Calpain and the glutamatergic synapse.
Calpain and the glutamatergic synapse.
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DOI：
10.2741/s38
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发表时间：
2009-06-01
期刊：
影响因子：
--
通讯作者：
Lynch DR
中科院分区：
文献类型：
--
作者：
Doshi S;Lynch DR
钙蛋白酶是一种普遍存在于不同组织类型和许多生物体（包括哺乳动物）中的蛋白酶。它通常不会破坏其各种各样的底物，但更常见的是破坏它们的功能。在神经元中，由于这种蛋白酶切割其调节结构域，其许多底物变得失调，导致细胞之间的信号传导改变。在谷氨酸能突触传递中，钙蛋白酶的直接靶点包括所有主要的谷氨酸受体：NMDA受体、AMPA受体和mGluR。通过切割这些受体和相关的细胞内蛋白质，钙蛋白酶可以调节突触的生理学。因此，钙蛋白酶介导的神经元分裂不仅可能参与兴奋性毒性等病理事件，而且可能具有神经保护作用和生理突触传递作用。
Calpain is a ubiquitous protease found in different tissue types and in many organisms including mammals. It generally does not destroy its large variety of substrates, but more commonly disrupts their function. In neurons, many of its substrates become dysregulated as a result of cleavage of their regulatory domain by this protease, leading to altered signaling between cells. In glutamatergic synaptic transmission, direct targets of calpain include all of the major glutamate receptors: NMDA receptors, AMPA receptors and mGluR. By cleaving these receptors and associated intracellular proteins, calpain may regulate the physiology at glutamatergic synapses. As a result, calpain-mediated cleavage in neurons might not only be involved in pathological events like excitotoxicity, but may also have neuroprotective effects and roles in physiological synaptic transmission.