{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361137044801734272.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1016/j.lfs.2010.03.002"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0024320510000986?httpAccept=text/xml"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0024320510000986?httpAccept=text/plain"}},{"identifier":{"@type":"PMID","@value":"20226794"}}],"dc:title":[{"@value":"Inhibition of mitochondrial membrane bound-glutathione transferase by mitochondrial permeability transition inhibitors including cyclosporin A"}],"description":[{"notation":[{"@value":"Effect of mitochondrial permeability transition (MPT) inhibitors on mitochondrial membrane-bound glutathione transferase (mtMGST1) activity in rat liver was investigated in vitro.When mitochondria were incubated with MPT inhibitors, mtMGST1 activity was decreased dose dependently and their 50% inhibition concentration (IC(50)) were 1.2 microM (cyclosporin A; CsA), 31 microM (bongkrekic acid; BKA), 1.8 mM (ADP), and 3.2 mM (ATP). The decrease of mtMGST1 activity by the MPT inhibitors was not observed in the presence of detergent Triton X-100. On the contrary, mtMGST1 inhibition by GST inhibitors such as cibacron blue (IC(50), 4.2 microM) and S-hexylglutathione (IC(50), 480 microM) was not affected in the presence of detergent. Although mtMGST1 resides in both the inner (IMM) and outer mitochondrial membranes (OMM), only mtMGST1 in the IMM was inhibited by the MPT inhibitors in the absence of detergent. GST inhibitors decreased mtMGST1 activity both in the IMM and OMM regardless of the presence or absence of detergent. Cytosolic GSTs and microsomal MGST1 were not inhibited by the MPT inhibitors.These results indicate that mtMGST1 is inhibited by MPT inhibitors through membrane components, not directly by the inhibitors.Since CsA binds to cyclophilin D (Cyp-D) in the mitochondrial matrix whereas BKA or ADP binds to adenine nucleotide translocator (ANT) in the IMM, it was suggested that mtMGST1 in the IMM interacts with Cyp-D/ANT and the binding of MPT inhibitors to Cyp-D or ANT causes their conformational change followed by an alteration of mtMGST1 conformation, resulting in decreasing mtMGST1 activity."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381137044801734144","@type":"Researcher","foaf:name":[{"@value":"Enkhbaatar Ulziikhishig"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137044801734274","@type":"Researcher","foaf:name":[{"@value":"Kang Kwang Lee"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137044801734272","@type":"Researcher","foaf:name":[{"@value":"Quazi Sohel Hossain"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137044801734145","@type":"Researcher","foaf:name":[{"@value":"Yumiko Higa"}]},{"@id":"https://cir.nii.ac.jp/crid/1420564276181994112","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"10547384"},{"@type":"NRID","@value":"1000010547384"},{"@type":"NRID","@value":"9000240067947"},{"@type":"NRID","@value":"9000000636949"},{"@type":"NRID","@value":"9000021100454"},{"@type":"NRID","@value":"9000391998954"},{"@type":"NRID","@value":"9000411001666"},{"@type":"NRID","@value":"9000283732440"},{"@type":"NRID","@value":"9000003122922"},{"@type":"NRID","@value":"9000411001692"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/read0151763"}],"foaf:name":[{"@value":"Naoki Imaizumi"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137044801734146","@type":"Researcher","foaf:name":[{"@value":"Yoko Aniya"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00243205"}],"prism:publicationName":[{"@value":"Life Sciences"}],"dc:publisher":[{"@value":"Elsevier BV"}],"prism:publicationDate":"2010-05","prism:volume":"86","prism:number":"19-20","prism:startingPage":"726","prism:endingPage":"732"},"reviewed":"false","dc:rights":["https://www.elsevier.com/tdm/userlicense/1.0/"],"url":[{"@id":"https://api.elsevier.com/content/article/PII:S0024320510000986?httpAccept=text/xml"},{"@id":"https://api.elsevier.com/content/article/PII:S0024320510000986?httpAccept=text/plain"}],"createdAt":"2010-03-12","modifiedAt":"2025-02-19","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Male","dc:title":"Male"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Conformation","dc:title":"Protein Conformation"},{"@id":"https://cir.nii.ac.jp/all?q=Mitochondrial%20Membrane%20Transport%20Proteins","dc:title":"Mitochondrial Membrane Transport Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Rats,%20Sprague-Dawley","dc:title":"Rats, Sprague-Dawley"},{"@id":"https://cir.nii.ac.jp/all?q=Cyclophilins","dc:title":"Cyclophilins"},{"@id":"https://cir.nii.ac.jp/all?q=Inhibitory%20Concentration%2050","dc:title":"Inhibitory Concentration 50"},{"@id":"https://cir.nii.ac.jp/all?q=Cytosol","dc:title":"Cytosol"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Peptidyl-Prolyl%20Isomerase%20F","dc:title":"Peptidyl-Prolyl Isomerase F"},{"@id":"https://cir.nii.ac.jp/all?q=Enzyme%20Inhibitors","dc:title":"Enzyme Inhibitors"},{"@id":"https://cir.nii.ac.jp/all?q=Glutathione%20Transferase","dc:title":"Glutathione Transferase"},{"@id":"https://cir.nii.ac.jp/all?q=Dose-Response%20Relationship,%20Drug","dc:title":"Dose-Response Relationship, Drug"},{"@id":"https://cir.nii.ac.jp/all?q=Mitochondrial%20Permeability%20Transition%20Pore","dc:title":"Mitochondrial Permeability Transition Pore"},{"@id":"https://cir.nii.ac.jp/all?q=Rats","dc:title":"Rats"},{"@id":"https://cir.nii.ac.jp/all?q=Adenosine%20Diphosphate","dc:title":"Adenosine Diphosphate"},{"@id":"https://cir.nii.ac.jp/all?q=Liver","dc:title":"Liver"},{"@id":"https://cir.nii.ac.jp/all?q=Mitochondrial%20Membranes","dc:title":"Mitochondrial Membranes"},{"@id":"https://cir.nii.ac.jp/all?q=Cyclosporine","dc:title":"Cyclosporine"},{"@id":"https://cir.nii.ac.jp/all?q=Bongkrekic%20Acid","dc:title":"Bongkrekic Acid"},{"@id":"https://cir.nii.ac.jp/all?q=Mitochondrial%20ADP,%20ATP%20Translocases","dc:title":"Mitochondrial ADP, ATP Translocases"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Binding","dc:title":"Protein Binding"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360283691661462656","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Molecular Design, Synthesis, and Evaluation of Novel Potent Apoptosis Inhibitors Inspired 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