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Article: Marfan syndrome: Absence of type I or III collagen structural defects in 25 patients

TitleMarfan syndrome: Absence of type I or III collagen structural defects in 25 patients
Authors
Issue Date1990
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0141-8955
Citation
Journal Of Inherited Metabolic Disease, 1990, v. 13 n. 2, p. 219-226 How to Cite?
AbstractThe structure and metabolism of type I and III collagens were studied in fibroblast cultures and dermis from 25 unrelated patients including 23 with typical Marfan syndrome and two infants with a very severe clinical form of this syndrome. Electrophoretic analysis of collagen α-chains, as well as one- and two-dimensional electrophoresis of collagen cyanogen bromide peptides, failed to show any evidence of primary structure defects or overmodification of lysine residues in thesed collagens. The proportion of hydroxylated prolyl residues in isolated α1(I) chains was also normal. There was a minimal increase in the proportion of type III collagen produced by nine cultures. The findings in this study indicate that the underlying molecular defects in the patients studied are unlikely to involve the structure of the main fibrillar type I and III collagens.
Persistent Identifierhttp://hdl.handle.net/10722/147353
ISSN
2015 Impact Factor: 3.541
2015 SCImago Journal Rankings: 1.389
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHarley, VRen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorRogers, JGen_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:03:07Z-
dc.date.available2012-05-29T06:03:07Z-
dc.date.issued1990en_US
dc.identifier.citationJournal Of Inherited Metabolic Disease, 1990, v. 13 n. 2, p. 219-226en_US
dc.identifier.issn0141-8955en_US
dc.identifier.urihttp://hdl.handle.net/10722/147353-
dc.description.abstractThe structure and metabolism of type I and III collagens were studied in fibroblast cultures and dermis from 25 unrelated patients including 23 with typical Marfan syndrome and two infants with a very severe clinical form of this syndrome. Electrophoretic analysis of collagen α-chains, as well as one- and two-dimensional electrophoresis of collagen cyanogen bromide peptides, failed to show any evidence of primary structure defects or overmodification of lysine residues in thesed collagens. The proportion of hydroxylated prolyl residues in isolated α1(I) chains was also normal. There was a minimal increase in the proportion of type III collagen produced by nine cultures. The findings in this study indicate that the underlying molecular defects in the patients studied are unlikely to involve the structure of the main fibrillar type I and III collagens.en_US
dc.languageengen_US
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0141-8955en_US
dc.relation.ispartofJournal of Inherited Metabolic Diseaseen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCollagen - Metabolismen_US
dc.subject.meshCollagen Diseases - Metabolism - Pathologyen_US
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_US
dc.subject.meshFibroblastsen_US
dc.subject.meshHumansen_US
dc.subject.meshInfanten_US
dc.subject.meshLysine - Metabolismen_US
dc.subject.meshMarfan Syndrome - Metabolism - Pathologyen_US
dc.subject.meshSkinen_US
dc.titleMarfan syndrome: Absence of type I or III collagen structural defects in 25 patientsen_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.doi10.1007/BF01799689en_US
dc.identifier.pmid2116553-
dc.identifier.scopuseid_2-s2.0-0025339487en_US
dc.identifier.volume13en_US
dc.identifier.issue2en_US
dc.identifier.spage219en_US
dc.identifier.epage226en_US
dc.identifier.isiWOS:A1990EJ28000014-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridHarley, VR=35465928300en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridRogers, JG=7404268782en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

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