{"@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/1361699994667085440.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1093/oxfordjournals.jbchem.a022781"}},{"identifier":{"@type":"URI","@value":"http://academic.oup.com/jb/article-pdf/128/3/509/2370621/128-3-509.pdf"}},{"identifier":{"@type":"PMID","@value":"10965052"}}],"dc:title":[{"@value":"Tripeptidyl Peptidase I, the Late Infantile Neuronal Ceroid Lipofuscinosis Gene Product, Initiates the Lysosomal Degradation of Subunit c of ATP Synthase"}],"description":[{"notation":[{"@value":"The specific accumulation of a hydrophobic protein, subunit c of ATP synthase, in lysosomes from the cells of patients with the late infantile form of NCL (LINCL) is caused by a defect in the CLN2 gene product, tripeptidyl peptidase I (TPP-I). The data here show that TPP-I is involved in the initial degradation of subunit c in lysosomes and suggest that its absence leads directly to the lysosomal accumulation of subunit c. The inclusion of a specific inhibitor of TPP-I, Ala-Ala-Phe-chloromethylketone (AAF-CMK), in the culture medium of normal fibroblasts induced the lysosomal accumulation of subunit c. In an in vitro incubation experiment the addition of AAF-CMK to mitochondrial-lysosomal fractions from normal cells inhibited the proteolysis of subunit c, but not the b-subunit of ATP synthase. The use of two antibodies that recognize the aminoterminal and the middle portion of subunit c revealed that the subunit underwent aminoterminal proteolysis, when TPP-I, purified from rat spleen, was added to the mitochondrial fractions. The addition of both purified TPP-I and the soluble lysosomal fractions, which contain various proteinases, to the mitochondrial fractions resulted in rapid degradation of the entire molecule of subunit c, whereas the degradation of subunit c was markedly delayed through the specific inhibition of TPP-I in lysosomal extracts by AAF-CMK. The stable subunit c in the mitochondrial-lysosomal fractions from cells of a patient with LINCL was degraded on incubation with purified TPP-I. The presence of TPP-I led to the sequential cleavage of tripeptides from the N-terminus of the peptide corresponding to the amino terminal sequence of subunit c."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380006464267574144","@type":"Researcher","foaf:name":[{"@value":"J. Ezaki"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994667085440","@type":"Researcher","foaf:name":[{"@value":"M. Takeda-Ezaki"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994667085441","@type":"Researcher","foaf:name":[{"@value":"E. Kominami"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"0021924X"},{"@type":"PISSN","@value":"http://id.crossref.org/issn/0021924X"}],"prism:publicationName":[{"@value":"Journal of Biochemistry"}],"dc:publisher":[{"@value":"Oxford University Press (OUP)"}],"prism:publicationDate":"2000-09-01","prism:volume":"128","prism:number":"3","prism:startingPage":"509","prism:endingPage":"516"},"reviewed":"false","url":[{"@id":"http://academic.oup.com/jb/article-pdf/128/3/509/2370621/128-3-509.pdf"}],"createdAt":"2012-04-19","modifiedAt":"2017-08-23","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Serine%20Proteinase%20Inhibitors","dc:title":"Serine Proteinase Inhibitors"},{"@id":"https://cir.nii.ac.jp/all?q=Gene%20Expression","dc:title":"Gene Expression"},{"@id":"https://cir.nii.ac.jp/all?q=Cytochrome%20c%20Group","dc:title":"Cytochrome c Group"},{"@id":"https://cir.nii.ac.jp/all?q=Aminopeptidases","dc:title":"Aminopeptidases"},{"@id":"https://cir.nii.ac.jp/all?q=Amino%20Acid%20Chloromethyl%20Ketones","dc:title":"Amino Acid Chloromethyl Ketones"},{"@id":"https://cir.nii.ac.jp/all?q=Electron%20Transport%20Complex%20IV","dc:title":"Electron Transport Complex IV"},{"@id":"https://cir.nii.ac.jp/all?q=Neuronal%20Ceroid-Lipofuscinoses","dc:title":"Neuronal Ceroid-Lipofuscinoses"},{"@id":"https://cir.nii.ac.jp/all?q=Endopeptidases","dc:title":"Endopeptidases"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Humans","dc:title":"Humans"},{"@id":"https://cir.nii.ac.jp/all?q=Dipeptidyl-Peptidases%20and%20Tripeptidyl-Peptidases","dc:title":"Dipeptidyl-Peptidases and Tripeptidyl-Peptidases"},{"@id":"https://cir.nii.ac.jp/all?q=Tripeptidyl-Peptidase%201","dc:title":"Tripeptidyl-Peptidase 1"},{"@id":"https://cir.nii.ac.jp/all?q=Infant","dc:title":"Infant"},{"@id":"https://cir.nii.ac.jp/all?q=Intracellular%20Membranes","dc:title":"Intracellular Membranes"},{"@id":"https://cir.nii.ac.jp/all?q=Fibroblasts","dc:title":"Fibroblasts"},{"@id":"https://cir.nii.ac.jp/all?q=Mitochondria","dc:title":"Mitochondria"},{"@id":"https://cir.nii.ac.jp/all?q=Rats","dc:title":"Rats"},{"@id":"https://cir.nii.ac.jp/all?q=Kinetics","dc:title":"Kinetics"},{"@id":"https://cir.nii.ac.jp/all?q=Proton-Translocating%20ATPases","dc:title":"Proton-Translocating ATPases"},{"@id":"https://cir.nii.ac.jp/all?q=Serine%20Proteases","dc:title":"Serine Proteases"},{"@id":"https://cir.nii.ac.jp/all?q=Lysosomes","dc:title":"Lysosomes"},{"@id":"https://cir.nii.ac.jp/all?q=Peptides","dc:title":"Peptides"},{"@id":"https://cir.nii.ac.jp/all?q=Spleen","dc:title":"Spleen"},{"@id":"https://cir.nii.ac.jp/all?q=Peptide%20Hydrolases","dc:title":"Peptide Hydrolases"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002215789977216","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Lysosomal Storage of Subunit c of Mitochondrial ATP Synthase in Brain-Specific Atp13a2-Deficient Mice"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004235508344576","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Differences in expression patterns of cathepsin <scp>C</scp>/dipeptidyl peptidase <scp>I</scp> in normal, pathological and aged mouse central nervous system"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283690766697984","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Purkinje Cells Are More Vulnerable to the Specific Depletion of Cathepsin D Than to That of 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