Cohen-Kashi Malina Katayun, Ganor Yonatan, Levite Mia, Teichberg Vivian I
Department of Neurobiology, The Weizmann Institute of Science, 76100 Rehovot, Israel.
Neurochem Res. 2006 Oct;31(10):1181-90. doi: 10.1007/s11064-006-9143-6. Epub 2006 Sep 12.
Autoantibodies to the GluR3-subtype of AMPA/glutamate receptors are found in the sera and cerebrospinal fluid of some individuals with epilepsy. They could possibly play a role in the pathophysiology of epilepsy since anti-GluR3 sera display glutamatergic agonist activity. We have investigated here the ability of affinity-purified antibodies (Abs) directed against the immunogenic peptide GluR3B (amino-acid 372-395) to interact with and activate recombinant GluR3-receptor channels expressed by Xenopus oocytes. We report here that the affinity-purified anti-GluR3B Abs directly activate GluR3-containing homomeric and heteromeric AMPA receptor complexes without the requirement of neuronal, glial or blood ancillary molecules. We present some of the properties of the purified anti-GluR3B Abs and discuss the possible physiological or pathological consequences of their activation of glutamate receptors.
在一些癫痫患者的血清和脑脊液中发现了针对AMPA/谷氨酸受体GluR3亚型的自身抗体。由于抗GluR3血清表现出谷氨酸能激动剂活性，它们可能在癫痫的病理生理学中发挥作用。我们在此研究了针对免疫原性肽GluR3B（氨基酸372 - 395）的亲和纯化抗体与非洲爪蟾卵母细胞表达的重组GluR3受体通道相互作用并激活该通道的能力。我们在此报告，亲和纯化的抗GluR3B抗体直接激活含GluR3的同源和异源AMPA受体复合物，而无需神经元、神经胶质或血液辅助分子。我们展示了纯化的抗GluR3B抗体的一些特性，并讨论了其激活谷氨酸受体可能产生的生理或病理后果。
