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Identification of activity‐regulated proteins in the postsynaptic density fraction
Author(s) -
Satoh Keiko,
Takeuchi Masakazu,
Oda Yoshiya,
DeguchiTawarada Maki,
Sakamoto Yoshimasa,
Matsubara Kaho,
Nagasu Takeshi,
Takai Yoshimi
Publication year - 2002
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1046/j.1356-9597.2001.00505.x
Subject(s) - postsynaptic density , biology , postsynaptic potential , gel electrophoresis , neurotransmitter receptor , cytoskeleton , two dimensional gel electrophoresis , guanylate kinase , protein subunit , kainate receptor , biochemistry , polyacrylamide gel electrophoresis , receptor , proteomics , membrane protein , glutamate receptor , enzyme , cell , membrane , ampa receptor , gene
Background: The postsynaptic density (PSD) at synapses is a specialized submembranous structure where neurotransmitter receptors are linked to cytoskeleton and signalling molecules. Activity‐dependent dynamic change in the components of the PSD is a mechanism of synaptic plasticity. Identification of the PSD proteins and examination of their modulations dependent on synaptic activity will be valuable for an understanding of the molecular basis of learning and memory. Result: We attempted here to identify proteins in the PSD fraction by two‐dimensional (2D) gel electrophoresis and mass spectrometry. About 1.7 × 10 3 protein spots were detected on 2D gels. A total of 90 spots were identified, containing 47 different protein species. In addition to previously identified PSD proteins such as PSD‐95/SAP90, several new proteins were identified in the PSD fraction. They included stomatin‐like protein 2 and NIPSNAP1. We also examined activity‐dependent modulations of PSD proteins by 2D gel electrophoresis. The spot concentration of G protein β subunit 5 and NIPSNAP1 increased 2 h after kainate treatment that caused generalized seizures. Conclusion: These results indicate that the combination of 2D gel electrophoresis and mass spectrometry is an excellent tool for the identification of activity‐regulated PSD proteins.