Abstract

BackgroundTo determine the antiproliferative effect of gamma-tocotrienol (GTT) treatment on differential protein expression in HepG2 cells.MethodsHepG2 cells were treated with 70 μM GTT for 48 hours and differentially expressed protein spots were determined by two-dimensional electrophoresis (2DE), identified by MALDI-TOF mass spectrometer (MS) and validated by quantitative real-time polymerase chain reaction (qRT-PCR).ResultsGTT treatment on HepG2 cells showed a total of five differentially expressed proteins when compared to their respective untreated cells where three proteins were down-regulated and two proteins were up-regulated. One of these upregulated proteins was identified as peroxiredoxin-4 (Prx4). Validation by qRT-PCR however showed decreased expression of Prx4 mRNA in HepG2 cells following GTT treatment.ConclusionsGTT might directly influence the expression dynamics of peroxiredoxin-4 to control proliferation in liver cancer.

Highlights

  • To determine the antiproliferative effect of gamma-tocotrienol (GTT) treatment on differential protein expression in HepG2 cells

  • Differential analysis of 2DE protein maps of HepG2 cells The expression patterns of protein spots from HepG2 cells treated with GTT were compared to untreated control using 2DE image analysis software

  • Differential protein expression data were obtained from an independent comparison of at least three pairs of gels obtained from three independent cell growths

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Summary

Introduction

To determine the antiproliferative effect of gamma-tocotrienol (GTT) treatment on differential protein expression in HepG2 cells. GTT increases the expression of several antioxidant enzymes such as thioredoxin and quinine reductase 2 (NQO2) while suppressing the growth of MCF-7 cells [15]. In MDA-MB-231 cells, treatment by tocotrienols led to several fold increase of NRF2 expression marked by corresponding decrease in Kelch-like ECH-associated protein 1 (KEAP1) levels [15]. Major intracellular antioxidants such as glutathione, superoxide dismutase and catalase have long been recognized as part of our body’s detoxification mechanisms. A recently identified novel antioxidant from a family of peroxidases, the peroxiredoxins

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