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Article: Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMS

TitleTransmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMS
Authors
KeywordsBasement membrane
Hemidesmosome
Metalloprotease
Secretase
Skin
Issue Date2002
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/emboj/index.html
Citation
Embo Journal, 2002, v. 21 n. 19, p. 5026-5035 How to Cite?
AbstractCollagen XVII, a type II transmembrane protein and epithelial adhesion molecule, can be proteolytically shed from the cell surface to generate a soluble collagen. Here we investigated the release of the ectodomain and identified the enzymes involved. After surface biotinylation of keratinocytes, the ectodomain was detectable in the medium within minutes and remained stable for >48 h. Shedding was enhanced by phorbol esters and inhibited by metalloprotease inhibitors, including hydroxamates and TIMP-3, but not by inhibitors of other protease classes or by TIMP-2. This profile implicated MMPs or ADAMs as candidate sheddases. MMP-2, MMP-9 and MT1-MMP were excluded, but TACE, ADAM-10 and ADAM-9 were shown to be expressed in keratinocytes and to be actively involved. Transfection with cDNAs for the three ADAMs resulted in increased shedding and, vice versa, in TACE-deficient cells shedding was significantly reduced, indicating that transmembrane collagen XVII represents a novel class of substrates for ADAMs. Functionally, release of the ectodomain of collagen XVII from the cell surface was associated with altered keratinocyte motility in vitro.
Persistent Identifierhttp://hdl.handle.net/10722/48982
ISSN
2015 Impact Factor: 9.643
2015 SCImago Journal Rankings: 7.450
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFranzke, CWen_HK
dc.contributor.authorTasanen, Ken_HK
dc.contributor.authorSchäcke, Hen_HK
dc.contributor.authorZhou, Zen_HK
dc.contributor.authorTryggvason, Ken_HK
dc.contributor.authorMauch, Cen_HK
dc.contributor.authorZigrino, Pen_HK
dc.contributor.authorSunnarborg, Sen_HK
dc.contributor.authorLee, DCen_HK
dc.contributor.authorFahrenholz, Fen_HK
dc.contributor.authorBrucknerTuderman, Len_HK
dc.date.accessioned2008-06-12T06:31:20Z-
dc.date.available2008-06-12T06:31:20Z-
dc.date.issued2002en_HK
dc.identifier.citationEmbo Journal, 2002, v. 21 n. 19, p. 5026-5035en_HK
dc.identifier.issn0261-4189en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48982-
dc.description.abstractCollagen XVII, a type II transmembrane protein and epithelial adhesion molecule, can be proteolytically shed from the cell surface to generate a soluble collagen. Here we investigated the release of the ectodomain and identified the enzymes involved. After surface biotinylation of keratinocytes, the ectodomain was detectable in the medium within minutes and remained stable for >48 h. Shedding was enhanced by phorbol esters and inhibited by metalloprotease inhibitors, including hydroxamates and TIMP-3, but not by inhibitors of other protease classes or by TIMP-2. This profile implicated MMPs or ADAMs as candidate sheddases. MMP-2, MMP-9 and MT1-MMP were excluded, but TACE, ADAM-10 and ADAM-9 were shown to be expressed in keratinocytes and to be actively involved. Transfection with cDNAs for the three ADAMs resulted in increased shedding and, vice versa, in TACE-deficient cells shedding was significantly reduced, indicating that transmembrane collagen XVII represents a novel class of substrates for ADAMs. Functionally, release of the ectodomain of collagen XVII from the cell surface was associated with altered keratinocyte motility in vitro.en_HK
dc.format.extent386 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/emboj/index.htmlen_HK
dc.relation.ispartofEMBO Journalen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectBasement membraneen_HK
dc.subjectHemidesmosomeen_HK
dc.subjectMetalloproteaseen_HK
dc.subjectSecretaseen_HK
dc.subjectSkinen_HK
dc.titleTransmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMSen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0261-4189&volume=21&issue=19&spage=5026&epage=5035&date=2002&atitle=Transmembrane+collagen+XVII,+an+epithelial+adhesion+protein,+is+shed+from+the+cell+surface+by+ADAMsen_HK
dc.identifier.emailZhou, Z:zhongjun@hkucc.hku.hken_HK
dc.identifier.authorityZhou, Z=rp00503en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1093/emboj/cdf532en_HK
dc.identifier.pmid12356719-
dc.identifier.pmcidPMC129053en_HK
dc.identifier.scopuseid_2-s2.0-18644384411en_HK
dc.identifier.hkuros84054-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-18644384411&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume21en_HK
dc.identifier.issue19en_HK
dc.identifier.spage5026en_HK
dc.identifier.epage5035en_HK
dc.identifier.isiWOS:000178502600003-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridFranzke, CW=7004439651en_HK
dc.identifier.scopusauthoridTasanen, K=6701847498en_HK
dc.identifier.scopusauthoridSchäcke, H=36838478700en_HK
dc.identifier.scopusauthoridZhou, Z=8631856300en_HK
dc.identifier.scopusauthoridTryggvason, K=7102025185en_HK
dc.identifier.scopusauthoridMauch, C=7005219019en_HK
dc.identifier.scopusauthoridZigrino, P=6602613780en_HK
dc.identifier.scopusauthoridSunnarborg, S=6507311657en_HK
dc.identifier.scopusauthoridLee, DC=36072101200en_HK
dc.identifier.scopusauthoridFahrenholz, F=7006150584en_HK
dc.identifier.scopusauthoridBrucknerTuderman, L=7006538168en_HK

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