Autoantibodies against an extracellular peptide of the GluR3 subtype of AMPA receptors activate both homomeric and heteromeric AMPA receptor channels.
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.
Cohen-Kashi Malina
Katayun
K
Department of Neurobiology, The Weizmann Institute of Science, 76100 Rehovot, Israel.
Ganor
Yonatan
Y
Levite
Mia
M
Teichberg
Vivian I
VI
D000595:Amino Acid Sequence; D000818:Animals; D001323:Autoantibodies / Q000276:immunology* / Q000302:isolation & purification; D002846:Chromatography, Affinity; D019281:Dimerization; D005260:Female; D008969:Molecular Sequence Data; D051381:Rats; D018091:Receptors, AMPA / Q000737:chemistry / Q000276:immunology*; D014982:Xenopus laevis
D001323:Autoantibodies; D018091:Receptors, AMPA; C104723:glutamate receptor ionotropic, AMPA 3