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Article: Lethal perinatal osteogenesis imperfecta due to a type I collagen α2(I) gly to arg substitution detected by chemical cleavage of an mRNA:cDNA sequence mismatch

TitleLethal perinatal osteogenesis imperfecta due to a type I collagen α2(I) gly to arg substitution detected by chemical cleavage of an mRNA:cDNA sequence mismatch
Authors
Issue Date1992
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/38515
Citation
Human Mutation, 1992, v. 1 n. 1, p. 55-62 How to Cite?
AbstractA single base mismatch was detected by a chemical cleavage method in heteroduplexes formed between patient mRNA and a control collagen α2(I) cDNA probe in a case of osteogenesis imperfecta type II. The region of the mRNA mismatch was amplified using the polymerase chain reaction, cloned and sequenced. A heterozygous point mutation of G to C at base pair 1,774 of the collagen α2(I) mRNA resulted in the substitution of glycine with arginine at amino acid position 457 of the helix. Type I collagen of α1(I)- and α2(I)-chains from the patient migrated slowly on electrophoresis due to increased levels of posttranslational modification of lysine. The parents' fibroblast collagen did not contain the mRNA mismatch and the collagens showed normal electrophoretic behaviour. Two-dimensional electrophoresis of the CNBr peptides from the patient's collagen confirmed the excessive posttranslational modification of the α1(I)- and α2(I)-chains in the CNBr peptides N-terminal to the mutation due to disruption of the obligatory Gly-X-Y triplet repeat of the helix. The mutation led to reduced procollagen secretion and helix destabilization as evidenced by a decreased thermal stability. These data lend further support to the accumulating evidence that type I collagen α2(I) glycine substitution mutations result in the same spectrum of clinical severity as those in the α1(I)-chain. The disruptive effect of the glycine mutations seems to be largely dependent on the nature of the substituted amino acid, the position in the α-chain of the mutation, and the nature of the local surrounding amino acid sequence, rather than whether the mutation resides in the α1(I)- or α2(I)-chain. © 1992 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/147372
ISSN
2015 Impact Factor: 5.089
2015 SCImago Journal Rankings: 3.670
References

 

DC FieldValueLanguage
dc.contributor.authorBateman, JFen_US
dc.contributor.authorMoeller, Ien_US
dc.contributor.authorHannagan, Men_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:03:14Z-
dc.date.available2012-05-29T06:03:14Z-
dc.date.issued1992en_US
dc.identifier.citationHuman Mutation, 1992, v. 1 n. 1, p. 55-62en_US
dc.identifier.issn1059-7794en_US
dc.identifier.urihttp://hdl.handle.net/10722/147372-
dc.description.abstractA single base mismatch was detected by a chemical cleavage method in heteroduplexes formed between patient mRNA and a control collagen α2(I) cDNA probe in a case of osteogenesis imperfecta type II. The region of the mRNA mismatch was amplified using the polymerase chain reaction, cloned and sequenced. A heterozygous point mutation of G to C at base pair 1,774 of the collagen α2(I) mRNA resulted in the substitution of glycine with arginine at amino acid position 457 of the helix. Type I collagen of α1(I)- and α2(I)-chains from the patient migrated slowly on electrophoresis due to increased levels of posttranslational modification of lysine. The parents' fibroblast collagen did not contain the mRNA mismatch and the collagens showed normal electrophoretic behaviour. Two-dimensional electrophoresis of the CNBr peptides from the patient's collagen confirmed the excessive posttranslational modification of the α1(I)- and α2(I)-chains in the CNBr peptides N-terminal to the mutation due to disruption of the obligatory Gly-X-Y triplet repeat of the helix. The mutation led to reduced procollagen secretion and helix destabilization as evidenced by a decreased thermal stability. These data lend further support to the accumulating evidence that type I collagen α2(I) glycine substitution mutations result in the same spectrum of clinical severity as those in the α1(I)-chain. The disruptive effect of the glycine mutations seems to be largely dependent on the nature of the substituted amino acid, the position in the α-chain of the mutation, and the nature of the local surrounding amino acid sequence, rather than whether the mutation resides in the α1(I)- or α2(I)-chain. © 1992 Wiley-Liss, Inc.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/38515en_US
dc.relation.ispartofHuman Mutationen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshArginineen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshCollagen - Biosynthesis - Chemistry - Geneticsen_US
dc.subject.meshDna - Chemistry - Geneticsen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFemaleen_US
dc.subject.meshFibroblasts - Metabolismen_US
dc.subject.meshGenes, Lethalen_US
dc.subject.meshGlycineen_US
dc.subject.meshHumansen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNucleic Acid Heteroduplexes - Chemistry - Geneticsen_US
dc.subject.meshOligodeoxyribonucleotidesen_US
dc.subject.meshOsteogenesis Imperfecta - Geneticsen_US
dc.subject.meshPeptide Fragments - Isolation & Purificationen_US
dc.subject.meshPoint Mutationen_US
dc.subject.meshPolymerase Chain Reaction - Methodsen_US
dc.subject.meshRna - Isolation & Purificationen_US
dc.subject.meshRna, Messenger - Chemistry - Geneticsen_US
dc.titleLethal perinatal osteogenesis imperfecta due to a type I collagen α2(I) gly to arg substitution detected by chemical cleavage of an mRNA:cDNA sequence mismatchen_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.pmid1284475-
dc.identifier.scopuseid_2-s2.0-0027026419en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0027026419&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume1en_US
dc.identifier.issue1en_US
dc.identifier.spage55en_US
dc.identifier.epage62en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridMoeller, I=7004124283en_US
dc.identifier.scopusauthoridHannagan, M=6507095190en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

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