Tat protein from HIV-1 activates MAP kinase in granular neurons and glial cells from rat cerebellum

Andrea Menegon, Chiara Leoni, Fabio Benfenati, Flavia Valtorta

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)800-805
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume238
Issue number3
DOIs
Publication statusPublished - Sep 29 1997

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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