File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: An α1(II) Gly913 to Cys substitution prevents the matrix incorporation of type II collagen which is replaced with type I and III collagens in cartilage from a patient with hypochondrogenesis

TitleAn α1(II) Gly913 to Cys substitution prevents the matrix incorporation of type II collagen which is replaced with type I and III collagens in cartilage from a patient with hypochondrogenesis
Authors
Issue Date1996
Citation
American Journal Of Medical Genetics - Seminars In Medical Genetics, 1996, v. 63 n. 1, p. 129-136 How to Cite?
AbstractA heterozygous mutation in the COL2A1 gene was identified in a patient with hypochondrogenesis. The mutation was a single nucleotide transition of G3285T that resulted in an amino acid substitution of Cys for Gly913 in the α1(II) chain of type II collagen. This amino acid change disrupted the obligatory Gly-X-Y triplet motif required for the normal formation of a stable collagen triple helix and prevented the deposition of type II collagen into the proposita's cartilage, which contained predominantly type I and III collagens and minor amounts of type XI collagen. Biosynthetic analysis of collagens produced and secreted by the patient's chondrocytes cultured in alginate beads was consistent with the in vivo matrix composition, demonstrating that the main products were type I and III collagens, along with type XI collagen. The synthesis of the cartilage-specific type XI collagen at similar levels to controls indicated that the isolated cartilage cells had re-differentiated to the chondrocyte phenotype. The chondrocytes also produced small amounts of type II collagen, but this was post-translationally overmodified and not secreted. These data further delineate the biochemical and phenotypic consequences of mutations in the COL2A1 gene and suggest that cartilage formation and bone development can take place in the absence of type II collagen. © 1996 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/147407
ISSN
2003 Impact Factor: -999.999
2009 SCImago Journal Rankings: 1.100
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMundlos, Sen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorMcgill, Jen_US
dc.contributor.authorBateman, JFen_US
dc.date.accessioned2012-05-29T06:03:30Z-
dc.date.available2012-05-29T06:03:30Z-
dc.date.issued1996en_US
dc.identifier.citationAmerican Journal Of Medical Genetics - Seminars In Medical Genetics, 1996, v. 63 n. 1, p. 129-136en_US
dc.identifier.issn0148-7299en_US
dc.identifier.urihttp://hdl.handle.net/10722/147407-
dc.description.abstractA heterozygous mutation in the COL2A1 gene was identified in a patient with hypochondrogenesis. The mutation was a single nucleotide transition of G3285T that resulted in an amino acid substitution of Cys for Gly913 in the α1(II) chain of type II collagen. This amino acid change disrupted the obligatory Gly-X-Y triplet motif required for the normal formation of a stable collagen triple helix and prevented the deposition of type II collagen into the proposita's cartilage, which contained predominantly type I and III collagens and minor amounts of type XI collagen. Biosynthetic analysis of collagens produced and secreted by the patient's chondrocytes cultured in alginate beads was consistent with the in vivo matrix composition, demonstrating that the main products were type I and III collagens, along with type XI collagen. The synthesis of the cartilage-specific type XI collagen at similar levels to controls indicated that the isolated cartilage cells had re-differentiated to the chondrocyte phenotype. The chondrocytes also produced small amounts of type II collagen, but this was post-translationally overmodified and not secreted. These data further delineate the biochemical and phenotypic consequences of mutations in the COL2A1 gene and suggest that cartilage formation and bone development can take place in the absence of type II collagen. © 1996 Wiley-Liss, Inc.en_US
dc.languageengen_US
dc.relation.ispartofAmerican Journal of Medical Genetics - Seminars in Medical Geneticsen_US
dc.subject.meshAdulten_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshCartilage - Metabolismen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshCollagen - Biosynthesis - Chemistry - Geneticsen_US
dc.subject.meshCysteineen_US
dc.subject.meshExtracellular Matrix - Metabolismen_US
dc.subject.meshFemaleen_US
dc.subject.meshGlycineen_US
dc.subject.meshHeterozygoteen_US
dc.subject.meshHumansen_US
dc.subject.meshInfant, Newbornen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshOsteochondrodysplasias - Genetics - Radiographyen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshPoint Mutationen_US
dc.subject.meshPolymerase Chain Reactionen_US
dc.subject.meshPolymorphism, Single-Stranded Conformationalen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshRna Processing, Post-Transcriptionalen_US
dc.titleAn α1(II) Gly913 to Cys substitution prevents the matrix incorporation of type II collagen which is replaced with type I and III collagens in cartilage from a patient with hypochondrogenesisen_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.pmid8723098-
dc.identifier.scopuseid_2-s2.0-0029870866en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0029870866&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume63en_US
dc.identifier.issue1en_US
dc.identifier.spage129en_US
dc.identifier.epage136en_US
dc.identifier.isiWOS:A1996UH93900023-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMundlos, S=7005248176en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridMcGill, J=8320808200en_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats