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Article: Collagen composition of normal and myxomatous human mitral heart valves

TitleCollagen composition of normal and myxomatous human mitral heart valves
Authors
Issue Date1984
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1984, v. 219 n. 2, p. 451-460 How to Cite?
AbstractThe collagens were studied in 13 normal and 19 myxomatous human mitral valves. The collagens of the valve were completely solubilized by using a method consisting of guanidinium chloride extraction, limited pepsin digestions and CNBr cleavage of the residue. The normal valves contained 74% type I, 24% type III and 2% type V collagen. The type I and type III collagens had similar solubility patterns, although only type I collagen was detected in the guanidinium chloride extract. Type V collagen was only detected in the first pepsin extract. The type I and III collagens had higher contents of hydroxylysine than did the same collagens from age-matched dermis. The two-dimensional electrophoretic 'maps' of CNBr-cleavage peptides showed low recoveries of the C-terminal α1(I) CB6 and α1(III) CB9 peptides, which are involved in forming intermolecular cross-linkages. Most of the reducible cross-linkages were present in large-M(r) peptide complexes, and these complexes were shown by labelling with 125I to include the tyrosine-containing α1(I) CB6 peptide. The myxomatous valves contained 67% type I, 31% type III and 2% type V collagens. There was a significant increase in the concentration of each type of collagen, which consisted of a 9% increase of type I collagen, a 53% increase of type III collagen and a 25% increase of type V collagen. The contents of hydroxylysine in type I and III collagens and the electrophoretic 'maps' of the CNBr-cleavage peptides involved in cross-linkages did not differ significantly from the results obtained from the normal valves. The biochemical findings suggest that there is an increased production of collagen, in particular type III collagen, and glycosaminoglycan as well as a proliferation of cells as part of a repair process in the myxomatous valves.
Persistent Identifierhttp://hdl.handle.net/10722/147309
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorCole, WGen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorHickey, AJen_US
dc.contributor.authorWilcken, DELen_US
dc.date.accessioned2012-05-29T06:02:50Z-
dc.date.available2012-05-29T06:02:50Z-
dc.date.issued1984en_US
dc.identifier.citationBiochemical Journal, 1984, v. 219 n. 2, p. 451-460en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttp://hdl.handle.net/10722/147309-
dc.description.abstractThe collagens were studied in 13 normal and 19 myxomatous human mitral valves. The collagens of the valve were completely solubilized by using a method consisting of guanidinium chloride extraction, limited pepsin digestions and CNBr cleavage of the residue. The normal valves contained 74% type I, 24% type III and 2% type V collagen. The type I and type III collagens had similar solubility patterns, although only type I collagen was detected in the guanidinium chloride extract. Type V collagen was only detected in the first pepsin extract. The type I and III collagens had higher contents of hydroxylysine than did the same collagens from age-matched dermis. The two-dimensional electrophoretic 'maps' of CNBr-cleavage peptides showed low recoveries of the C-terminal α1(I) CB6 and α1(III) CB9 peptides, which are involved in forming intermolecular cross-linkages. Most of the reducible cross-linkages were present in large-M(r) peptide complexes, and these complexes were shown by labelling with 125I to include the tyrosine-containing α1(I) CB6 peptide. The myxomatous valves contained 67% type I, 31% type III and 2% type V collagens. There was a significant increase in the concentration of each type of collagen, which consisted of a 9% increase of type I collagen, a 53% increase of type III collagen and a 25% increase of type V collagen. The contents of hydroxylysine in type I and III collagens and the electrophoretic 'maps' of the CNBr-cleavage peptides involved in cross-linkages did not differ significantly from the results obtained from the normal valves. The biochemical findings suggest that there is an increased production of collagen, in particular type III collagen, and glycosaminoglycan as well as a proliferation of cells as part of a repair process in the myxomatous valves.en_US
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_US
dc.relation.ispartofBiochemical Journalen_US
dc.subject.meshCollagen - Metabolismen_US
dc.subject.meshCyanogen Bromideen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshHumansen_US
dc.subject.meshMacromolecular Substancesen_US
dc.subject.meshMitral Valve - Metabolismen_US
dc.subject.meshMitral Valve Prolapse - Metabolismen_US
dc.subject.meshPepsin Aen_US
dc.subject.meshPeptide Fragments - Analysisen_US
dc.subject.meshSolubilityen_US
dc.titleCollagen composition of normal and myxomatous human mitral heart valvesen_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.pmid6430269-
dc.identifier.scopuseid_2-s2.0-0021267187en_US
dc.identifier.volume219en_US
dc.identifier.issue2en_US
dc.identifier.spage451en_US
dc.identifier.epage460en_US
dc.identifier.isiWOS:A1984SN35000013-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridHickey, AJ=7006559720en_US
dc.identifier.scopusauthoridWilcken, DEL=7005182174en_US

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