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Article: Extensive alternative splicing within the amino-propeptide coding domain of α2(XI) procollagen mRNAs: Expression of transcripts encoding truncated pro-α chains

TitleExtensive alternative splicing within the amino-propeptide coding domain of α2(XI) procollagen mRNAs: Expression of transcripts encoding truncated pro-α chains
Authors
Issue Date1996
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, 1996, v. 271 n. 28, p. 16945-16951 How to Cite?
AbstractHeterogeneity in type XI procollagen structure is extensive because all three α(XI) collagen genes undergo complex alternative splicing within the amino-propeptide coding domain. Exon 7 of the human and exons 6-8 of the mouse α2(XI) collagen genes, encoding part of the amino-propeptide variable region, have recently been shown to be alternatively spliced. We show that exon 6-containing mRNAs for human α2(XI) procollagen are expressed at 28 weeks in fetal tendon and cartilage but not at 38-44 days or 11 weeks. In the mouse, exon 6 is expressed in chondrocytes from 13.5 days onward. We recently identified conserved sequences within intron 6 of the human and mouse α2(XI) collagen genes, containing additional consensus splice acceptor and donor sites that potentially increase the size of exon 7, dividing it into three parts, designated 7A, 7B, and 7C. We show by reverse transcription polymerase chain reaction and in situ hybridization that these potential splice sites are used to yield additional α2(XI) procollagen mRNA splice variants that are expressed in fetal tissues. In human, expression of exon 7B-containing transcripts may be developmental stage-specific. Interestingly, inclusion of exon 7A or exon 7B in human and mouse α2(XI) procollagen mRNAs, respectively, would result in the insertion of an in-frame termination codon, suggesting that some of the additional splice variants encode a truncated pro-α2(XI) chain.
Persistent Identifierhttp://hdl.handle.net/10722/48967
ISSN
2020 Impact Factor: 5.157
2023 SCImago Journal Rankings: 1.766
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLui, VCHen_HK
dc.contributor.authorNg, LJen_HK
dc.contributor.authorSat, EWYen_HK
dc.contributor.authorNicholls, Jen_HK
dc.contributor.authorCheah, KSEen_HK
dc.date.accessioned2008-06-12T06:30:59Z-
dc.date.available2008-06-12T06:30:59Z-
dc.date.issued1996en_HK
dc.identifier.citationJournal of Biological Chemistry, 1996, v. 271 n. 28, p. 16945-16951en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48967-
dc.description.abstractHeterogeneity in type XI procollagen structure is extensive because all three α(XI) collagen genes undergo complex alternative splicing within the amino-propeptide coding domain. Exon 7 of the human and exons 6-8 of the mouse α2(XI) collagen genes, encoding part of the amino-propeptide variable region, have recently been shown to be alternatively spliced. We show that exon 6-containing mRNAs for human α2(XI) procollagen are expressed at 28 weeks in fetal tendon and cartilage but not at 38-44 days or 11 weeks. In the mouse, exon 6 is expressed in chondrocytes from 13.5 days onward. We recently identified conserved sequences within intron 6 of the human and mouse α2(XI) collagen genes, containing additional consensus splice acceptor and donor sites that potentially increase the size of exon 7, dividing it into three parts, designated 7A, 7B, and 7C. We show by reverse transcription polymerase chain reaction and in situ hybridization that these potential splice sites are used to yield additional α2(XI) procollagen mRNA splice variants that are expressed in fetal tissues. In human, expression of exon 7B-containing transcripts may be developmental stage-specific. Interestingly, inclusion of exon 7A or exon 7B in human and mouse α2(XI) procollagen mRNAs, respectively, would result in the insertion of an in-frame termination codon, suggesting that some of the additional splice variants encode a truncated pro-α2(XI) chain.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
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.meshAlternative Splicingen_HK
dc.subject.meshProcollagen - geneticsen_HK
dc.subject.meshProtein Precursors - geneticsen_HK
dc.subject.meshRNA, Messenger - geneticsen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.titleExtensive alternative splicing within the amino-propeptide coding domain of α2(XI) procollagen mRNAs: Expression of transcripts encoding truncated pro-α chainsen_HK
dc.typeArticleen_HK
dc.identifier.emailLui, VCH: vchlui@hkucc.hku.hken_HK
dc.identifier.emailNicholls, J: nicholls@pathology.hku.hken_HK
dc.identifier.emailCheah, KSE: hrmbdkc@hku.hken_HK
dc.identifier.authorityLui, VCH=rp00363en_HK
dc.identifier.authorityNicholls, J=rp00364en_HK
dc.identifier.authorityCheah, KSE=rp00342en_HK
dc.description.naturelink_to_OA_fulltexten_HK
dc.identifier.doi10.1074/jbc.271.28.16945en_HK
dc.identifier.pmid8663204-
dc.identifier.scopuseid_2-s2.0-8944244526en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-8944244526&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume271en_HK
dc.identifier.issue28en_HK
dc.identifier.spage16945en_HK
dc.identifier.epage16951en_HK
dc.identifier.isiWOS:A1996UX12600079-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLui, VCH=7004231344en_HK
dc.identifier.scopusauthoridNg, LJ=7201477760en_HK
dc.identifier.scopusauthoridSat, EWY=6506589776en_HK
dc.identifier.scopusauthoridNicholls, J=7201463077en_HK
dc.identifier.scopusauthoridCheah, KSE=35387746200en_HK
dc.identifier.issnl0021-9258-

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