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Article: MT1-MMP-dependent and -independent regulation of gelatinase A activation in long-term, ascorbate-treated fibroblast cultures: Regulation by fibrillar collagen

TitleMT1-MMP-dependent and -independent regulation of gelatinase A activation in long-term, ascorbate-treated fibroblast cultures: Regulation by fibrillar collagen
Authors
Issue Date2002
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcr
Citation
Experimental Cell Research, 2002, v. 272 n. 2, p. 109-118 How to Cite?
AbstractHuman skin fibroblasts were cultured long-term in the presence of ascorbic acid to allow formation of a three-dimensional collagen matrix, and the effects of this on activation of secreted matrix metalloproteinase-2 (MMP-2) were examined. Accumulation of collagen over time correlated with increased levels of both mature MMP-2 and cell-associated membrane type 1-MMP (MT1-MMP), and subsequently increased mRNA levels for MT1-MMP, providing temporal resolution of the nontranscriptional and transcriptional effects of collagen on MT-1MMP functionality. MMP-2 activation by these cultures was blocked by inhibitors of prolyl-4-hydroxylase, or when fibroblasts derived from the collagen α1(I) gene-deficient Mov-13 mouse were used. MMP-2 activation by the Mov-13 fibroblasts was rescued by transfection of a full-length α1(I) collagen cDNA, and to our surprise, also by transfection with an α1(I) collagen cDNA carrying a mutation at the C-proteinase cleavage, which almost abrogated fibrillogenesis. Although studies with ascorbate-cultured MT1-MMP-/- fibroblasts showed that MT1-MMP played a significant role in the collagen-induced MMP-2 activation, a residual MT1-MMP-independent activation of MMP-2 was seen which resembled the level of MMP-2 activation persisting when wild-type fibroblasts were cultured in the presence of both ascorbic acid and MMP inhibitors. We were also unable to block this residual activation with inhibitors specific for serinyl, aspartyl, or cysteinyl enzymes. © 2001 Elsevier Science.
Persistent Identifierhttp://hdl.handle.net/10722/68268
ISSN
2015 Impact Factor: 3.378
2015 SCImago Journal Rankings: 1.900
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorRuangpanit, Nen_HK
dc.contributor.authorPrice, JTen_HK
dc.contributor.authorHolmbeck, Ken_HK
dc.contributor.authorBirkedalHansen, Hen_HK
dc.contributor.authorGuenzler, Ven_HK
dc.contributor.authorHuang, Xen_HK
dc.contributor.authorChan, Den_HK
dc.contributor.authorBateman, JFen_HK
dc.contributor.authorThompson, EWen_HK
dc.date.accessioned2010-09-06T06:02:57Z-
dc.date.available2010-09-06T06:02:57Z-
dc.date.issued2002en_HK
dc.identifier.citationExperimental Cell Research, 2002, v. 272 n. 2, p. 109-118en_HK
dc.identifier.issn0014-4827en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68268-
dc.description.abstractHuman skin fibroblasts were cultured long-term in the presence of ascorbic acid to allow formation of a three-dimensional collagen matrix, and the effects of this on activation of secreted matrix metalloproteinase-2 (MMP-2) were examined. Accumulation of collagen over time correlated with increased levels of both mature MMP-2 and cell-associated membrane type 1-MMP (MT1-MMP), and subsequently increased mRNA levels for MT1-MMP, providing temporal resolution of the nontranscriptional and transcriptional effects of collagen on MT-1MMP functionality. MMP-2 activation by these cultures was blocked by inhibitors of prolyl-4-hydroxylase, or when fibroblasts derived from the collagen α1(I) gene-deficient Mov-13 mouse were used. MMP-2 activation by the Mov-13 fibroblasts was rescued by transfection of a full-length α1(I) collagen cDNA, and to our surprise, also by transfection with an α1(I) collagen cDNA carrying a mutation at the C-proteinase cleavage, which almost abrogated fibrillogenesis. Although studies with ascorbate-cultured MT1-MMP-/- fibroblasts showed that MT1-MMP played a significant role in the collagen-induced MMP-2 activation, a residual MT1-MMP-independent activation of MMP-2 was seen which resembled the level of MMP-2 activation persisting when wild-type fibroblasts were cultured in the presence of both ascorbic acid and MMP inhibitors. We were also unable to block this residual activation with inhibitors specific for serinyl, aspartyl, or cysteinyl enzymes. © 2001 Elsevier Science.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcren_HK
dc.relation.ispartofExperimental Cell Researchen_HK
dc.subject.meshAscorbic Acid - pharmacologyen_HK
dc.subject.meshCells, Cultureden_HK
dc.subject.meshCollagen - metabolismen_HK
dc.subject.meshCollagen Type I - geneticsen_HK
dc.subject.meshCross-Linking Reagentsen_HK
dc.subject.meshEnzyme Activationen_HK
dc.subject.meshFibrillar Collagens - metabolismen_HK
dc.subject.meshFibroblasts - cytology - drug effects - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMatrix Metalloproteinase 14en_HK
dc.subject.meshMatrix Metalloproteinase 2 - metabolismen_HK
dc.subject.meshMatrix Metalloproteinases, Membrane-Associateden_HK
dc.subject.meshMetalloendopeptidases - metabolism - physiologyen_HK
dc.subject.meshProcollagen-Proline Dioxygenase - antagonists & inhibitorsen_HK
dc.subject.meshSkin - cytologyen_HK
dc.subject.meshTime Factorsen_HK
dc.titleMT1-MMP-dependent and -independent regulation of gelatinase A activation in long-term, ascorbate-treated fibroblast cultures: Regulation by fibrillar collagenen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-4827&volume=272&spage=109&epage=118&date=2002&atitle=MT1-MMP-dependent+and+-independent+regulation+of+gelatinase+A+activation+in+long-term,+ascorbate-treated+fibroblast+cultures:+regulation+by+fibrillar+collagenen_HK
dc.identifier.emailChan, D:chand@hkucc.hku.hken_HK
dc.identifier.authorityChan, D=rp00540en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1006/excr.2001.5403en_HK
dc.identifier.pmid11777335-
dc.identifier.scopuseid_2-s2.0-0036056980en_HK
dc.identifier.hkuros68640en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036056980&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume272en_HK
dc.identifier.issue2en_HK
dc.identifier.spage109en_HK
dc.identifier.epage118en_HK
dc.identifier.isiWOS:000173216900002-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridRuangpanit, N=6507950128en_HK
dc.identifier.scopusauthoridPrice, JT=7404020566en_HK
dc.identifier.scopusauthoridHolmbeck, K=6602337156en_HK
dc.identifier.scopusauthoridBirkedalHansen, H=7004711975en_HK
dc.identifier.scopusauthoridGuenzler, V=6506241133en_HK
dc.identifier.scopusauthoridHuang, X=14820358300en_HK
dc.identifier.scopusauthoridChan, D=7402216545en_HK
dc.identifier.scopusauthoridBateman, JF=16135557700en_HK
dc.identifier.scopusauthoridThompson, EW=7402849735en_HK

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