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.
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.
Massé
T
T
Immuno-Virologie Moléculaire et Cellulaire, l'Université Claude Bernard, Faculté de Médecine Alexis Carrel, Lyon, France.
Garcin
D
D
Jacquemont
B
B
Madjar
J J
JJ
D000818:Animals; D002294:Carcinoma, Squamous Cell; D002471:Cell Transformation, Neoplastic / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D011905:Genes, ras; D006561:Herpes Simplex / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D009355:Neomycin / Q000494:pharmacology*; D010716:Phosphatidylinositols / Q000378:metabolism / Q000502:physiology*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D051381:Rats; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins / Q000378:metabolism*; D018139:Simplexvirus / Q000502:physiology*; D013755:Tetradecanoylphorbol Acetate / Q000008:administration & dosage; D014407:Tumor Cells, Cultured
D010716:Phosphatidylinositols; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins; D011493:Protein Kinase C; D009355:Neomycin; D013755:Tetradecanoylphorbol Acetate