Tat protein from HIV-1 activates MAP kinase in granular neurons and glial cells from rat cerebellum
| Autor: | Fabio Benfenati, Andrea Menegon, Flavia Valtorta, Chiara Leoni |
|---|---|
| Přispěvatelé: | Menegon, Andrea, Leoni, Chiara, Benfenati, Fabio, Valtorta, Flavia |
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Biophysics
Protein tyrosine phosphatase Calcium-Calmodulin-Dependent Protein Kinase Mitogen-activated protein kinase kinase Cytoplasmic Granules Biochemistry Receptor tyrosine kinase MAP2K7 Rats Sprague-Dawley chemistry.chemical_compound Cerebellum Animals ASK1 Phosphorylation Phosphotyrosine Molecular Biology Cells Cultured Neurons Kinetic biology MAP kinase kinase kinase Animal tat Gene Products Human Immunodeficiency Viru Tyrosine phosphorylation Cell Biology Neuron Molecular biology Cell biology Rats Enzyme Activation Molecular Weight Kinetics chemistry Biophysic Calcium-Calmodulin-Dependent Protein Kinases Gene Products tat biology.protein HIV-1 Rat tat Gene Products Human Immunodeficiency Virus Cytoplasmic Granule Neuroglia Proto-oncogene tyrosine-protein kinase Src Signal Transduction |
| Popis: | We have investigated the effect of extracellularly applied Tat protein of the human immunodeficiency virus type 1 (HIV-1) on tyrosine phosphorylation processes, which represent a major signal transduction pathway of cells of the central nervous system. Primary cultures of rat cerebellar astrocytes or granule cells were incubated with synthetic Tat (10 ng/ml) for various periods of time and analyzed for their phosphotyrosine content by Western blotting. In both types of cultures Tat was able to induce the phosphorylation of mitogen-activated protein kinase (MAP kinase) on tyrosine residues, although with different kinetics and isoform specificity. In addition, in neuronal cells, but not in astrocytes, Tat increased the phosphotyrosine content of Shc, a protein involved in signal transduction downstream of receptor tyrosine kinase activation. This study shows that Tat applied extracellularly is able to induce the generation of intracellular signals in neuronal as well as glial cells. |
| Databáze: | OpenAIRE |
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