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Title

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

Authors
Massé, T
Jacquemont, B
Madjar, J J
Published in European Journal of Biochemistry. 1990, vol. 194, no. 1, p. 287-91
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 AnimalsCarcinoma, Squamous CellCell Transformation, Neoplastic/metabolismDose-Response Relationship, DrugGenes, rasHerpes Simplex/metabolismHumansHydrogen-Ion ConcentrationNeomycin/pharmacologyPhosphatidylinositols/metabolism/physiologyPhosphorylationProtein Kinase C/metabolismRatsRibosomal Protein S6Ribosomal Proteins/metabolismSimplexvirus/physiologyTetradecanoylphorbol Acetate/administration & dosageTumor Cells, Cultured
Identifiers
PMID: 2174778
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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. 287-91. https://archive-ouverte.unige.ch/unige:37927

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Deposited on : 2014-06-18

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