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Article: Lethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the α1(I) chain of type I collagen

TitleLethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the α1(I) chain of type I collagen
Authors
Issue Date1987
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, 1987, v. 262 n. 15, p. 7021-7027 How to Cite?
AbstractA baby with the lethal perinatal form of osteogenesis imperfecta was shown to have a structural defect in the α1(I) chain of type I procollagen. Normal and mutant α1(I) CB8 cyanogen bromide peptides, from the helical part of the α1(I) chains, were purified from bone. Amino acid sequencing of tryptic peptides derived from the mutant α1(I) CB8 peptide showed that the glycine residue at position 391 of the α1(I) chain had been replaced by an arginine residue. This substitution accounted for the more basic charged form of this peptide that was observed on two-dimensional electrophoresis of the collagen peptides obtained from the tissues. The substitution was associated with increased enzymatic hydroxylation of lysine residues in the α1(I) CB8 and the adjoining CB3 peptides but not in the carboxyl-terminal CB6 and CB7 peptides. This finding suggested that the sequence abnormality had interfered with the propagation of the triple helix across the mutant region. The abnormal collagen was not incorporated into the more insoluble fraction of bone collagen. The baby appeared to be heterozygous for the sequence abnormality and as the parents did not show any evidence of the defect it is likely that the baby had a new mutation of one allele of the pro-α1(I) gene. The amino acid substitution could result from a single nucleotide mutation in the codon GGC (glycine) to produce the codon CGC (arginine).
Persistent Identifierhttp://hdl.handle.net/10722/147323
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.authorChan, Den_US
dc.contributor.authorWalker, IDen_US
dc.date.accessioned2012-05-29T06:02:55Z-
dc.date.available2012-05-29T06:02:55Z-
dc.date.issued1987en_US
dc.identifier.citationJournal Of Biological Chemistry, 1987, v. 262 n. 15, p. 7021-7027en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147323-
dc.description.abstractA baby with the lethal perinatal form of osteogenesis imperfecta was shown to have a structural defect in the α1(I) chain of type I procollagen. Normal and mutant α1(I) CB8 cyanogen bromide peptides, from the helical part of the α1(I) chains, were purified from bone. Amino acid sequencing of tryptic peptides derived from the mutant α1(I) CB8 peptide showed that the glycine residue at position 391 of the α1(I) chain had been replaced by an arginine residue. This substitution accounted for the more basic charged form of this peptide that was observed on two-dimensional electrophoresis of the collagen peptides obtained from the tissues. The substitution was associated with increased enzymatic hydroxylation of lysine residues in the α1(I) CB8 and the adjoining CB3 peptides but not in the carboxyl-terminal CB6 and CB7 peptides. This finding suggested that the sequence abnormality had interfered with the propagation of the triple helix across the mutant region. The abnormal collagen was not incorporated into the more insoluble fraction of bone collagen. The baby appeared to be heterozygous for the sequence abnormality and as the parents did not show any evidence of the defect it is likely that the baby had a new mutation of one allele of the pro-α1(I) gene. The amino acid substitution could result from a single nucleotide mutation in the codon GGC (glycine) to produce the codon CGC (arginine).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.meshBone And Bones - Analysisen_US
dc.subject.meshCollagen - Geneticsen_US
dc.subject.meshCyanogen Bromideen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFemaleen_US
dc.subject.meshGlycineen_US
dc.subject.meshHumansen_US
dc.subject.meshHydroxylationen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshLysine - Metabolismen_US
dc.subject.meshMutationen_US
dc.subject.meshOsteogenesis Imperfecta - Geneticsen_US
dc.subject.meshPeptide Fragmentsen_US
dc.subject.meshProcollagen - Geneticsen_US
dc.subject.meshTrypsinen_US
dc.titleLethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the α1(I) chain of type I collagenen_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.pmid3108247en_US
dc.identifier.scopuseid_2-s2.0-0023198485en_US
dc.identifier.volume262en_US
dc.identifier.issue15en_US
dc.identifier.spage7021en_US
dc.identifier.epage7027en_US
dc.identifier.isiWOS:A1987H414700017-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridWalker, ID=35601918000en_US

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