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Glutathione S-transferase π complexes with and stimulates Na(+) ,K(+) -ATPase.
MedLine Citation:
PMID:  23280615     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Glutathione S-transferase (GST) was found to complex with the Na(+) ,K(+) -ATPase as shown by binding assay using quartz crystal microbalance. The complexation was obstructed by the addition of antiserum to the α-subunit of the Na(+) ,K(+) -ATPase, suggesting the specificity of complexation between GST and the Na(+) ,K(+) -ATPase. Co-immunoprecipitation experiments, using the anti-α-subunit antiserum to precipitate the GST-Na(+) ,K(+) -ATPase complex and then using antibodies specific to an isoform of GST to identify the co-precipitated proteins, revealed that GSTπ was complexed with the Na(+) ,K(+) -ATPase. GST stimulated the Na(+) ,K(+) -ATPase activity up to 1.4-fold. The level of stimulation exhibited a saturable dose-response relationship with the amount of GST added, although the level of stimulation varied depending on the content of GSTπ in the lots of GST received from supplier. The stimulation was also obtained when recombinant GSTπ was used, confirming the results. When GST was treated with reduced glutathione, GST activity was greatly stimulated, whereas the level of stimulation of the Na(+) ,K(+) -ATPase activity was similar to that when untreated GST was added. When GST was treated with H(2) O(2) , GST activity was greatly diminished while the stimulation of the Na(+) ,K(+) -ATPase activity was preserved. The results suggest that GSTπ complexes with the Na(+) ,K(+) -ATPase and stimulates the latter independent of its GST activity. Copyright © 2012 John Wiley & Sons, Ltd.
Authors:
Hideo Ochiai; Hiroshi Eguchi; Shunsuke Noguchi; Yutaro Hayashi; Hideaki Nishino; Masaru Kawamura; Chau H Wu
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular recognition : JMR     Volume:  26     ISSN:  1099-1352     ISO Abbreviation:  J. Mol. Recognit.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-02     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9004580     Medline TA:  J Mol Recognit     Country:  England    
Other Details:
Languages:  eng     Pagination:  32-7     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 John Wiley & Sons, Ltd.
Affiliation:
Department of Cell Biology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, 807-8555, Japan; The Center for Student Health, Kyushu Institute of Technology, Kitakyushu, 804-8550, Japan.
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