1
Introduction
Peroxisome proliferator-activated receptors (PPARs)
belong to the nuclear hormone receptor superfamily
of ligand-activated transcription factors. Upon ligand
activation, PPAR translocates from cytoplasm to nucleus
and heterodimerizes with retinoid X receptor (RXR) to
regulate gene expression. hree isoforms (α, β, and γ)
for PPAR have been identiied so far in Xenopus, mouse,
human, rats, and hamsters. he PPAR subtypes share a
highly conserved DNA-binding domain that matches
with speciic DNA sequences known as peroxisome
proliferator response elements (PPREs). hese PPAR
isoforms are encoded by diferent genes, perform diferent
functions and exhibit diferent tissue localizations
(Issemann & Green, 1990; Dreyer et al., 1992; Kliewer
et al., 1994; Rosen et al., 2000; Zhu et al., 1993; Reddy &
Mannaerts, 1994). Imbalances in expression of target
genes that have a pivotal role in regulating metabolic
syndrome and cancer through atherogenic metabolic
triad/lipid triad metabolism has recently been noted
to be modulated by PPARs (Smith & Muscat, 2006).
15-Deoxy-Δ
12, 14
-prostaglandin J
2
(15d-PGJ2) is a natural
ligand for PPARγ and thiazolidinediones are synthetic
ligands (Houseknecht et al., 2002). It is prudent to note
that the expression of PPARγ in tumor breast tissue is
signiicantly higher than in normal breast epithelium.
Toward this end, development of a new class of anticancer
drugs through a new approach employing PPARγ activators
RESEARCH ARTICLE
Glycolytic enzymes PGK1 and PKM2 as novel
transcriptional targets of PPARγ in breast cancer
pathophysiology
Babita Shashni
1
, Kishore R. Sakharkar
2
, Yukio Nagasaki
3–5
, and Meena K. Sakharkar
1
1
Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan,
2
Omics Vista,
Singapore, Singapore,
3
Department of Materials Sciences, Graduate School of Pure and Applied Sciences, University of
Tsukuba, Ibaraki, Japan,
4
Master’s School of Medical Sciences, Graduate School of Comprehensive Human Sciences,
University of Tsukuba, Ibaraki, Japan, and
5
Satellite Laboratory, International Center for Materials Nanoarchitectonics
(WPI-MANA), National Institute for Materials Science (NIMS), University of Tsukuba, Ibaraki, Japan
Abstract
Peroxisome proliferator-activated receptor γ (PPARγ) is a nuclear receptor and plays important roles in breast cancer
cell proliferation. The complexity of the underlying biochemical and molecular mechanisms of breast cancer and the
involvement of PPARγ in breast cancer pathophysiology are unclear. In this study, we carried out prediction of the
peroxisome proliferator response element (PPRE) motifs in 2332 genes reported to be involved in breast cancer in
literature. A total of 178 genes were found to have PPRE (DR1/DR2) and / or PPAR-associated conserved motif (PACM)
motifs. We further constructed protein-protein interaction network, disease gene network and gene ontology (GO)
analyses to identify novel key genes for experimental validation. We identiied two genes in the glycolytic pathway
(phosphoglycerate kinase 1 (PGK1) and pyruvate kinase M2 (PKM2)) at the ATP production steps and experimentally
validated their repression by PPARγ in two breast cancer cell lines MDA-MB-231 and MCF-7. Further analysis suggested
that this repression leads to decrease in ATP levels and apoptosis. These investigations will help us in understanding
the molecular mechanisms by which PPARγ regulates the cellular energy pathway and the use of its ligands in human
breast cancer therapeutics.
Keywords: PPARγ, glycolysis, PGK1, PKM2, breast cancer
Address for Correspondence: Meena K. Sakharkar, Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba,
Ibaraki, Japan. Tel.: +81-29-853-8834. E-mail: msakharkar@gmail.com (or) meena.sak.gn@u.tsukuba.ac.jp
(Received 17 August 2012; revised 30 September 2012; accepted 02 October 2012)
Journal of Drug Targeting, 2012; Early Online: 1–14
© 2012 Informa UK, Ltd.
ISSN 1061-186X print/ISSN 1029-2330 online
DOI: 10.3109/1061186X.2012.736998
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