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Article: Collagen defects in lethal perinatal osteogenesis imperfecta

TitleCollagen defects in lethal perinatal osteogenesis imperfecta
Authors
Issue Date1986
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1986, v. 240 n. 3, p. 699-708 How to Cite?
AbstractQuantitative and qualitative abnormalities of collagen were observed in tissues and fibroblast cultures from 17 consecutive cases of lethal perinatal osteogenesis imperfecta (OI). The content of type I collagen was reduced in OI dermis and bone and the content of type II collagen was also reduced in the dermis. Normal bone contained 99.3% type I and 0.7% type V collagen whereas OI bone contained a lower proportion of type I, a greater proportion of type V and a significant amount of type III collagen. The type III and V collagens appeared to be structurally normal. In contrast, abnormal type I collagen chains, which migrated slowly on electrophoresis, were observed in all babies with OI. Cultured fibroblasts from five babies produced a mixture of normal and abnormal type I collagens; the abnormal collagen was not secreted in two cases and was slowly secreted in the others. Fibroblasts from 12 babies produced only abnormal type I collagens and they were also secreted slowly. The slower electrophoretic migration of the abnormal chains was due to enzymic overmodification of the lysine residues. The distribution of the cyanogen bromide peptides containing the overmodified residues was used to localize the underlying structural abnormalities to three regions of the type I procollagen chains. These regions included the carboxy-propeptide of the proα1(I)-chain, the helical α1(I) CB7 peptide and the helical α1(I) CB8 and CB3 peptides. In one baby a basic charge mutation was observed in the α1(I) CB7 peptide and in another baby a basic charge mutation was observed in the α1(I) CB8 peptide. The primary defects in lethal perinatal OI appear to reside in the type I collagen chains. Type III and V collagens did not appear to compensate for the deficiency of type I collagen in the tissues.
Persistent Identifierhttp://hdl.handle.net/10722/147318
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBateman, JFen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorMascara, Ten_US
dc.date.accessioned2012-05-29T06:02:53Z-
dc.date.available2012-05-29T06:02:53Z-
dc.date.issued1986en_US
dc.identifier.citationBiochemical Journal, 1986, v. 240 n. 3, p. 699-708en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttp://hdl.handle.net/10722/147318-
dc.description.abstractQuantitative and qualitative abnormalities of collagen were observed in tissues and fibroblast cultures from 17 consecutive cases of lethal perinatal osteogenesis imperfecta (OI). The content of type I collagen was reduced in OI dermis and bone and the content of type II collagen was also reduced in the dermis. Normal bone contained 99.3% type I and 0.7% type V collagen whereas OI bone contained a lower proportion of type I, a greater proportion of type V and a significant amount of type III collagen. The type III and V collagens appeared to be structurally normal. In contrast, abnormal type I collagen chains, which migrated slowly on electrophoresis, were observed in all babies with OI. Cultured fibroblasts from five babies produced a mixture of normal and abnormal type I collagens; the abnormal collagen was not secreted in two cases and was slowly secreted in the others. Fibroblasts from 12 babies produced only abnormal type I collagens and they were also secreted slowly. The slower electrophoretic migration of the abnormal chains was due to enzymic overmodification of the lysine residues. The distribution of the cyanogen bromide peptides containing the overmodified residues was used to localize the underlying structural abnormalities to three regions of the type I procollagen chains. These regions included the carboxy-propeptide of the proα1(I)-chain, the helical α1(I) CB7 peptide and the helical α1(I) CB8 and CB3 peptides. In one baby a basic charge mutation was observed in the α1(I) CB7 peptide and in another baby a basic charge mutation was observed in the α1(I) CB8 peptide. The primary defects in lethal perinatal OI appear to reside in the type I collagen chains. Type III and V collagens did not appear to compensate for the deficiency of type I collagen in the tissues.en_US
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_US
dc.relation.ispartofBiochemical Journalen_US
dc.subject.meshBone And Bones - Analysisen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshChromatography, High Pressure Liquiden_US
dc.subject.meshCollagen - Analysis - Metabolismen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFibroblasts - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshOsteogenesis Imperfecta - Congenital - Metabolismen_US
dc.subject.meshPeptide Fragments - Analysisen_US
dc.subject.meshSkin - Analysisen_US
dc.titleCollagen defects 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.pmid3827862en_US
dc.identifier.scopuseid_2-s2.0-0022894942en_US
dc.identifier.volume240en_US
dc.identifier.issue3en_US
dc.identifier.spage699en_US
dc.identifier.epage708en_US
dc.identifier.isiWOS:A1986F269900010-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridMascara, T=6602227390en_US

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