与长时程增强相关的突触质膜52-kDa磷蛋白与主要包被小泡磷蛋白的比较。

Comparison of a 52-kDa phosphoprotein from synaptic plasma membranes related to long-term potentiation and the major coated vesicle phosphoprotein.

作者信息

Schrama L H, de Graan P N, Zwiers H, Gispen W H

出版信息

J Neurochem. 1986 Dec;47(6):1843-8. doi: 10.1111/j.1471-4159.1986.tb13097.x.

DOI:10.1111/j.1471-4159.1986.tb13097.x

Abstract

In the in vitro hippocampal slice preparation a short tetanus induces long-term potentiation (LTP) and an increase 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 cyclic AMP. This resemblance prompted us to compare 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: relative molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peptide mapping, phospho-amino acid content, and isoelectric point. Since 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.

摘要

在体外海马脑片制备中，短暂的强直刺激可诱导长时程增强（LTP），并使从这些脑片中制备的突触体细胞膜（SPM）中一种52 kDa蛋白的事后磷酸化增加。这种52 kDa的SPM磷蛋白在其磷酸化对Ca2+/钙调蛋白和环磷酸腺苷的不敏感性方面，与被膜小泡中的主要磷蛋白pp50非常相似。这种相似性促使我们在大鼠脑中比较52 kDa的SPM蛋白与分离的被膜小泡中的pp50。基于以下标准，这两种蛋白似乎非常相似：十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上的相对分子量、肽图谱、磷酸氨基酸含量和等电点。由于被膜小泡被认为参与受体介导的内吞作用和膜循环，我们的数据表明，与LTP相关的52 kDa磷酸化变化可能反映了被膜小泡活性的增加。