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Nuclear translocation of glutathione S-transferase π is mediated by a non-classical localization signal.

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Title: Nuclear translocation of glutathione S-transferase π is mediated by a non-classical localization signal.
Authors: Kawakatsu, Miho / Goto, Shinji / Yoshida, Takako / Urata, Yoshishige / Li, Tao-Sheng
Issue Date: 12-Aug-2011
Publisher: Elsevier Inc.
Citation: Biochemical and Biophysical Research Communications, 411(4), pp.745-750; 2011
Abstract: Glutathione S-transferase π (GSTπ), a member of the GST family of multifunctional enzymes, is highly expressed in human placenta and involved in the protection of cellular components against electrophilic compounds or oxidative stress. We have recently found that GSTπ is expressed in the cytoplasm, mitochondria, and nucleus in some cancer cells, and that the nuclear expression of GSTπ appears to correlate with resistance to anti-cancer drugs. Although the mitochondrial targeting signal of GSTπ was previously identified in the amino-terminal region, the mechanism of nuclear translocation remains completely unknown. In this study, we find that the region of GSTπ195-208 is critical for nuclear translocation, which is mediated by a novel and non-classical nuclear localization signal. In addition, using an in vitro transport assay, we demonstrate that the nuclear translocation of GSTπ depends on the cytosolic extract and ATP. Although further experiments are needed to understand in depth the precise mechanism of nuclear translocation of GSTπ, our results may help to establish more efficient anti-cancer therapy, especially with respect to resistance to anti-cancer drugs.
Keywords: Cancer / Glutathione S-transferase π / Nuclear localization signal
URI: http://hdl.handle.net/10069/26096
ISSN: 0006291X
DOI: 10.1016/j.bbrc.2011.07.018
PubMed ID: 21782793
Rights: Copyright © 2011 Elsevier Inc. All rights reserved.
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/26096

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