{"@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/1361699993408591104.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1083/jcb.115.4.983"}},{"identifier":{"@type":"URI","@value":"https://rupress.org/jcb/article-pdf/115/4/983/1468609/983.pdf"}},{"identifier":{"@type":"NAID","@value":"80006211857"}}],"dc:title":[{"@value":"Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum."}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>Dilated cisternae of the ER resembling Russell Bodies (RBs) are induced in light (L) chain producing myeloma cell lines by transfection of a mu heavy (H) chain gene lacking the first constant domain (mu delta CH1). RBs do not appear to be tissue specific, since they are also induced in a rat glioma cell line transfected with mu delta CH1 and L chain genes. Efficient RB biogenesis requires H-L assembly and polymerization. The mutant Ig is partially degraded in a pre-Golgi compartment. The remnant, however, becomes an insoluble lattice when intersubunit disulphide bonds are formed. The resulting insoluble aggregate accumulates in RBs. Replacing the COOH-terminal cysteine of mu delta CH1 chains with alanine reverses the RB-phenotype: the double mutant mu ala delta CH1 chains assemble noncovalently with L and are secreted as H2L2 complexes. Similarly, secretion of mu delta CH1 chains can be induced by culturing transfectant cells in the presence of reducing agents. The presence of RBs does not alter transport of other secretory or membrane molecules, nor does it affect cell division. Resident proteins of the ER and other secretory proteins are not concentrated in RBs, implying sorting at the ER level. Sorting could be the result of the specific molecular structure of the insoluble lattice. We propose that RBs represent a general response of the cell to the accumulation of abundant, nondegradable protein(s) that fail to exit from the ER.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1583950401454270208","@type":"Researcher","foaf:name":[{"@value":"C Valetti"}],"jpcoar:affiliationName":[{"@value":"Istituto Scientifico San Raffaele, Milano, Italy."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993408591104","@type":"Researcher","foaf:name":[{"@value":"C E Grossi"}],"jpcoar:affiliationName":[{"@value":"Istituto Scientifico San Raffaele, Milano, Italy."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993408591106","@type":"Researcher","foaf:name":[{"@value":"C Milstein"}],"jpcoar:affiliationName":[{"@value":"Istituto Scientifico San Raffaele, Milano, Italy."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699993408591107","@type":"Researcher","foaf:name":[{"@value":"R Sitia"}],"jpcoar:affiliationName":[{"@value":"Istituto Scientifico San Raffaele, Milano, Italy."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219525"},{"@type":"EISSN","@value":"15408140"}],"prism:publicationName":[{"@value":"The Journal of cell biology"}],"dc:publisher":[{"@value":"Rockefeller University Press"}],"prism:publicationDate":"1991-11-15","prism:volume":"115","prism:number":"4","prism:startingPage":"983","prism:endingPage":"994"},"reviewed":"false","url":[{"@id":"https://rupress.org/jcb/article-pdf/115/4/983/1468609/983.pdf"}],"createdAt":"2004-05-15","modifiedAt":"2023-07-22","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050282677702088192","@type":"Article","resourceType":"紀要論文(departmental bulletin paper)","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@value":"aly/alyマウス胆管上皮内及び胆管腔内にみられる異常好酸性物質の病理学的,免疫組織化学的解析"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004234496191232","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"COPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartments"}]},{"@id":"https://cir.nii.ac.jp/crid/1360576118696867584","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Endoplasmic reticulum–to–Golgi trafficking of procollagen III via conventional vesicular and tubular carriers"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204335210752","@type":"Article","relationType":["isReferencedBy","isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"A case of primary cutaneous marginal zone B-cell lymphoma with Russell bodies"},{"@language":"ja","@value":"Russell小体の出現を伴った皮膚原発marginal zone B－cell lymphomaの1例"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204438129152","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Formation of Endoplasmic Reticulum-Associated Compartment in Vasopressin Neurons: A Mechanism by Which Endoplasmic Reticulum Stress is Reduced"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204708761728","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"An Equine Case of Malignant Lymphoma with Numerous Russell Bodies"},{"@language":"ja","@value":"ラッセル小体の多数出現を伴う馬の悪性リンパ腫の1例"},{"@language":"ja-Kana","@value":"ラッセル ショウタイ ノ タスウ シュツゲン オ トモナウ ウマ ノ アクセイ リンパ シュ ノ 1レイ"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679610030976","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Characterization of Russell Bodies Accumulating Mutant Antithrombin Derived from the Endoplasmic Reticulum"}]},{"@id":"https://cir.nii.ac.jp/crid/1520853833846068224","@type":"Article","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@value":"Mott cell tumor of the stomach with Helicobacter pylori infection"},{"@language":"ja-Kana","@value":"Mott cell tumor of the stomach with Helicobacter pylori infection"}]},{"@id":"https://cir.nii.ac.jp/crid/1522543655513518208","@type":"Article","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@value":"Mutation Study of Antithrombin: The Roles of Disulfide Bonds in Intracellular Accumulation and Formation of Russell Body-Like Structures"},{"@language":"ja-Kana","@value":"Mutation Study of Antithrombin The Roles of Disulfide Bonds in Intracellular Accumulation and Formation of Russell Body Like 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