Neuronal protein tyrosine kinases associated with synaptosomal glycoproteins
| Autor: | S. H. Hanissian, N. Sahyoun |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Immunoprecipitation
Immunoblotting Synaptic Membranes Biology Cellular and Molecular Neuroscience chemistry.chemical_compound Animals Phosphorylation Receptor chemistry.chemical_classification Neurons Membrane Glycoproteins Tyrosine phosphorylation Protein-Tyrosine Kinases Precipitin Tests Rats Membrane glycoproteins chemistry Biochemistry biology.protein Electrophoresis Polyacrylamide Gel Glycoprotein Tyrosine kinase Proto-oncogene tyrosine-protein kinase Src Synaptosomes |
| Zdroj: | Journal of neuroscience research. 32(4) |
| ISSN: | 0360-4012 |
| Popis: | Protein tyrosine kinase (PTK) activity associated with synaptosomal membrane glycoprotein (SMGP) fractions of rat brain was examined. The synthetic substrate poly(Glu4-Tyr) was phosphorylated by SMGP in the presence of Mg2+ and Mn2+, whose stimulatory effects were additive. In contrast, endogenous tyrosine phosphorylation in SMGPs was strictly dependent on Mn2+. Anti-phosphotyrosine antibodies (PY20) immunoprecipitated two polypeptides in SMGPs of Mr 170K and 60K. Upon preincubation with IGF-I, 97/90K polypeptides were phosphorylated, corresponding to the IGF-I receptor beta-subunits, and were immunoprecipitated with both PY20 and anti-IGF-I-receptor antibodies. Immunoblot analysis using anti-src antibody revealed that there was src protein associated with the glycoprotein fractions of solubilized synaptosomal membranes. Additional experiments revealed that the 60K tyrosine-phosphorylated polypeptide present in the PY20 precipitates was indeed pp60 c-src. This was confirmed by subjecting the PY20 immunoprecipitates to immunoblotting using anti-src antibodies. In addition, src protein was directly immunoprecipitated by anti-src antibodies from the SMGP preparations. Hence, IGF-I receptors and glycoprotein-associated PTKs in cluding pp60c-src may play an important role in synaptic transmembrane signalling, plasticity, and neuronal survival. © 1992 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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