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Vol. 298, Issue 1, 339-345, July 2001
) Influences Cell
Proliferation Pathways
Department of Pharmacology, Fox Chase Cancer Center, Philadelphia,
Pennsylvania (T.W., L.G., P.A., K.D.T.); Imperial Cancer Research
Fund Molecular Pharmacology Unit, University of Dundee, Dundee,
United Kingdom (C.R.W., C.J.H.); and Ruttenberg Cancer Center, Mt.
Sinai School of Medicine, New York, New York (Z.R.)
Glutathione S-transferase P1-1 (GST
) is an
abundant and ubiquitously expressed protein in normal and malignant
mammalian tissues and possesses catalytic and ligand binding
properties. Our present data suggest that the protein contributes to
the regulation of cell proliferation. Mouse embryo fibroblasts (MEFs)
isolated from mice with a GSTP1-1 [glutathione
S-transferase P1-1 (isozyme in nonhepatic tissue)]
null genotype (GST
/) doubled their population
in 26.2 h versus 33.6 h for the wild type
(GST+/+). Retroviral transfection of GSTP1-1
into GST/ MEF cells slowed the doubling time to
30.4 h. Both early passage and immortalized MEF cells from
GST/ animals expressed significantly elevated
activity of extracellular signal-regulated kinases ERK1/ERK2, kinases
linked to cell proliferation pathways. In vivo, GST/
mice had higher basal levels of circulating white blood cells compared
with GST+/+. Administration of a peptidomimetic
inhibitor of GSTP1-1, TLK199, (
-glutamyl-S-(benzyl)cysteinyl-R-phenyl
glycine diethyl ester), stimulated both lymphocyte production and bone
marrow progenitor (colony-forming unit-granulocyte macrophage)
proliferation, but only in GST+/+ and not in
GST/ animals. Selection of a resistant clone of an
HL60 tumor cell line through chronic exposure to TLK199 resulted in
cells with elevated activities of c-Jun NH2 terminal kinase
(JNK1) and ERK1/ERK2, and allowed the cells to proliferate under stress
conditions that induced high levels of apoptosis in the wild type
cells. The in vitro and in vivo data are consistent with the principle
that GSTP1-1 influences cell proliferation.
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