Autoantibodies against an extracellular peptide of the GluR3 subtype of AMPA receptors activate both homomeric and heteromeric AMPA receptor channels

被引：25

作者：

Malina, Katayun Cohen-Kashi ^{[1
]}

Ganor, Yonatan ^{[1
]}

Levite, Mia ^{[1
]}

Teichberg, Vivian I. ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel

来源：

NEUROCHEMICAL RESEARCH | 2006年 / 31卷 / 10期

关键词：

glutamate receptors; GluR3; autoantibodies; epilepsy; whole cell recording; oocytes; AMPA receptor; brain;

D O I：

10.1007/s11064-006-9143-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1181 / 1190

页数：10

共 24 条

[1] Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes [J].