Linked Life Data

19269317

Source:http://linkedlifedata.com/resource/pubmed/id/19269317

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2009-4-20
pubmed:abstractText
Glutathione S-transferases (GSTs) are multifunctional enzymes involved in the protection of cellular components against anti-cancer drugs or peroxidative stress. Previously we found that GST pi, an isoform of the GSTs, is transported into the nucleus. In the present study, we found that GST pi is present in mitochondria as well as in the cytosol and nucleus in mammalian cell lines. A construct comprising the 84 amino acid residues in the amino-terminal region of GST pi and green fluorescent protein was detected in the mitochondria. The mutation of arginine to alanine at positions 12, 14, 19, 71, and 75 in full-length GST pi completely abrogated the ability to distribute in the mitochondria, suggesting that arginine, a positively charged residue, is required for the mitochondrial transport of GST pi. Chemicals generating reactive oxygen species, such as rotenone and antimycin A, decreased cell viability and reduced mitochondrial membrane potential. The overexpression of GST pi diminished these changes. GST pi-targeting siRNA abolished the protective effect of GST pi on the mitochondria under oxidative stress. The findings indicate that the peptide signal is conducive to the mitochondrial localization of GST pi under steady-state conditions without alternative splicing or posttranslational modifications such as proteolysis, suggesting that GST pi protects mitochondria against oxidative stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1873-4596
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1392-403
pubmed:meshHeading
pubmed-meshheading:19269317-Animals, pubmed-meshheading:19269317-Antimycin A, pubmed-meshheading:19269317-Arginine, pubmed-meshheading:19269317-COS Cells, pubmed-meshheading:19269317-Cercopithecus aethiops, pubmed-meshheading:19269317-Cytoprotection, pubmed-meshheading:19269317-Epithelial Cells, pubmed-meshheading:19269317-Glutathione S-Transferase pi, pubmed-meshheading:19269317-Humans, pubmed-meshheading:19269317-Membrane Potentials, pubmed-meshheading:19269317-Mitochondria, pubmed-meshheading:19269317-Mutagenesis, Site-Directed, pubmed-meshheading:19269317-Oxidative Stress, pubmed-meshheading:19269317-Protein Sorting Signals, pubmed-meshheading:19269317-Protein Transport, pubmed-meshheading:19269317-RNA, Small Interfering, pubmed-meshheading:19269317-Rotenone, pubmed-meshheading:19269317-Uncoupling Agents
pubmed:year
2009
pubmed:articleTitle
Glutathione S-transferase pi localizes in mitochondria and protects against oxidative stress.
pubmed:affiliation
Department of Biochemistry and Molecular Biology in Disease, Atomic Bomb Disease Institute, Nagasaki University Graduate School of Biomedical Sciences, Japan. sgoto@nagasaki-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't