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Article: The human α2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization

TitleThe human α2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization
Authors
Issue Date1989
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, 1989, v. 264 n. 23, p. 13910-13916 How to Cite?
AbstractWe have isolated three overlapping cDNA clones encoding the proα2(XI) collagen chain from a human chondrocyte cDNA library. Together, the cDNAs code for 257 uninterrupted Gly-X-Y triplets (almost 80% of the triple helical domain) and about 200 amino acid residues of the carboxyl telopeptide and carboxyl propeptide. The identification of the clones as proα2(XI) cDNAs was based on the complete identity between the amino acid sequences of three tryptic peptides derived from human α2(XI) collagen and the cDNA-derived sequence. We have also sequenced six exons within a human genomic α2(XI) cosmid clone. This sequence shows that although type XI collagen belongs to the fibril-forming class of collagens, there are substantial differences in exon sizes at the 3' end of the gene when comparing the α2(XI) gene with those of human types I, II, and III collagens. Finally, proα2(XI) cDNA has been used as a probe to determine the location of the gene by in situ hybridization of chromosome spreads. The results demonstrate that the gene is located close to the region p212 on chromosome 6. Northern blot analysis shows that the gene is expressed in cartilage but not in adult liver, skin, and tendon.
Persistent Identifierhttp://hdl.handle.net/10722/147336
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKimura, Ten_HK
dc.contributor.authorCheah, KSEen_HK
dc.contributor.authorChan, SDHen_HK
dc.contributor.authorLui, VCHen_HK
dc.contributor.authorMattei, MGen_HK
dc.contributor.authorVan Der Rest, Men_HK
dc.contributor.authorOno, Ken_HK
dc.contributor.authorSolomon, Een_HK
dc.contributor.authorNinomiya, Yen_HK
dc.contributor.authorOlsen, BRen_HK
dc.date.accessioned2012-05-29T06:03:00Z-
dc.date.available2012-05-29T06:03:00Z-
dc.date.issued1989en_HK
dc.identifier.citationJournal Of Biological Chemistry, 1989, v. 264 n. 23, p. 13910-13916en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/147336-
dc.description.abstractWe have isolated three overlapping cDNA clones encoding the proα2(XI) collagen chain from a human chondrocyte cDNA library. Together, the cDNAs code for 257 uninterrupted Gly-X-Y triplets (almost 80% of the triple helical domain) and about 200 amino acid residues of the carboxyl telopeptide and carboxyl propeptide. The identification of the clones as proα2(XI) cDNAs was based on the complete identity between the amino acid sequences of three tryptic peptides derived from human α2(XI) collagen and the cDNA-derived sequence. We have also sequenced six exons within a human genomic α2(XI) cosmid clone. This sequence shows that although type XI collagen belongs to the fibril-forming class of collagens, there are substantial differences in exon sizes at the 3' end of the gene when comparing the α2(XI) gene with those of human types I, II, and III collagens. Finally, proα2(XI) cDNA has been used as a probe to determine the location of the gene by in situ hybridization of chromosome spreads. The results demonstrate that the gene is located close to the region p212 on chromosome 6. Northern blot analysis shows that the gene is expressed in cartilage but not in adult liver, skin, and tendon.en_HK
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_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCartilage, Articular - Metabolismen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshChromosome Mappingen_US
dc.subject.meshChromosomes, Human, Pair 6en_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshCollagen - Geneticsen_US
dc.subject.meshCosmidsen_US
dc.subject.meshDna - Geneticsen_US
dc.subject.meshExonsen_US
dc.subject.meshGenesen_US
dc.subject.meshHumansen_US
dc.subject.meshKaryotypingen_US
dc.subject.meshMacromolecular Substancesen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshProcollagen - Geneticsen_US
dc.subject.meshSequence Homology, Nucleic Aciden_US
dc.titleThe human α2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organizationen_HK
dc.typeArticleen_HK
dc.identifier.emailCheah, KSE: hrmbdkc@hku.hken_HK
dc.identifier.emailLui, VCH: vchlui@hkucc.hku.hken_HK
dc.identifier.authorityCheah, KSE=rp00342en_HK
dc.identifier.authorityLui, VCH=rp00363en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid2760050-
dc.identifier.scopuseid_2-s2.0-0024356083en_HK
dc.identifier.volume264en_HK
dc.identifier.issue23en_HK
dc.identifier.spage13910en_HK
dc.identifier.epage13916en_HK
dc.identifier.isiWOS:A1989AK17900085-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKimura, T=7405708537en_HK
dc.identifier.scopusauthoridCheah, KSE=35387746200en_HK
dc.identifier.scopusauthoridChan, SDH=7404255758en_HK
dc.identifier.scopusauthoridLui, VCH=7004231344en_HK
dc.identifier.scopusauthoridMattei, MG=36049369100en_HK
dc.identifier.scopusauthoridVan Der Rest, M=7005803336en_HK
dc.identifier.scopusauthoridOno, K=7403887499en_HK
dc.identifier.scopusauthoridSolomon, E=7201615395en_HK
dc.identifier.scopusauthoridNinomiya, Y=7201658687en_HK
dc.identifier.scopusauthoridOlsen, BR=35403161200en_HK

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