Selective increase in phosphorylation of a 47-kDa protein (F1) directly related to long-term potentiation |
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| Authors: | A Routtenberg D M Lovinger |
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| Affiliation: | 1. Department of Chemistry, University of Kentucky, Lexington, KY 40506-0055, USA;2. Department of Pediatrics, University of Kentucky, Lexington, KY 40536, USA;3. Markey Cancer Center, University of Kentucky, Lexington, KY 40536, USA;4. Department of Toxicology and Cancer Biology, University of Kentucky, Lexington, KY 40536-0305, USA;5. Department of Radiation Medicine, University of Kentucky, Lexington, KY 40506-9983, USA;6. Sanders-Brown Center on Aging, University of Kentucky, Lexington, KY 40506-0055, USA |
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| Abstract: | Five minutes after the induction of long-term potentiation (LTP) in the intact hippocampal formation of chloralose/urethane-anesthetized rats there was a selective increase in the in vitro phosphorylation state of a 47-kDa band (designated Protein F1). When low frequency, nonpotentiating stimulation was used, no change in Protein F1 was observed. LTP had no significant effect on other phosphoproteins measured at the 5-min time point. In vitro phosphorylation of Protein F1 5 min after LTP was directly related to the change in synaptic efficiency (r = +0.86, p less than .01). The calcium-dependent, synaptically localized Protein F1 may be the same as the brain-specific Protein B-50. The regulation of the plastic LTP response may involve the novel multifunctional phospholipid-dependent enzyme, Protein Kinase C, which has been shown to phosphorylate B50. |
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