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Article: A frameshift mutation results in a truncated nonfunctional carboxyl-terminal Proα1(I) propeptide of type I collagen in osteogenesis imperfecta

TitleA frameshift mutation results in a truncated nonfunctional carboxyl-terminal Proα1(I) propeptide of type I collagen in osteogenesis imperfecta
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. 19, p. 10960-10964 How to Cite?
AbstractA codon frameshift mutation caused by a single base (U) insertion after base pair 4088 of preproα1(I) mRNA of type I procollagen was identified in a baby with lethal perinatal osteogenesis imperfecta. The mutation was identified in fibroblast RNA by a new method that allows the direct detection of mismatched bases by chemical modification and cleavage in heteroduplexes formed between mRNA and control cDNA probes. The region of mismatches was specifically amplified by the polymerase chain reaction and sequenced. The heterozygous mutation in the amplified cDNA most likely resulted from a T insertion in exon 49 of COL1A1. The frameshift resulted in a truncated proα1(I) carboxyl-terminal propeptide in which the amino acid sequence was abnormal from Val1146 to the carboxyl terminus. The propeptide lacked Asn118a7, which normally carries an N-linked oligosaccharide unit, and was more basic than the normal propeptide. The distribution of cysteines was altered and the mutant propeptide was unable to form normal interchain disulfide bonds. Some of the mutant proα1(I)' chains were incorporated into type I procollagen molecules but resulted in abnormal helix formation with overhydroxylation of lysine residues, increased degradation, and poor secretion. Only normal type I collagen was incorporated into the extracellular matrix in vivo resulting in a tissue type I collagen content approximately 20% of that of control (Bateman, J. F., Chan, D., Mascara, T., Rogers, J. G., and Cole, W. G. (1986) Biochem. J. 240, 699-708).
Persistent Identifierhttp://hdl.handle.net/10722/147334
ISSN
2020 Impact Factor: 5.157
2020 SCImago Journal Rankings: 2.361
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBateman, JFen_US
dc.contributor.authorLamande, SRen_US
dc.contributor.authorDahl, HHMen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorMascara, Ten_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:02:59Z-
dc.date.available2012-05-29T06:02:59Z-
dc.date.issued1989en_US
dc.identifier.citationJournal Of Biological Chemistry, 1989, v. 264 n. 19, p. 10960-10964en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147334-
dc.description.abstractA codon frameshift mutation caused by a single base (U) insertion after base pair 4088 of preproα1(I) mRNA of type I procollagen was identified in a baby with lethal perinatal osteogenesis imperfecta. The mutation was identified in fibroblast RNA by a new method that allows the direct detection of mismatched bases by chemical modification and cleavage in heteroduplexes formed between mRNA and control cDNA probes. The region of mismatches was specifically amplified by the polymerase chain reaction and sequenced. The heterozygous mutation in the amplified cDNA most likely resulted from a T insertion in exon 49 of COL1A1. The frameshift resulted in a truncated proα1(I) carboxyl-terminal propeptide in which the amino acid sequence was abnormal from Val1146 to the carboxyl terminus. The propeptide lacked Asn118a7, which normally carries an N-linked oligosaccharide unit, and was more basic than the normal propeptide. The distribution of cysteines was altered and the mutant propeptide was unable to form normal interchain disulfide bonds. Some of the mutant proα1(I)' chains were incorporated into type I procollagen molecules but resulted in abnormal helix formation with overhydroxylation of lysine residues, increased degradation, and poor secretion. Only normal type I collagen was incorporated into the extracellular matrix in vivo resulting in a tissue type I collagen content approximately 20% of that of control (Bateman, J. F., Chan, D., Mascara, T., Rogers, J. G., and Cole, W. G. (1986) Biochem. J. 240, 699-708).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.meshBase Sequenceen_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshCodonen_US
dc.subject.meshCollagen - Genetics - Metabolismen_US
dc.subject.meshDna Probesen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFibroblasts - Analysisen_US
dc.subject.meshGene Amplificationen_US
dc.subject.meshHumansen_US
dc.subject.meshMutationen_US
dc.subject.meshNucleic Acid Heteroduplexesen_US
dc.subject.meshNucleic Acid Hybridizationen_US
dc.subject.meshOsteogenesis Imperfecta - Geneticsen_US
dc.subject.meshPepsin A - Metabolismen_US
dc.subject.meshProcollagen - Geneticsen_US
dc.subject.meshRna, Messenger - Geneticsen_US
dc.titleA frameshift mutation results in a truncated nonfunctional carboxyl-terminal Proα1(I) propeptide of type I collagen in osteogenesis imperfectaen_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.pmid2500431-
dc.identifier.scopuseid_2-s2.0-0024320170en_US
dc.identifier.volume264en_US
dc.identifier.issue19en_US
dc.identifier.spage10960en_US
dc.identifier.epage10964en_US
dc.identifier.isiWOS:A1989AC81700007-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridLamande, SR=7004500719en_US
dc.identifier.scopusauthoridDahl, HHM=7101725390en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridMascara, T=6602227390en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.issnl0021-9258-

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