Title
Comparison of a 52-kDa phosphoprotein from synaptic plasma membranes related to long-term potentiation and the major coated vesicle phosphoprotein
Author
Gezondheidsorganisatie TNO Commissie voor landelijk epilepsie-onderzoek TNO
Schrama, L.H.
de Graan, P.N.E.
Zwiers, H.
Gispen, W.H.
Publication year
1986
Abstract
Abstract: In the in vitro hippocampal slice preparation a short tetanus induces long-term potentiation (LTP) and an inerease in the post hoc phosphorylation of a 52-kDa protein in synaptosomal plasma membranes (SPM) prepared from these slices. This 52-kDa SPM phosphoprotein closely resembles the predominant phosphoprotein in coated vesicles, pp50, with respect to the insensitivity of its phosphorylation to Ca2*/calmodulin and cyelic AMP. This resemblance prompted us to comparo in rat brain the 52-kDa SPM protein with pp50 in isolated coated vesicles. Both proteins appear to be very similar on basis of the following criteria: ( I ) relative molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, (2) peptide mapping, (3) phospho-amino acid content, and (4) isoelectric point. Sirice coated vesicles are thought to be involved in receptor-mediated endocytosis and membrane recycling, our data suggest that LTP-correlated changes in 52-kDa phosphorylation may reflect increased coated vesicle activity.
Subject
Long-term potentiation
Protein phosphorylation
Coated vesicles
Synaptosomal plasma membranes
Healthy for Life
Healthy Living
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TNO identifier
288182
Source
Journal of Neurochemistry, 47 (47), 1843-1848
Document type
article