn2+. Ca2+-impermeability inGluR2-containing receptors is specified by the presence of an arginine (R)residue present in transmembrane domain 2 of this subunit instead of theglutamine residue (Q) in the GluR1, GluR3, and GluR4 subunits. Although thevast majority of GluR2 subunits in the brain contain arginine at this site, thisphenotype is not encoded at the genomic level but is the result of RNA editingof the GluR2 pre-mRNA in the nucleus by the enzyme adenosine deaminase 2(ADAR2), which catalyzes site-selective deamination of adenosine in thegenomic glutamine codon (CAG) to an inosine, giving an arginine codon (CIG)in the mRNA. This position is nearly 100% edited in the brain, so the vastmajority of GluR2-containing AMPARs in the CNS containing GluR2(R) areCa2+-impermeable. In addition, Q/R editing also influences subunit assembly,membrane trafficking, and synaptic targeting of GluR2-containing receptors.The observation that GluR2 expression is specifically attenuated in vulnerableCA1 pyramidal neurons after transient ischemia led to the‘‘GluR2 hypothesis,’’which proposed that decreased availability of Ca2+-impermeable GluR2(R)protein after a neurological insult would result in augmented formation of Ca2+-permeable AMPARs and consequently increased neurotoxic Ca2+ (and possiblyZn2+) influx. Remaining more controversial are the molecular mechanisms that underlie the postischemic downregulation of GluR2(R) protein and, the role ofGluR2 Q/R editing in this process. Peng promoted further understanding ofthe mechanisms that increase AMPAR Ca2+ permeability in vulnerable CA1hippocampal cells after transient forebrain ischemia. By combination ofelectrophysiology and single-cell RT-PCR, the authors correlated GluR2 Q/Rediting efficiency with the Ca2+ permeability of AMPARs in single neuron.Postischemic CA1 pyramidal cells exhibited high levels of heterogeneity in Q/Rediting (7%–98%) compared with sham controls and other less-vulnerablehippocampal cell types (CA3 pyramidal or dentate granule cells), which allexhibited over 95% editing efficiency, suggesting that GluR2Q/R editing inCA1 pyramidal neurons is particularly vulnerable to ischemic insult.Importantly, the impaired GluR2 Q/R editing correlated closely with the Ca2+-permeability of AMPAR channels (assessed from the reversal potential of theAMPAR current) in these cells.Failure to detect alterations in levels of GluR2protein, GluR2 Q/R editing in ischemia in early research may reflect the use ofwhole hippocampal tissue rather than RNA derived from singleelectrophysiologicallycharacterised cells.The postischemic reduction inADAR2-dependent GluR2 Q/R editing results in accumulation of uneditedGluR2 pre-mRNA in the nucleus, which downregulates both GluR2 mRNA andprotein levels, while the remaining GluR2(Q) proteinis preferentially assembledto produce Ca2+-permeable AMPARs that are exported to synapses. Furtherinvestigaton is needed to address these differences.
The AMPA receptor subunits GluR2/3 can bind specifically to a kind ofPDZ proteins, termed as glutamate receptor-interacting protein (GRIP), AMPAreceptor-binding protein (ABP), and protein interacting with C kinase 1 (PICK1).Both GRIP1 and GRIP2 contain seven PDZ domains without other recognizable motif, ABP resembles GRIP in primary sequence; it differs from GRIP mostnotably in lacking the C-terminal seventh PDZ domain. GRIP1 also binds akinesin that functions in transport of dendritic vesicles along microtubules indendrites, showing that the scaffolding protein determines the direction oftransport .When the kinesin was bound to a member of the JIP group of scaffoldproteins, JSAP, it moved toward the axon, while when it was bound to GRIP1, itmoved toward the dendrite.GRIP1 can directly interact and steer kinesin heavychains to dendrites of neurons as a motor for AMPA receptors.So GRIP1 andGRIP2 may play important role on exporting GluR2/3 to synapses during anoxiaand ischemia.To clarify the mechanisms of the GRIP1 and GRIP2 for exportingGluR2/3 to synapses during anoxia and ischemia will facilitate to find effectiveantagonist to anoxia and ischemia.
In this study, focal cerebral infarction model of adult rat were establishedbased on the principle of photochemical initiation of thrombosis, the rats weredivided into 5 groups according to the timecourse after cerebral local ischemia.Anti GRIP1 and GRIP2 antibodies were used via immunohistochemistry toanalysis the differences between the normal and the injury cerebral and thedifferences among every time point after ischemia.The results show that necrosishappened around the focus of injury region.And we can also find the GRIP1 andGRIP2 labeled neurons and immunoreactive nerve fibers in the ischemicpenumbra. Neurons in the cerebral of 6h and 1d groups are more heavily labeledthan others, cells labeled by GRIP1 and GRIP2 antibodys were coincide with theischemic penumbra. It suggests that the expression of GRIP1 and GRIP2increased after irradiation, GRIPs may be play a role on the mechanisms ofischemia injury. Because of the excitotoxicity of AMPA receptors and theinteraction between GRIP1/2 and AMPA receptors, the relationship between GRIP1/2 and AMPA receptors was further investigated next. Double-labelimmunocytochemistry was used demonstrating that the GluR2、GluR3 werecolocalized with GRIP1/2 in cerebral neuron, specially in the ischemicpenumbra and V pyramidal cells, and the colocalization happeded more at 6h and1d after the irradiation. Furthermore, using Western blotting, we study therelationship the levels of GRIP1 in ischemic penumbra and the levels ofmembrane GluR2/3, we found that the elevated levels of GRIP1 was coincidewith the accumulating of GluR2/3 after rat brain ischemia.When the levels ofGRIP1 were highest during 6h~12h after rat brain ischemia, the levels ofmembrane GluR2/3 reached the highest level suggesting that the accumulatingof membrane GluR2/3 may be induced by GRIPs. We demonstrated for the firsttime that ischemia can induce the expression of GRIP1 and GRIP2 on theoligendendrocytes in corpus callosum implying an important role of GRIP1 andGRIP2 in brain ischemia.
引文
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