File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Imbalance in the synthesis of collagen type I and collagen type III in smooth muscle cells derived from human varicose veins

TitleImbalance in the synthesis of collagen type I and collagen type III in smooth muscle cells derived from human varicose veins
Authors
KeywordsCollagens type I, III and V
Smooth muscle cells
Tissue elasticity and rigidity
Varicose veins
Issue Date2001
PublisherS Karger AG. The Journal's web site is located at http://www.karger.com/JVR
Citation
Journal Of Vascular Research, 2001, v. 38 n. 6, p. 560-568 How to Cite?
AbstractVaricose veins have a thickening wall. Their smooth muscle cells are disorganized as regards proliferation and production of extracellular matrix protein. An imbalance between the synthesis of collagen type I protein (collagen I) and collagen type III protein (collagen III) could explain the lack of elasticity of varicose veins. Therefore, collagen synthesis was compared in the media and in cultured smooth muscle cells derived from human control and varicose saphenous veins. An increase in total collagen synthesis was observed in the media and in smooth muscle cells derived from varicose veins. This augmentation was due to an overproduction of collagen I in cultured cells from varicose veins consistent with an increase in the release of collagen I metabolites in the media. A concomitant decrease in collagen III was observed in cultures of smooth muscle cells from varicose veins. The increase in the synthesis of collagen I in cells from varicose veins was correlated with an over-expression of the gene since mRNAs for collagen I were augmented without change in mRNA-half-life. This augmentation in the synthesis of collagen I was reduced by the addition of exogenous collagen III in cultures from varicose veins. These findings suggest a dysregulation of the synthesis of collagen I and III in smooth muscle cells derived from varicose veins. Copyright © 2001 S. Karger AG, Basel.
Persistent Identifierhttp://hdl.handle.net/10722/171269
ISSN
2023 Impact Factor: 1.8
2023 SCImago Journal Rankings: 0.486
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSansilvestriMorel, Pen_US
dc.contributor.authorRupin, Aen_US
dc.contributor.authorBadierCommander, Cen_US
dc.contributor.authorKern, Pen_US
dc.contributor.authorFabiani, JNen_US
dc.contributor.authorVerbeuren, TJen_US
dc.contributor.authorVanhoutte, PMen_US
dc.date.accessioned2012-10-30T06:13:04Z-
dc.date.available2012-10-30T06:13:04Z-
dc.date.issued2001en_US
dc.identifier.citationJournal Of Vascular Research, 2001, v. 38 n. 6, p. 560-568en_US
dc.identifier.issn1018-1172en_US
dc.identifier.urihttp://hdl.handle.net/10722/171269-
dc.description.abstractVaricose veins have a thickening wall. Their smooth muscle cells are disorganized as regards proliferation and production of extracellular matrix protein. An imbalance between the synthesis of collagen type I protein (collagen I) and collagen type III protein (collagen III) could explain the lack of elasticity of varicose veins. Therefore, collagen synthesis was compared in the media and in cultured smooth muscle cells derived from human control and varicose saphenous veins. An increase in total collagen synthesis was observed in the media and in smooth muscle cells derived from varicose veins. This augmentation was due to an overproduction of collagen I in cultured cells from varicose veins consistent with an increase in the release of collagen I metabolites in the media. A concomitant decrease in collagen III was observed in cultures of smooth muscle cells from varicose veins. The increase in the synthesis of collagen I in cells from varicose veins was correlated with an over-expression of the gene since mRNAs for collagen I were augmented without change in mRNA-half-life. This augmentation in the synthesis of collagen I was reduced by the addition of exogenous collagen III in cultures from varicose veins. These findings suggest a dysregulation of the synthesis of collagen I and III in smooth muscle cells derived from varicose veins. Copyright © 2001 S. Karger AG, Basel.en_US
dc.languageengen_US
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/JVRen_US
dc.relation.ispartofJournal of Vascular Researchen_US
dc.subjectCollagens type I, III and V-
dc.subjectSmooth muscle cells-
dc.subjectTissue elasticity and rigidity-
dc.subjectVaricose veins-
dc.subject.meshAgeden_US
dc.subject.meshAged, 80 And Overen_US
dc.subject.meshCell Divisionen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCollagen - Biosynthesisen_US
dc.subject.meshCollagen Type I - Biosynthesis - Geneticsen_US
dc.subject.meshCollagen Type Iii - Biosynthesis - Pharmacologyen_US
dc.subject.meshFemaleen_US
dc.subject.meshHalf-Lifeen_US
dc.subject.meshHumansen_US
dc.subject.meshHydroxyproline - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshMiddle Ageden_US
dc.subject.meshMuscle, Smooth, Vascular - Metabolism - Pathologyen_US
dc.subject.meshOrgan Culture Techniquesen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshReference Valuesen_US
dc.subject.meshVaricose Veins - Metabolism - Pathologyen_US
dc.titleImbalance in the synthesis of collagen type I and collagen type III in smooth muscle cells derived from human varicose veinsen_US
dc.typeArticleen_US
dc.identifier.emailVanhoutte, PM:vanhoutt@hku.hken_US
dc.identifier.authorityVanhoutte, PM=rp00238en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1159/000051092en_US
dc.identifier.pmid11740155-
dc.identifier.scopuseid_2-s2.0-0035217825en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035217825&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume38en_US
dc.identifier.issue6en_US
dc.identifier.spage560en_US
dc.identifier.epage568en_US
dc.identifier.isiWOS:000173837300005-
dc.publisher.placeSwitzerlanden_US
dc.identifier.scopusauthoridSansilvestriMorel, P=7801596301en_US
dc.identifier.scopusauthoridRupin, A=6701753601en_US
dc.identifier.scopusauthoridBadierCommander, C=6603040792en_US
dc.identifier.scopusauthoridKern, P=7202583140en_US
dc.identifier.scopusauthoridFabiani, JN=7102990953en_US
dc.identifier.scopusauthoridVerbeuren, TJ=7007006534en_US
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_US
dc.identifier.issnl1018-1172-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats