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Article: Substitution of arginine for glycine 664 in the collagen α1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA

TitleSubstitution of arginine for glycine 664 in the collagen α1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA
Authors
Issue Date1988
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1988, v. 263 n. 24, p. 11627-11630 How to Cite?
AbstractStructurally abnormal type I collagen was identified in tissues and cultured fibroblasts from a case of lethal perinatal osteogenesis imperfecta. Two-dimensional gel electrophoresis of the CNBr peptides demonstrated that the α1(I)CB7 peptide from the α1(I) chain of type I collagen existed in a normal form and a mutant form with a more basic charge distribution (Bateman, J.F., Mascara, T., Chan, D., and Cole, W.G. (1987) J. Biol. Chem. 262, 4445-4451). Sequencing of cloned α1(I) cDNAs prepared using mRNA from the patient's fibroblasts demonstrated that one clone had a single base substitution of A for G which resulted in the substitution of arginine for glycine 664 within the α1(I)CB7 peptide. To determine whether this mutation was responsible for the peptide map abnormality, in vitro transcription of mRNA from the mutant cDNA was performed using an SP6 vector system. The mRNA was then translated into mutant protein in a rabbit reticulocyte lysate. Peptide analysis of the protein produced from the mutant cDNA demonstrated the same altered charge distribution of the α1(I)CB7 peptide as observed with tissue- and cell-derived mutant collagen peptides. This finding confirmed that the arginine for glycine 664 sequence abnormality defined in the cDNA clone was the mutation causing the observed protein peptide map defect. This mutation is consistent with the functional abnormalities of collagen observed in this case such as reduced helical stability, reduced secretion, increased degradation, and excessive posttranslational modification of lysine.
Persistent Identifierhttp://hdl.handle.net/10722/147328
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBateman, JFen_US
dc.contributor.authorLamande, SRen_US
dc.contributor.authorDahl, HHMen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:02:57Z-
dc.date.available2012-05-29T06:02:57Z-
dc.date.issued1988en_US
dc.identifier.citationJournal Of Biological Chemistry, 1988, v. 263 n. 24, p. 11627-11630en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147328-
dc.description.abstractStructurally abnormal type I collagen was identified in tissues and cultured fibroblasts from a case of lethal perinatal osteogenesis imperfecta. Two-dimensional gel electrophoresis of the CNBr peptides demonstrated that the α1(I)CB7 peptide from the α1(I) chain of type I collagen existed in a normal form and a mutant form with a more basic charge distribution (Bateman, J.F., Mascara, T., Chan, D., and Cole, W.G. (1987) J. Biol. Chem. 262, 4445-4451). Sequencing of cloned α1(I) cDNAs prepared using mRNA from the patient's fibroblasts demonstrated that one clone had a single base substitution of A for G which resulted in the substitution of arginine for glycine 664 within the α1(I)CB7 peptide. To determine whether this mutation was responsible for the peptide map abnormality, in vitro transcription of mRNA from the mutant cDNA was performed using an SP6 vector system. The mRNA was then translated into mutant protein in a rabbit reticulocyte lysate. Peptide analysis of the protein produced from the mutant cDNA demonstrated the same altered charge distribution of the α1(I)CB7 peptide as observed with tissue- and cell-derived mutant collagen peptides. This finding confirmed that the arginine for glycine 664 sequence abnormality defined in the cDNA clone was the mutation causing the observed protein peptide map defect. This mutation is consistent with the functional abnormalities of collagen observed in this case such as reduced helical stability, reduced secretion, increased degradation, and excessive posttranslational modification of lysine.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshArginineen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCollagen - Geneticsen_US
dc.subject.meshDna - Geneticsen_US
dc.subject.meshDna, Recombinanten_US
dc.subject.meshGlycineen_US
dc.subject.meshHumansen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutationen_US
dc.subject.meshOsteogenesis Imperfecta - Geneticsen_US
dc.subject.meshProtein Biosynthesisen_US
dc.subject.meshTranscription, Geneticen_US
dc.titleSubstitution of arginine for glycine 664 in the collagen α1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNAen_US
dc.typeArticleen_US
dc.identifier.emailChan, D:chand@hkucc.hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid3403550-
dc.identifier.scopuseid_2-s2.0-0023685746en_US
dc.identifier.volume263en_US
dc.identifier.issue24en_US
dc.identifier.spage11627en_US
dc.identifier.epage11630en_US
dc.identifier.isiWOS:A1988P765000006-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridLamande, SR=7004500719en_US
dc.identifier.scopusauthoridDahl, HHM=7101725390en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

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