Alteration in Protein Phosphorylation Associated with Olfactory Bulb Kindling

Soon Eng Tan, Robert F Berman

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Kindling is a model of neuronal plasticity underlying both epilepsy and memory. One of the cellular mechanisms associated with the increased synaptic efficacy is the modification of the structural configuration of synaptic membrane proteins. The present study examined changes in protein phosphorylation associated with olfactory bulb kindling. The differences in the degree of protein phosphorylation in four brain regions, i.e., olfactory bulb, pyriform cortex, hippocampus and frontal cortex, were examined in kindled, non-kindled and implanted control rats. Two phosphoproteins (45k and 48k, named according to their mol. wt.) in frontal cortex were altered after kindling. There was a two-fold increase in phosphorylation of a 48k phosphoprotein in the frontal cortex of kindled rats compared to controls. This phosphorylation was stimulated by Ca2+/calmodulin, and depressed by ACTH1-24. The 45k phosphoprotein in frontal cortex of kindled rats was decreased to 52% of the controls. The changes in protein phosphorylation found in frontal cortex are consistent with the hypothesis that permanent information storage may reside in cortical areas, while hippocampus and pyriform cortex may be the major relaying centers. This phenomenon could theoretically model an information storage process occurring in the cortex following relay of experiential input from subcortical areas.

Original languageEnglish (US)
Pages (from-to)123-129
Number of pages7
JournalChinese Journal of Physiology
Issue number2
StatePublished - 1996
Externally publishedYes


  • ACTH
  • Ca/calmodulin
  • Olfactory bulb kindling
  • Protein phosphorylation

ASJC Scopus subject areas

  • Physiology


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