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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A reelin-integrin receptor interaction regulates Arc mRNA translation in synaptoneurosomes.
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A reelin-integrin receptor interaction regulates Arc mRNA translation in synaptoneurosomes.

机译：reelin-整合素受体相互作用调节突触神经小体中Arc mRNA的翻译。

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摘要

Reelin is synthesized and secreted into extracellular matrix by cortical gamma-aminobutyric acid (GABA)ergic interneurons and binds with high affinity to the extracellular domain of integrin receptors expressed in dendritic shaft and spine postsynaptic densities (DSPSD) of pyramidal neurons. In heterozygous reeler mice, reelin bound to DSPSD, and the expression of Arc (activity-regulated cytoskeletal protein) is lower than in wild-type mice. We studied the effect of reelin on Arc and total protein synthesis in synaptoneurosomes (SNSs) prepared from mouse neocortex. Recombinant full-length mouse reelin displaces the high affinity (K(D) = 60 fM) binding of [(125)I]echistatin (a competitive integrin receptor antagonist) to integrin receptors with a K(i) of 22 pM and with a Hill slope close to 1. Echistatin (50-100 nM) competitively antagonizes and abates reelin binding. The addition of reelin (2-40 pM) to SNSs enhances the incorporation of [(35)S]methionine into Arc and other rapidly translated proteins in a concentration-dependent manner. This incorporation is virtually abolished by 50-100 nM echistatin or by 5-10 nM rapamycin, a blocker of the mammalian target of rapamycin kinase. We conclude that reelin binds with high affinity to integrin receptors expressed in SNSs and thereby activates Arc protein synthesis.
机译：Reelin是由皮质γ-氨基丁酸（GABA）能性神经元合成并分泌到细胞外基质中的，并以高亲和力与锥体神经元的树突状干和突触后突触密度（DSPSD）中表达的整联蛋白受体的胞外域结合。在杂合子盘小鼠中，reelin与DSPSD结合，并且Arc（活性调节的细胞骨架蛋白）的表达低于野生型小鼠。我们研究了reelin对由小鼠新皮层制备的突触神经小体（SNSs）中Arc和总蛋白合成的影响。重组全长小鼠reelin以22 pM的K（i）取代[（125）I] echistatin（一种竞争性整合素受体拮抗剂）与整合素受体的高亲和力（K（D）= 60 fM）结合。接近1的山坡。棘皮抑素（50-100 nM）竞争性拮抗并减少瑞林结合。向SNSs中加入reelin（2-40 pM）可增强[（35）S]蛋氨酸以浓度依赖的方式掺入Arc和其他快速翻译的蛋白质中。这种掺入实际上被50-100 nM echistatin或5-10 nM雷帕霉素（雷帕霉素激酶的哺乳动物靶标阻滞剂）消除了。我们得出的结论是，reelin以高亲和力与SNS中表达的整合素受体结合，从而激活Arc蛋白的合成。

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