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‐regulat...

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Published inEuropean journal of biochemistry Vol. 194; no. 1; pp. 287 - 291
Main Authors MASSÉ, Thierry, GARCIN, Dominique, JACQUEMONT, Bernard, MADJAR, Jean‐Jacques
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 26.11.1990
Blackwell
Subjects
Animals
Biological and medical sciences
Carcinoma, Squamous Cell
Cell Transformation, Neoplastic - metabolism
Dose-Response Relationship, Drug
Fundamental and applied biological sciences. Psychology
Genes, ras
Herpes Simplex - metabolism
Humans
Hydrogen-Ion Concentration
In Vitro Techniques
Molecular and cellular biology
Molecular genetics
neomycin
Neomycin - pharmacology
Phosphatidylinositols - metabolism
Phosphatidylinositols - physiology
Phosphorylation
Protein Kinase C - metabolism
Rats
Replication
Ribosomal Protein S6
ribosomal proteins
Ribosomal Proteins - metabolism
Simplexvirus - physiology
Tetradecanoylphorbol Acetate - administration & dosage
Tumor Cells, Cultured
Human
Phosphoinositide
Phosphorylation
Protein kinase C
Herpesviridae
Transformed cell
Alphaherpesvirinae
Ribosomal protein
Virus
Infection
Signal transduction
Antibiotic
Herpesvirus hominis 1
Neomycin
Inhibition
Tumor cell
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Summary: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.
Bibliography:After this paper was submitted, an article by Kaner et al. [43] appeared demonstrating that the fibroblast growth factor receptor is a portal for cellular entry for HSV‐1 into vertebrate cells. Fibroblast growth factor treatment of Swiss 3T3 cells activates a subunit of S6 kinase [44]. If our cells express the fibroblast growth factor receptor, the stimulation of inositol phospholipid pathway and of S6 phosphorylation after HSV‐1 infection could be explained by a direct interaction between the viral particle and the fibroblast growth factor receptor.
Note.
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-2956
1432-1033
DOI:10.1111/j.1432-1033.1990.tb19455.x