{"@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/1361699993605494016.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1046/j.1432-1327.1998.2510504.x"}},{"identifier":{"@type":"URI","@value":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.1998.2510504.x"}},{"identifier":{"@type":"URI","@value":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.1998.2510504.x"}},{"identifier":{"@type":"NAID","@value":"80010155605"}}],"dc:title":[{"@value":"Chitotriosidase, a chitinase, and the 39‐kDa human cartilage glycoprotein, a chitin‐binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>In various mammals, enzymatically active and inactive members of family 18 glycosyl hydrolases, containing chitinases, have been identified. In man, chitotriosidase is the functional chitinolytic enzyme, whilst the homologous human cartilage 39‐kDa glycoprotein (HC gp‐39) does not exhibit chitinase activity and its function is unknown. This study establishes that HC gp‐39 is a chitin‐specific lectin. It is experimentally demonstrated that a single amino acid substitution in the catalytic centre of the 39‐kDa isoform of chitotriosidase, which generates a similar sequence to that in HC gp‐39, results in a loss of hydrolytic activity and creates the capacity to bind to chitin. The possible implication of the finding for chitinolytic and chitin‐binding proteins that are produced in high quantities by activated macrophages are discussed.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381699993605494018","@type":"Researcher","foaf:name":[{"@value":"G. Herma Renkema"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993605494023","@type":"Researcher","foaf:name":[{"@value":"Rolf G. Boot"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993605494016","@type":"Researcher","foaf:name":[{"@value":"Fung Lin Au"}]},{"@id":"https://cir.nii.ac.jp/crid/1380861294658853248","@type":"Researcher","foaf:name":[{"@value":"Wilma E. Donker‐Koopman"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993605494020","@type":"Researcher","foaf:name":[{"@value":"Anneke Strijland"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993605494017","@type":"Researcher","foaf:name":[{"@value":"Anton O. Muijsers"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993605494021","@type":"Researcher","foaf:name":[{"@value":"Martin Hrebicek"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993605494022","@type":"Researcher","foaf:name":[{"@value":"Johannes M. F. G. Aerts"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00142956"},{"@type":"EISSN","@value":"14321033"}],"prism:publicationName":[{"@value":"European Journal of Biochemistry"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"1998-01","prism:volume":"251","prism:number":"1-2","prism:startingPage":"504","prism:endingPage":"509"},"reviewed":"false","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.1998.2510504.x"},{"@id":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.1998.2510504.x"}],"createdAt":"2003-03-11","modifiedAt":"2023-08-31","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360004231952857344","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Chitinase Inhibition Promotes Atherosclerosis in Hyperlipidemic 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disorders"}]},{"@id":"https://cir.nii.ac.jp/crid/1390856693957910912","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Pathological examination of Ym1, a chitinase family protein, in <i>Mesocestoides corti</i>-infected mice"}]},{"@id":"https://cir.nii.ac.jp/crid/1390860532056106240","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Chitinase 3-Like-1 Expression Is Upregulated Under Inflammatory Conditions in Human Oral Epithelial Cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1520009407964215168","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@value":"Molecular Studies of Family 18 Chitinases in Animals--Structural and Functional Diversity"},{"@language":"ja-Kana","@value":"Molecular Studies of Family 18 Chitinases in Animals Structural and Functional Diversity"}]},{"@id":"https://cir.nii.ac.jp/crid/1523669555759592704","@type":"Article","relationType":["isReferencedBy","isCitedBy"],"jpcoar:relatedTitle":[{"@value":"Molecular cloning of a putative gastric chitinase in the toad Bufo japonicus"},{"@language":"ja-Kana","@value":"Molecular cloning of a putative gastric chitinase in the toad Bufo japonicus"},{"@language":"en","@value":"Molecular Cloning of a Putative Gastric Chitinase in the Toad Bufo japonicus(Biochemistry) :"}]},{"@id":"https://cir.nii.ac.jp/crid/1573387449801345664","@type":"Article","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@language":"ja","@value":"植物の生体防御機構を活性化するシグナルとしてのキチン・キチンオリゴ糖"},{"@language":"en","@value":"Chitin and Chitin Oligosaccharides as a Signal Molecule to Activate Plant Defense 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