Selective increase in phosphorylation of a 47-kDa protein (F1) directly related to long-term potentiation.
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.
Routtenberg
A
A
Lovinger
D M
DM
D000818:Animals; D001923:Brain Chemistry; D005071:Evoked Potentials; D006624:Hippocampus / Q000502:physiology*; D066298:In Vitro Techniques; D008297:Male; D009419:Nerve Tissue Proteins / Q000502:physiology*; D010750:Phosphoproteins / Q000502:physiology*; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D013569:Synapses / Q000502:physiology*; D013997:Time Factors
D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D011494:Protein Kinases; D011493:Protein Kinase C