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Amygdaloid Kindling Elicits Persistent Changes in Pertussis Toxin‐Catalyzed ADP‐Ribosylation
Author(s) -
Iwasa Hiroto,
Hasegawa Shuji,
Kikuchi Shuichi,
Watanabe Kaori,
Sato Toshio
Publication year - 1994
Publication title -
epilepsia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.687
H-Index - 191
eISSN - 1528-1167
pISSN - 0013-9580
DOI - 10.1111/j.1528-1157.1994.tb02523.x
Subject(s) - pertussis toxin , epileptogenesis , adp ribosylation , kindling , g protein , toxin , hippocampus , amygdala , epilepsy , chemistry , neuroscience , endocrinology , signal transduction , medicine , biology , biochemistry , enzyme , nad+ kinase
Summary: 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 39–4 1‐kDa proteins in hippocampus and cerebral cortex of kindled animals. The 39‐to 41‐kDa proteins were shown to be a ‐subunits of Gi and Go by immunoblotting with specific anti‐Cia and anti‐Goa. The increase in ADP‐ribosylation of these proteins was observed on stimulated and unstimulated sides of brains 24 h after the last genralized 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.