title: Amygdaloid kindling elicits persistent changes in pertussis toxin-catalyzed ADP-ribosylation.
abstract: We examined the changes in pertussis toxin (PTX)-catalyzed ADP-ribosylation in amygdaloid-kindled rats to clarify the role of G proteins in the basic mechanisms of epilepsies. Autoradiographic analysis showed a remarkable increase in PTX-catalyzed ADP-ribosylation in 39-41-kDa proteins in hippocampus and cerebral cortex of kindled animals. The 39- to 41-kDa proteins were shown to be alpha-subunits of Gi and Go by immunoblotting with specific anti-Gi alpha and anti-Go alpha. The increase in ADP-ribosylation of these proteins was observed on stimulated and unstimulated sides of brains 24 h after the last generalized seizure and persisted for at least 3-4 weeks. These results suggest that persistent alterations in signal transduction through Gi and Go might be related to acquisition of long-lasting epileptogenesis.
authors.affiliation: Department of Neuropsychiatry, Faculty of Medicine, Chiba University, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Iwasa
authors.forename: S
authors.initials: S
authors.lastname: Hasegawa
authors.forename: S
authors.initials: S
authors.lastname: Kikuchi
authors.forename: K
authors.initials: K
authors.lastname: Watanabe
authors.forename: T
authors.initials: T
authors.lastname: Sato
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D000679:Amygdala / Q000378:metabolism* / Q000502:physiology; D000818:Animals; D001345:Autoradiography; D004827:Epilepsy / Q000209:etiology; D019204:GTP-Binding Proteins / Q000378:metabolism*; D015151:Immunoblotting; D007696:Kindling, Neurologic / Q000502:physiology*; D008297:Male; D037342:Pertussis Toxin; D051381:Rats; D017207:Rats, Sprague-Dawley; D015398:Signal Transduction / Q000502:physiology; D010566:Virulence Factors, Bordetella
chemical_list: D010566:Virulence Factors, Bordetella; D000255:Adenosine Triphosphate; D037342:Pertussis Toxin; D019204:GTP-Binding Proteins