Abstract
In this study, we investigated the effects of protein tyrosine kinase (PTK) and protein tyrosine phosphatase (PTP) on the tyrosine phosphorylation of N-methyl-D-aspartate receptor subunit 2A (NR2A) and the interactions among NR2A, postsynaptic density protein 95 (PSD-95), Fyn/Src after brain ischemia/reperfusion (I/R). The following results were observed: (1) the increase in tyrosine phosphorylation of NR2A induced by I/R was suppressed by genistein, an inhibitor of PTK, but was further enhanced by sodium orthovanadate, an inhibitor of PTP, which were administered to the SD rats 20 min before ischemia. (2) Importantly, genistein and sodium orthovanadate increased and decreased the interactions involving NR2A, PSD-95, Fyn and Src, respectively. These results demonstrated that PTK and PTP were involved in regulating tyrosine phosphorylation of NR2A through changing the interaction among NR2A, PSD-95, Fyn/Src.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Disks Large Homolog 4 Protein
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Intracellular Signaling Peptides and Proteins
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Ischemic Attack, Transient / metabolism*
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Membrane Proteins
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Nerve Tissue Proteins / metabolism*
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Phosphorylation
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Protein Subunits
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Protein Tyrosine Phosphatases / metabolism*
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Protein-Tyrosine Kinases / metabolism*
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-fyn
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Rats
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Rats, Sprague-Dawley
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Receptors, N-Methyl-D-Aspartate / metabolism*
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Tyrosine / metabolism
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src-Family Kinases / metabolism*
Substances
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Disks Large Homolog 4 Protein
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Dlg4 protein, rat
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Nerve Tissue Proteins
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Protein Subunits
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Proto-Oncogene Proteins
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Receptors, N-Methyl-D-Aspartate
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postsynaptic density proteins
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Tyrosine
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Protein-Tyrosine Kinases
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Fyn protein, rat
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Proto-Oncogene Proteins c-fyn
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src-Family Kinases
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Protein Tyrosine Phosphatases
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N-methyl D-aspartate receptor subtype 2A