{"@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/1364233270748833152.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1073/pnas.89.4.1189"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.89.4.1189"}},{"identifier":{"@type":"NAID","@value":"80006356415"}}],"dc:title":[{"@value":"GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol-anchored proteins in apical secretory compartments of pancreas and kidney."}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>A family of homologous genes is shown to encode GP-2, the major glycosylphosphatidylinositol (GPI)-linked glycoprotein of pancreatic zymogen granule membranes, and Tamm-Horsfall protein (THP), a GPI-linked glycoprotein associated with apical vesicles in kidney thick ascending limb of Henle (TALH) cells. The C-terminal regions of GP-2 (Asp54-Phe530) and THP (Asp175-His644) from rat show 53% identity, 86% similarity, and 26 conserved cysteine residues including one epidermal growth factor motif. The unique N-terminal domain of rat THP (unique-THP, Pro29-Gln174) shows four conserved epidermal growth factor motifs, three in tandem and one in reverse orientation. GP-2 homologues are observed in a wide variety of epithelial cells, several of which contain highly regulated secretory processes. GP-2 released from zymogen granule membranes with phosphatidylinositol phospholipase C reacts with anti-cross-reactive determinant antibody (anti-CRD), confirming the GPI nature of the pancreatic homologue. In contrast, GP-2 and THP, released endogenously from pancreas and kidney, respectively, do not react with anti-cross-reactive determinant antibody, suggesting alternative enzymatic mechanisms for their physiological release. Globular domains of GP-2 and THP, but not albumin, show pH- and ion-dependent self-association in vitro. The GP-2/THP family appears to represent a newly discovered class of GPI-anchored proteins, which may utilize pH- and ion-dependent self-association mechanisms for establishing membrane (micro)domains targeted to intracellular secretory compartments.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1583668926470873728","@type":"Researcher","foaf:name":[{"@value":"S Fukuoka"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Cell and Molecular Biology, Charles A. Dana Research Institute, Thorndike Laboratory, Boston, MA 02215."}]},{"@id":"https://cir.nii.ac.jp/crid/1380013170945474434","@type":"Researcher","foaf:name":[{"@value":"S D Freedman"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Cell and Molecular Biology, Charles A. Dana Research Institute, Thorndike Laboratory, Boston, MA 02215."}]},{"@id":"https://cir.nii.ac.jp/crid/1380013170945474436","@type":"Researcher","foaf:name":[{"@value":"H Yu"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Cell and Molecular Biology, Charles A. Dana Research Institute, Thorndike Laboratory, Boston, MA 02215."}]},{"@id":"https://cir.nii.ac.jp/crid/1380013170945474433","@type":"Researcher","foaf:name":[{"@value":"V P Sukhatme"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Cell and Molecular Biology, Charles A. Dana Research Institute, Thorndike Laboratory, Boston, MA 02215."}]},{"@id":"https://cir.nii.ac.jp/crid/1380013170945474435","@type":"Researcher","foaf:name":[{"@value":"G A Scheele"}],"jpcoar:affiliationName":[{"@value":"Laboratory of Cell and Molecular Biology, Charles A. Dana Research Institute, Thorndike Laboratory, Boston, MA 02215."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"}],"prism:publicationName":[{"@value":"Proceedings of the National Academy of Sciences"}],"dc:publisher":[{"@value":"Proceedings of the National Academy of Sciences"}],"prism:publicationDate":"1992-02-15","prism:volume":"89","prism:number":"4","prism:startingPage":"1189","prism:endingPage":"1193"},"reviewed":"false","url":[{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.89.4.1189"}],"createdAt":"2006-06-02","modifiedAt":"2022-04-13","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360004233415430912","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Transcription factor Spi-B–dependent and –independent pathways for the development of Peyer's patch M 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