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Article: A structural mutation of the collagen α1(I)CB7 peptide in lethal perinatal osteogenesis imperfecta

TitleA structural mutation of the collagen α1(I)CB7 peptide in lethal perinatal osteogenesis imperfecta
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. 10, p. 4445-4451 How to Cite?
AbstractStructurally abnormal type I collagen was identified in the dermis, bone, and cultured fibroblasts obtained from a baby with 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. This heterozygous peptide defect was not detected in the collagens from either parent. The defect was localized to a 224-residue region at the NH2 terminus of the α1(I)CB7 peptide by mammalian collagenase digestion. Analysis of unhydroxylated collagens produced in cell culture indicated that the mutant α1(I)CB7 migrated faster on electrophoresis suggesting that the abnormality may be a small deletion or a mutation that alters sodium dodecyl sulfate binding. The post-translational hydroxylation of lysine residues was increased in the CB7 peptide and also in peptides CB3 and CB8 which are toward the NH2 terminus of the α1(I)-chain. The COOH-terminal CB6 peptide was normally hydroxylated. These findings support the proposal that the lysine overhydroxylation resulted from a perturbation of helix propagation from the COOH to NH2 terminus of the collagen trimer caused by the structural defect in α1(I)CB7.
Persistent Identifierhttp://hdl.handle.net/10722/147322
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.authorMascara, Ten_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_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. 10, p. 4445-4451en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147322-
dc.description.abstractStructurally abnormal type I collagen was identified in the dermis, bone, and cultured fibroblasts obtained from a baby with 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. This heterozygous peptide defect was not detected in the collagens from either parent. The defect was localized to a 224-residue region at the NH2 terminus of the α1(I)CB7 peptide by mammalian collagenase digestion. Analysis of unhydroxylated collagens produced in cell culture indicated that the mutant α1(I)CB7 migrated faster on electrophoresis suggesting that the abnormality may be a small deletion or a mutation that alters sodium dodecyl sulfate binding. The post-translational hydroxylation of lysine residues was increased in the CB7 peptide and also in peptides CB3 and CB8 which are toward the NH2 terminus of the α1(I)-chain. The COOH-terminal CB6 peptide was normally hydroxylated. These findings support the proposal that the lysine overhydroxylation resulted from a perturbation of helix propagation from the COOH to NH2 terminus of the collagen trimer caused by the structural defect in α1(I)CB7.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.meshCollagen - Genetics - Isolation & Purificationen_US
dc.subject.meshCyanogen Bromideen_US
dc.subject.meshFemaleen_US
dc.subject.meshHumansen_US
dc.subject.meshHydroxylysine - Metabolismen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshIsoelectric Pointen_US
dc.subject.meshMutationen_US
dc.subject.meshOsteogenesis Imperfecta - Genetics - Metabolismen_US
dc.subject.meshPeptide Fragments - Isolation & Purificationen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.titleA structural mutation of the collagen α1(I)CB7 peptide in lethal perinatal osteogenesis imperfectaen_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.pmid3558348-
dc.identifier.scopuseid_2-s2.0-0023178378en_US
dc.identifier.volume262en_US
dc.identifier.issue10en_US
dc.identifier.spage4445en_US
dc.identifier.epage4451en_US
dc.identifier.isiWOS:A1987G695300005-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridMascara, T=6602227390en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

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