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Article: Abnormal type I collagen metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta

TitleAbnormal type I collagen metabolism by cultured fibroblasts in lethal perinatal osteogenesis imperfecta
Authors
Issue Date1984
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1984, v. 217 n. 1, p. 103-115 How to Cite?
AbstractCultured skin fibroblasts from seven consecutive cases of lethal perinatal osteogenesis imperfecta (OI) expressed defects of type I collagen metabolism. The secretion of [14C]proline-labelled collagen by the OI cells was specifically reduced (51-79% of control), and collagen degradation was increased to twice that of control cells in five cases and increased by approx. 30% in the other two cases. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that four of the OI cell lines produced two forms of type I collagen consisting of both normally and slowly migrating forms of the α1(I)- and α2(I)-chains. In the other three OI cell lines only the 'slow' α(I)'- and α2(I)'-chains were detected. In both groups inhibition of the post-translational modifications of proline and lysine resulted in the production of a single species of type I collagen with normal electrophoretic migration. Proline hydroxylation was normal, but the hydroxylysine contents of α1(I)'- and α2(I)'-chains purified by h.p.l.c. were greater than in control α-chains. The glucosylgalactosylhydroxylysine content was increased approx. 3-fold while the galactosylhydroxylysine content was only slightly increased in the α1(I)'-chains relative to control α1(I)-chains. Peptide mapping of the CNBr-cleavage peptides provided evidence that the increased post-translational modifications were distributed throughout the α1(I)'- and α2(I)'-chains. It is postulated that the greater modification of these chains was due to structural defects of the α-chains leading to delayed helix formation. The abnormal charge heterogeneity observed in the α1 CB8 peptide of one patient may reflect such a structural defect in the type I collagen molecule.
Persistent Identifierhttp://hdl.handle.net/10722/147311
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.authorMascara, Ten_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:02:51Z-
dc.date.available2012-05-29T06:02:51Z-
dc.date.issued1984en_US
dc.identifier.citationBiochemical Journal, 1984, v. 217 n. 1, p. 103-115en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttp://hdl.handle.net/10722/147311-
dc.description.abstractCultured skin fibroblasts from seven consecutive cases of lethal perinatal osteogenesis imperfecta (OI) expressed defects of type I collagen metabolism. The secretion of [14C]proline-labelled collagen by the OI cells was specifically reduced (51-79% of control), and collagen degradation was increased to twice that of control cells in five cases and increased by approx. 30% in the other two cases. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that four of the OI cell lines produced two forms of type I collagen consisting of both normally and slowly migrating forms of the α1(I)- and α2(I)-chains. In the other three OI cell lines only the 'slow' α(I)'- and α2(I)'-chains were detected. In both groups inhibition of the post-translational modifications of proline and lysine resulted in the production of a single species of type I collagen with normal electrophoretic migration. Proline hydroxylation was normal, but the hydroxylysine contents of α1(I)'- and α2(I)'-chains purified by h.p.l.c. were greater than in control α-chains. The glucosylgalactosylhydroxylysine content was increased approx. 3-fold while the galactosylhydroxylysine content was only slightly increased in the α1(I)'-chains relative to control α1(I)-chains. Peptide mapping of the CNBr-cleavage peptides provided evidence that the increased post-translational modifications were distributed throughout the α1(I)'- and α2(I)'-chains. It is postulated that the greater modification of these chains was due to structural defects of the α-chains leading to delayed helix formation. The abnormal charge heterogeneity observed in the α1 CB8 peptide of one patient may reflect such a structural defect in the type I collagen molecule.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.meshCells, Cultureden_US
dc.subject.meshChromatography, High Pressure Liquiden_US
dc.subject.meshCollagen - Metabolismen_US
dc.subject.meshCyanogen Bromideen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFibroblasts - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshLysine - Metabolismen_US
dc.subject.meshOsteogenesis Imperfecta - Congenital - Metabolismen_US
dc.subject.meshPeptide Fragments - Analysisen_US
dc.subject.meshProcollagen - Metabolismen_US
dc.subject.meshProline - Metabolismen_US
dc.subject.meshProtein Biosynthesisen_US
dc.subject.meshSkin - Metabolismen_US
dc.titleAbnormal type I collagen metabolism by cultured fibroblasts 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.pmid6421277-
dc.identifier.scopuseid_2-s2.0-0021352121en_US
dc.identifier.volume217en_US
dc.identifier.issue1en_US
dc.identifier.spage103en_US
dc.identifier.epage115en_US
dc.identifier.isiWOS:A1984RY97000010-
dc.publisher.placeUnited Kingdomen_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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