Phosphorylation of the presynaptic protein B-50 (GAP-43) is increased during electrically induced long-term potentiation.
The protein B-50 (F1, GAP-43) is a presynaptic-specific substrate of protein kinase C, functionally related to neurotransmitter release. An increase in phosphorylation of this protein has been proposed as a molecular mechanism underlying long-term potentiation (LTP). B-50 phosphorylation measured by quantitative immunoprecipitation in rat hippocampal slices incubated in the presence of radiolabeled inorganic phosphate was increased for at least 1 hr after the induction of LTP in the CA1 region. No significant changes in B-50 phosphorylation were observed in untetanized slices stimulated at low frequency. The direct demonstration of an increased phosphorylation of the protein B-50 during LTP is consistent with the hypothesis that presynaptic mechanisms contribute to maintenance of LTP.
Gianotti
C
C
FIDIA Research Laboratories, Abano Terme, Italy.
Nunzi
M G
MG
Gispen
W H
WH
Corradetti
R
R
D000818:Animals; D004558:Electric Stimulation; D004594:Electrophysiology; D005071:Evoked Potentials; D019922:GAP-43 Protein; D006624:Hippocampus / Q000502:physiology*; D007163:Immunosorbent Techniques; D008297:Male; D008562:Membrane Glycoproteins / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D011921:Rats, Inbred WKY; D013569:Synapses / Q000502:physiology
D019922:GAP-43 Protein; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D011493:Protein Kinase C