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Article: Deletion of 24 amino acids from the Pro-α1(I) chain of type I procollagen in a patient with the Ehlers-Danlos syndrome type VII

TitleDeletion of 24 amino acids from the Pro-α1(I) chain of type I procollagen in a patient with the Ehlers-Danlos syndrome type VII
Authors
Issue Date1986
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, 1986, v. 261 n. 12, p. 5496-5503 How to Cite?
AbstractA child with the type VII form of the Ehlers-Danlos syndrome was shown to have a structural defect in the amino terminus of the pro-α1(I) chain of type I procollagen. Normal and mutant amino-terminal cyanogen bromide peptides (pN-α1(I) CB0,1 peptides) were purified from the medium of the patient's cultured fibroblasts. Amino acid sequencing of tryptic peptides derived from the mutant pN-α1(I) CB0,1 peptide showed that an expected sequence of 24 amino acids (positions 136-159 of the normal pN-α1(I) CB0,1 peptide) was deleted. The segment deleted from the mutant pro-α1(I) chain contains the small globular region of the NH 2-propeptide, the procollagen N-proteinase cleavage site, the NH 2-telopeptide, and first triplet of the helix of the αI(I) collagen chain (Chu, M.-L., de Wet, W., Bernard, M., Ding, J.F., Morabito, M., Myers, J., Williams, C., and Ramirez, F. (1984) Nature 310, 337-340). Loss of the procollagen N-proteinase cleavage site from the mutant pro-α1(I) chain accounted for the persistence of its NH 2-propeptide despite normal production of the N-proteinase by cultured mutant fibroblasts. Collagen production by mutant fibroblasts was doubled possibly due to reduced feedback inhibition by the NH 2-propeptides. The child appeared to be heterozygous for the peptide deletion and, as the parents did not show any evidence of the deletion, it is likely that the child had a new mutation of one allele of the pro-α1(I) gene. The deleted peptide corresponds precisely to the sequence coded by exon 46 of the normal pro-α1(I) gene (Chu, M.-L., de Wet, W., Bernard, M., Ding, J.F., Morabito, M., Myers, J., Williams, C., and Ramirez, F. (1984) Nature 310, 337-340).
Persistent Identifierhttp://hdl.handle.net/10722/147319
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCole, WGen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorChambers, GWen_US
dc.date.accessioned2012-05-29T06:02:53Z-
dc.date.available2012-05-29T06:02:53Z-
dc.date.issued1986en_US
dc.identifier.citationJournal Of Biological Chemistry, 1986, v. 261 n. 12, p. 5496-5503en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147319-
dc.description.abstractA child with the type VII form of the Ehlers-Danlos syndrome was shown to have a structural defect in the amino terminus of the pro-α1(I) chain of type I procollagen. Normal and mutant amino-terminal cyanogen bromide peptides (pN-α1(I) CB0,1 peptides) were purified from the medium of the patient's cultured fibroblasts. Amino acid sequencing of tryptic peptides derived from the mutant pN-α1(I) CB0,1 peptide showed that an expected sequence of 24 amino acids (positions 136-159 of the normal pN-α1(I) CB0,1 peptide) was deleted. The segment deleted from the mutant pro-α1(I) chain contains the small globular region of the NH 2-propeptide, the procollagen N-proteinase cleavage site, the NH 2-telopeptide, and first triplet of the helix of the αI(I) collagen chain (Chu, M.-L., de Wet, W., Bernard, M., Ding, J.F., Morabito, M., Myers, J., Williams, C., and Ramirez, F. (1984) Nature 310, 337-340). Loss of the procollagen N-proteinase cleavage site from the mutant pro-α1(I) chain accounted for the persistence of its NH 2-propeptide despite normal production of the N-proteinase by cultured mutant fibroblasts. Collagen production by mutant fibroblasts was doubled possibly due to reduced feedback inhibition by the NH 2-propeptides. The child appeared to be heterozygous for the peptide deletion and, as the parents did not show any evidence of the deletion, it is likely that the child had a new mutation of one allele of the pro-α1(I) gene. The deleted peptide corresponds precisely to the sequence coded by exon 46 of the normal pro-α1(I) gene (Chu, M.-L., de Wet, W., Bernard, M., Ding, J.F., Morabito, M., Myers, J., Williams, C., and Ramirez, F. (1984) Nature 310, 337-340).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.meshAmino Acids - Analysisen_US
dc.subject.meshChromatography, High Pressure Liquiden_US
dc.subject.meshChromatography, Ion Exchangeen_US
dc.subject.meshCyanogen Bromide - Pharmacologyen_US
dc.subject.meshEhlers-Danlos Syndrome - Metabolismen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFemaleen_US
dc.subject.meshHumansen_US
dc.subject.meshInfanten_US
dc.subject.meshPepsin A - Metabolismen_US
dc.subject.meshPeptide Fragments - Analysisen_US
dc.subject.meshProcollagen - Analysisen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshTrypsin - Metabolismen_US
dc.titleDeletion of 24 amino acids from the Pro-α1(I) chain of type I procollagen in a patient with the Ehlers-Danlos syndrome type VIIen_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.pmid3082886-
dc.identifier.scopuseid_2-s2.0-0022974587en_US
dc.identifier.volume261en_US
dc.identifier.issue12en_US
dc.identifier.spage5496en_US
dc.identifier.epage5503en_US
dc.identifier.isiWOS:A1986C054400043-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridChambers, GW=55197435500en_US

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