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Article: Gelatinase A (MMP-2) activation by skin fibroblasts: dependence on MT1-MMP expression and fibrillar collagen form

TitleGelatinase A (MMP-2) activation by skin fibroblasts: dependence on MT1-MMP expression and fibrillar collagen form
Authors
Issue Date2001
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/matbio
Citation
Matrix Biology, 2001, v. 20 n. 3, p. 193-203 How to Cite?
AbstractThe respective requirements of collagen and MT1-MMP in the activation of MMP-2 by primary fibroblast cultures were explored further. Three-dimensional gels enriched in human collagen types I and III or composed of recombinant human type II or III collagen, caused increased MT1-MMP production (mRNA and protein) and induced MMP-2 activation. Only marginal induction was seen with dried monomeric collagen confirming the need for collagen fibrillar organisation for activation. To our surprise, relatively low amounts (as low as 25 μg/ml) of acid soluble type I collagen added to fibroblast cultures also induced potent MMP-2 activation. However, the requirement for collagen fibril formation by the added collagen was indicated by the inhibition seen when the collagen was pre-incubated with a fibril-blocking peptide, and the reduced activation seen with alkali-treated collagen preparations known to have impaired fibrilisation. Pre-treatment of the collagen with sodium periodate also abrogated MMP-2 activation induction. Further evidence of the requirement for collagen fibril formation was provided by the lack of activation when type IV collagen, which does not form collagen fibrils, was added in the cultures. Fibroblasts derived from MT1-MMP-deficient mice were unable to activate MMP-2 in response to either three-dimensional collagen gel or added collagen solutions, compared to their littermate controls. Collectively, these data indicate that the fibrillar structure of collagen and MT1-MMP are essential for the MMP-2 activational response in fibroblasts. Copyright © 2001 Elsevier Science B.V./International Society of Matrix Biology.
Persistent Identifierhttp://hdl.handle.net/10722/68023
ISSN
2015 Impact Factor: 4.47
2015 SCImago Journal Rankings: 1.902
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorRuangpanit, Nen_HK
dc.contributor.authorChan, Den_HK
dc.contributor.authorHolmbeck, Ken_HK
dc.contributor.authorBirkedalHansen, Hen_HK
dc.contributor.authorPolarek, Jen_HK
dc.contributor.authorYang, Cen_HK
dc.contributor.authorBateman, JFen_HK
dc.contributor.authorThompson, EWen_HK
dc.date.accessioned2010-09-06T06:00:36Z-
dc.date.available2010-09-06T06:00:36Z-
dc.date.issued2001en_HK
dc.identifier.citationMatrix Biology, 2001, v. 20 n. 3, p. 193-203en_HK
dc.identifier.issn0945-053Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/68023-
dc.description.abstractThe respective requirements of collagen and MT1-MMP in the activation of MMP-2 by primary fibroblast cultures were explored further. Three-dimensional gels enriched in human collagen types I and III or composed of recombinant human type II or III collagen, caused increased MT1-MMP production (mRNA and protein) and induced MMP-2 activation. Only marginal induction was seen with dried monomeric collagen confirming the need for collagen fibrillar organisation for activation. To our surprise, relatively low amounts (as low as 25 μg/ml) of acid soluble type I collagen added to fibroblast cultures also induced potent MMP-2 activation. However, the requirement for collagen fibril formation by the added collagen was indicated by the inhibition seen when the collagen was pre-incubated with a fibril-blocking peptide, and the reduced activation seen with alkali-treated collagen preparations known to have impaired fibrilisation. Pre-treatment of the collagen with sodium periodate also abrogated MMP-2 activation induction. Further evidence of the requirement for collagen fibril formation was provided by the lack of activation when type IV collagen, which does not form collagen fibrils, was added in the cultures. Fibroblasts derived from MT1-MMP-deficient mice were unable to activate MMP-2 in response to either three-dimensional collagen gel or added collagen solutions, compared to their littermate controls. Collectively, these data indicate that the fibrillar structure of collagen and MT1-MMP are essential for the MMP-2 activational response in fibroblasts. Copyright © 2001 Elsevier Science B.V./International Society of Matrix Biology.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/matbioen_HK
dc.relation.ispartofMatrix Biologyen_HK
dc.rightsMatrix Biology. Copyright © Elsevier BV.en_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshCollagen - metabolismen_HK
dc.subject.meshEnzyme Activationen_HK
dc.subject.meshFibroblasts - cytologyen_HK
dc.subject.meshGene Expressionen_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 - metabolismen_HK
dc.subject.meshMiceen_HK
dc.subject.meshSkin - cytologyen_HK
dc.titleGelatinase A (MMP-2) activation by skin fibroblasts: dependence on MT1-MMP expression and fibrillar collagen formen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0945-053X&volume=20&spage=193&epage=203&date=2001&atitle=Gelatinase+A+(MMP-2)+activation+by+skin+fibroblasts:+dependence+on+MT1-MMP+expression+and+fibrillar+collagen+formen_HK
dc.identifier.emailChan, D:chand@hkucc.hku.hken_HK
dc.identifier.authorityChan, D=rp00540en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0945-053X(01)00135-4en_HK
dc.identifier.pmid11420151en_HK
dc.identifier.scopuseid_2-s2.0-0034985334en_HK
dc.identifier.hkuros58932en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034985334&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume20en_HK
dc.identifier.issue3en_HK
dc.identifier.spage193en_HK
dc.identifier.epage203en_HK
dc.identifier.isiWOS:000169782600004-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridRuangpanit, N=6507950128en_HK
dc.identifier.scopusauthoridChan, D=7402216545en_HK
dc.identifier.scopusauthoridHolmbeck, K=6602337156en_HK
dc.identifier.scopusauthoridBirkedalHansen, H=7004711975en_HK
dc.identifier.scopusauthoridPolarek, J=8749460400en_HK
dc.identifier.scopusauthoridYang, C=8975321100en_HK
dc.identifier.scopusauthoridBateman, JF=16135557700en_HK
dc.identifier.scopusauthoridThompson, EW=7402849735en_HK

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