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Scientific article
English

Herpes simplex virus type-1-induced stimulation of ribosomal protein S6 phosphorylation is inhibited in neomycin-treated human epidermoid carcinoma 2 cells and in ras-transformed cells

Published inEuropean journal of biochemistry, vol. 194, no. 1, p. 287-291
Publication date1990
Abstract

Neomycin, an inhibitor of inositol phospholipid turnover, prevents Herpes-simplex-virus-type-1 (HSV-1)-induced stimulation of ribosomal protein S6 phosphorylation, but does not impair the S6 phosphorylation induced by serum. Long-term treatment with phorbol 12-myristate 13-acetate, which down-regulates protein kinase C activity, does not inhibit virus-induced S6 phosphorylation. In ras-transformed cells, S6 phosphorylation is not stimulated after HSV-1 infection. These results suggest that activation of the inositol phospholipid pathway is involved in the HSV-1-induced stimulation of S6 phosphorylation. However, protein kinase C activation does not appear to be necessary for HSV-1-induced S6 phosphorylation.

Keywords
  • Animals
  • Carcinoma, Squamous Cell
  • Cell Transformation, Neoplastic/metabolism
  • Dose-Response Relationship, Drug
  • Genes, ras
  • Herpes Simplex/metabolism
  • Humans
  • Hydrogen-Ion Concentration
  • Neomycin/pharmacology
  • Phosphatidylinositols/metabolism/physiology
  • Phosphorylation
  • Protein Kinase C/metabolism
  • Rats
  • Ribosomal Protein S6
  • Ribosomal Proteins/metabolism
  • Simplexvirus/physiology
  • Tetradecanoylphorbol Acetate/administration & dosage
  • Tumor Cells, Cultured
Affiliation Not a UNIGE publication
Citation (ISO format)
MASSÉ, T et al. Herpes simplex virus type-1-induced stimulation of ribosomal protein S6 phosphorylation is inhibited in neomycin-treated human epidermoid carcinoma 2 cells and in ras-transformed cells. In: European journal of biochemistry, 1990, vol. 194, n° 1, p. 287–291. doi: 10.1111/j.1432-1033.1990.tb19455.x
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Article (Published version)
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ISSN of the journal0014-2956
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