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Article: A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilage

TitleA COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilage
Authors
Issue Date1995
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, 1995, v. 270 n. 4, p. 1747-1753 How to Cite?
AbstractAn autosomal dominant mutation in the COL2A1 gene was identified in a fetus with achondrogenesis type II. A transition of G2853 to A in exon 41 produced a substitution of Gly769 by Ser within the triple helical domain of the α1(II) chain of type II collagen, interrupting the mandatory Gly-X-Y triplet sequence required for the normal formation of stable triple helical type II collagen molecules, resulting in the complete absence of type II collagen in the cartilage, which had a gelatinous composition. Type I and III collagens were the major species found in cartilage tissue and synthesized by cultured chondrocytes along with cartilage type XI collagen. However, cultured chondrocytes produced a trace amount of type II collagen, which was retained within the cells and not secreted. In situ hybridization of cartilage sections showed that the chondrocytes produced both type II and type I collagen mRNA. As a result, it is likely that the chondrocytes produced type II collagen molecules, which were then degraded. The close proximity of the Gly769 substitution by Ser to the mammalian collagenase cleavage site at Gly775-Leu776 may have produced an unstable domain that was highly susceptible to proteolysis. The type I and III collagens that replaced type II collagen were unable to maintain the normal structure of the hyaline cartilage but did support chondrocyte maturation, evidenced by the expression of type X collagen in the hypertrophic zone of the growth plate cartilage.
Persistent Identifierhttp://hdl.handle.net/10722/147395
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.authorCole, WGen_US
dc.contributor.authorChow, CWen_US
dc.contributor.authorMundlos, Sen_US
dc.contributor.authorBateman, JFen_US
dc.date.accessioned2012-05-29T06:03:25Z-
dc.date.available2012-05-29T06:03:25Z-
dc.date.issued1995en_US
dc.identifier.citationJournal Of Biological Chemistry, 1995, v. 270 n. 4, p. 1747-1753en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147395-
dc.description.abstractAn autosomal dominant mutation in the COL2A1 gene was identified in a fetus with achondrogenesis type II. A transition of G2853 to A in exon 41 produced a substitution of Gly769 by Ser within the triple helical domain of the α1(II) chain of type II collagen, interrupting the mandatory Gly-X-Y triplet sequence required for the normal formation of stable triple helical type II collagen molecules, resulting in the complete absence of type II collagen in the cartilage, which had a gelatinous composition. Type I and III collagens were the major species found in cartilage tissue and synthesized by cultured chondrocytes along with cartilage type XI collagen. However, cultured chondrocytes produced a trace amount of type II collagen, which was retained within the cells and not secreted. In situ hybridization of cartilage sections showed that the chondrocytes produced both type II and type I collagen mRNA. As a result, it is likely that the chondrocytes produced type II collagen molecules, which were then degraded. The close proximity of the Gly769 substitution by Ser to the mammalian collagenase cleavage site at Gly775-Leu776 may have produced an unstable domain that was highly susceptible to proteolysis. The type I and III collagens that replaced type II collagen were unable to maintain the normal structure of the hyaline cartilage but did support chondrocyte maturation, evidenced by the expression of type X collagen in the hypertrophic zone of the growth plate cartilage.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.meshAbortion, Induceden_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCollagen - Biosynthesis - Chemistry - Geneticsen_US
dc.subject.meshCollagen Diseases - Embryology - Genetics - Pathologyen_US
dc.subject.meshDna Primersen_US
dc.subject.meshExonsen_US
dc.subject.meshFemaleen_US
dc.subject.meshFetusen_US
dc.subject.meshGenes, Dominanten_US
dc.subject.meshGrowth Plate - Embryology - Metabolism - Pathologyen_US
dc.subject.meshHumansen_US
dc.subject.meshIn Situ Hybridizationen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPeptide Fragments - Chemistry - Isolation & Purificationen_US
dc.subject.meshPoint Mutationen_US
dc.subject.meshPolymerase Chain Reactionen_US
dc.subject.meshPregnancyen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshReference Valuesen_US
dc.titleA COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilageen_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.doi10.1074/jbc.270.4.1747en_US
dc.identifier.pmid7829510-
dc.identifier.scopuseid_2-s2.0-0028938776en_US
dc.identifier.volume270en_US
dc.identifier.issue4en_US
dc.identifier.spage1747en_US
dc.identifier.epage1753en_US
dc.identifier.isiWOS:A1995QD20400043-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.scopusauthoridChow, CW=7402578595en_US
dc.identifier.scopusauthoridMundlos, S=7005248176en_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US

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