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Increased glutathione synthesis associated with platelet-derived growth factor stimulation of NIH3T3 fibroblasts

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
0167-4889
Publisher
Elsevier
Publication Date
Volume
1452
Issue
3
Identifiers
DOI: 10.1016/s0167-4889(99)00142-1
Keywords
  • Gsh Synthesis
  • Platelet-Derived Growth Factor
  • Nih3T3 Fibroblast
Disciplines
  • Biology

Abstract

Abstract Previous data show a relation between GSH content and proliferation of normal and tumour cells. We recently demonstrated a specific involvement of GSH in the autophosphorylation activity of the platelet-derived growth factor (PDGF) receptor in NIH3T3 fibroblasts. In this study we demonstrate that the stimulation by PDGF of serum-starved NIH3T3 cells increases cellular GSH content, while no change in oxidized GSH content was measured. Experiments performed with actinomycin, cycloheximide and buthionine sulfoximide, a specific inhibitor of the rate-limiting enzyme of the de novo synthesis of GSH γ-glutamylcysteine synthetase (γ-GCS), confirm PDGF induction of GSH synthesis. These results provide the first demonstration that PDGF mediated transduction signals seem strictly related to mechanisms involved in the increase of γ-GCS activity associated with increased γ-GCS heavy subunit mRNA levels. In fact, serum and epidermal growth factor (EGF) stimulation of quiescent NIH3T3 and NIH3T3, which overexpress EGF receptor, does not affect GSH content or its synthesis. These data may be related to a possible GSH role in the redox regulation of cell proliferation mediated by PDGF.

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