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Article: Characterization of an insulin-like growth factor binding protein (IGFBP-4) produced by the B104 rat neuronal cell line: Chemical and biological properties and differential synthesis by sublines

TitleCharacterization of an insulin-like growth factor binding protein (IGFBP-4) produced by the B104 rat neuronal cell line: Chemical and biological properties and differential synthesis by sublines
Authors
Issue Date1991
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 1991, v. 129 n. 2, p. 1006-1015 How to Cite?
AbstractA previous report from our laboratory described an approximately 30 kilodalton (kDa) insulin-like growth factor binding protein (IGFBP) that inhibited the binding of insulin-like growth factor I (IGF-I) by its receptor and was secreted by a subline of the B104 rat neuronal cell line. To better understand the biology of this IGFBP, it was purified from media conditioned by these B104 cells, and the chemical and biological properties of the protein were examined. The IGFBP existed as a 24 kDa form and a 28 kDa form when the conditioned media were analyzed by ligand blot. Deglycosylation studies indicated the 28 kDa species was the N-linked glycosylated form of the 24 kDa IGFBP. Multiple forms at both mol wts were found using two-dimensional electrophoresis, suggesting that there were posttranslational modifications in addition to glycosylation. The amino acid sequence of the 12 amino-terminal residues was identical to that of rat IGFBP-4. Increased synthesis of IGFBP-4 by the subline contrasted with negligible production by other B104 cells. Blot hybridization with rat IGFBP-4 complementary DNA showed differential expression of a 2.6 kilobase transcript among B104 cell lines that correlated with quantities of IGFBP-4 secreted in media. The difference persisted when the cells were xenografted into athymic nude mice. Purified IGFPB-4 inhibited the binding of [ 125I]IGF-I by its receptor and blunted stimulation of [ 3H]thymidine incorporation by IGF-I. These findings suggest a role for IGFBP-4 in neural cell function and indicate the B104 cell lines may be a useful model for further examination of IGFBP-4 biology.
Persistent Identifierhttp://hdl.handle.net/10722/170249
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCheung, PTen_US
dc.contributor.authorSmith, EPen_US
dc.contributor.authorShimasaki, Sen_US
dc.contributor.authorLing, Nen_US
dc.contributor.authorChernausek, SDen_US
dc.date.accessioned2012-10-30T06:06:57Z-
dc.date.available2012-10-30T06:06:57Z-
dc.date.issued1991en_US
dc.identifier.citationEndocrinology, 1991, v. 129 n. 2, p. 1006-1015en_US
dc.identifier.issn0013-7227en_US
dc.identifier.urihttp://hdl.handle.net/10722/170249-
dc.description.abstractA previous report from our laboratory described an approximately 30 kilodalton (kDa) insulin-like growth factor binding protein (IGFBP) that inhibited the binding of insulin-like growth factor I (IGF-I) by its receptor and was secreted by a subline of the B104 rat neuronal cell line. To better understand the biology of this IGFBP, it was purified from media conditioned by these B104 cells, and the chemical and biological properties of the protein were examined. The IGFBP existed as a 24 kDa form and a 28 kDa form when the conditioned media were analyzed by ligand blot. Deglycosylation studies indicated the 28 kDa species was the N-linked glycosylated form of the 24 kDa IGFBP. Multiple forms at both mol wts were found using two-dimensional electrophoresis, suggesting that there were posttranslational modifications in addition to glycosylation. The amino acid sequence of the 12 amino-terminal residues was identical to that of rat IGFBP-4. Increased synthesis of IGFBP-4 by the subline contrasted with negligible production by other B104 cells. Blot hybridization with rat IGFBP-4 complementary DNA showed differential expression of a 2.6 kilobase transcript among B104 cell lines that correlated with quantities of IGFBP-4 secreted in media. The difference persisted when the cells were xenografted into athymic nude mice. Purified IGFPB-4 inhibited the binding of [ 125I]IGF-I by its receptor and blunted stimulation of [ 3H]thymidine incorporation by IGF-I. These findings suggest a role for IGFBP-4 in neural cell function and indicate the B104 cell lines may be a useful model for further examination of IGFBP-4 biology.en_US
dc.languageengen_US
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_US
dc.relation.ispartofEndocrinologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAmino Acids - Analysisen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCarrier Proteins - Biosynthesis - Chemistry - Geneticsen_US
dc.subject.meshDna - Geneticsen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshInsulin-Like Growth Factor Binding Protein 4en_US
dc.subject.meshInsulin-Like Growth Factor I - Metabolism - Pharmacologyen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshNeuroblastomaen_US
dc.subject.meshNeurons - Metabolismen_US
dc.subject.meshNucleic Acid Hybridizationen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.subject.meshRna, Messenger - Analysisen_US
dc.subject.meshRatsen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.titleCharacterization of an insulin-like growth factor binding protein (IGFBP-4) produced by the B104 rat neuronal cell line: Chemical and biological properties and differential synthesis by sublinesen_US
dc.typeArticleen_US
dc.identifier.emailCheung, PT:ptcheung@hkucc.hku.hken_US
dc.identifier.authorityCheung, PT=rp00351en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1210/endo-129-2-1006-
dc.identifier.pmid1713156-
dc.identifier.scopuseid_2-s2.0-0026050994en_US
dc.identifier.volume129en_US
dc.identifier.issue2en_US
dc.identifier.spage1006en_US
dc.identifier.epage1015en_US
dc.identifier.isiWOS:A1991FY23400061-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridCheung, PT=7202595465en_US
dc.identifier.scopusauthoridSmith, EP=7408615693en_US
dc.identifier.scopusauthoridShimasaki, S=7005188303en_US
dc.identifier.scopusauthoridLing, N=35500564400en_US
dc.identifier.scopusauthoridChernausek, SD=7005403226en_US

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