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Article: Characterization of an arginine 789 to cysteine substitution in α1 (II) collagen chains of a patient with spondyloepiphyseal dysplasia

TitleCharacterization of an arginine 789 to cysteine substitution in α1 (II) collagen chains of a patient with spondyloepiphyseal dysplasia
Authors
Issue Date1993
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, 1993, v. 268 n. 20, p. 15238-15245 How to Cite?
AbstractA child with spondyloepiphyseal dysplasia congenita was shown to be heterozygous for a mutation of the COL2A1 gene that encodes the α1(II) chain of type II collagen. The α1(II) chains extracted from cartilage contained disulfide-bonded dimeric and trimeric α1(II) chains. Carboxymethylation confirmed that some of the type II collagen chains contained cysteine residues that are not normally present in α1(II) chains. Cyanogen bromide peptide mapping showed that the abnormal cysteine residue was located in the α1(II) CB10.5 peptide. Amplification products of the corresponding region of α1(II) cDNA prepared from cultured dermal fibroblasts were shown by chemical cleavage and single strand conformation polymorphism analyses to contain a sequence anomaly. DNA sequencing showed a transition of C2913T in exon 41 of one allele of the COL2A1 gene resulting in the substitution of arginine 789 by cysteine in the α1(II) chain. The mutation resulted in the loss of a MaeII cleavage site that was used to confirm that the proband was heterozygous for the mutation and that neither parent showed evidence of the mutation. The type II collagen extracted from cartilage and from chondrocytes cultured in alginate beads showed similar characteristics. Approximately a third of the type II collagen chains were mutant, and the secretion of molecules containing mutant chains was impaired. The thermal stability of the collagen extracted from cartilage was normal. This study confirmed the importance of dominant negative mutations of the COL2A1 gene in producing the spondyloepiphyseal dysplasia congenita phenotype.
Persistent Identifierhttp://hdl.handle.net/10722/147375
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, Den_US
dc.contributor.authorTaylor, TKFen_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:03:16Z-
dc.date.available2012-05-29T06:03:16Z-
dc.date.issued1993en_US
dc.identifier.citationJournal Of Biological Chemistry, 1993, v. 268 n. 20, p. 15238-15245en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147375-
dc.description.abstractA child with spondyloepiphyseal dysplasia congenita was shown to be heterozygous for a mutation of the COL2A1 gene that encodes the α1(II) chain of type II collagen. The α1(II) chains extracted from cartilage contained disulfide-bonded dimeric and trimeric α1(II) chains. Carboxymethylation confirmed that some of the type II collagen chains contained cysteine residues that are not normally present in α1(II) chains. Cyanogen bromide peptide mapping showed that the abnormal cysteine residue was located in the α1(II) CB10.5 peptide. Amplification products of the corresponding region of α1(II) cDNA prepared from cultured dermal fibroblasts were shown by chemical cleavage and single strand conformation polymorphism analyses to contain a sequence anomaly. DNA sequencing showed a transition of C2913T in exon 41 of one allele of the COL2A1 gene resulting in the substitution of arginine 789 by cysteine in the α1(II) chain. The mutation resulted in the loss of a MaeII cleavage site that was used to confirm that the proband was heterozygous for the mutation and that neither parent showed evidence of the mutation. The type II collagen extracted from cartilage and from chondrocytes cultured in alginate beads showed similar characteristics. Approximately a third of the type II collagen chains were mutant, and the secretion of molecules containing mutant chains was impaired. The thermal stability of the collagen extracted from cartilage was normal. This study confirmed the importance of dominant negative mutations of the COL2A1 gene in producing the spondyloepiphyseal dysplasia congenita phenotype.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.meshArginine - Geneticsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCartilage - Cytology - Metabolismen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshChild, Preschoolen_US
dc.subject.meshCollagen - Genetics - Metabolismen_US
dc.subject.meshCysteine - Geneticsen_US
dc.subject.meshDnaen_US
dc.subject.meshDna Mutational Analysisen_US
dc.subject.meshFemaleen_US
dc.subject.meshFibroblasts - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutationen_US
dc.subject.meshOsteochondrodysplasias - Congenital - Geneticsen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshSkin - Cytology - Metabolismen_US
dc.titleCharacterization of an arginine 789 to cysteine substitution in α1 (II) collagen chains of a patient with spondyloepiphyseal dysplasiaen_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.pmid8325895-
dc.identifier.scopuseid_2-s2.0-0027171315en_US
dc.identifier.volume268en_US
dc.identifier.issue20en_US
dc.identifier.spage15238en_US
dc.identifier.epage15245en_US
dc.identifier.isiWOS:A1993LL75900100-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridTaylor, TKF=7402298857en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

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