rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1997-7-1
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pubmed:abstractText |
CD9 is a protein with 4 transmembrane domains, and functions as a cell surface antigen. We have previously reported that CD9 functions as an up-regulator of membrane-anchored heparin-binding EGF-like growth factor (proHB-EGF) activity, which is a potent mitogen as well as a soluble HB-EGF. Anti-CD9 antibodies can neutralize the juxtacrine activity of proHB-EGF when both CD9 and proHB-EGF are coexpressed. We demonstrated here: (1) the CD9 gene was transcribed and translated in the cultured human keratinocytes; (2) anti-CD9 antibody inhibited the approximately 50% growth of human keratinocytes in culture; (3) CD9 was coprecipitated with proHB-EGF and membrane-anchored amphiregulin (proAR), and (4) the transient coexpression of CD9 with proHB-EGF or proAR in mouse L cells up-regulated their juxtacrine growth factor activities. These results suggest that CD9 would make a heterodimer and/or trimer complex with proHB-EGF and proAR, and might cooperate with proHB-EGF and proAR for human keratinocyte growth in a juxtacrine manner.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD9,
http://linkedlifedata.com/resource/pubmed/chemical/CD9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cd9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/amphiregulin,
http://linkedlifedata.com/resource/pubmed/chemical/heparin-binding EGF-like growth...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9541
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
171
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
291-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:9180898-Animals,
pubmed-meshheading:9180898-Antigens, CD,
pubmed-meshheading:9180898-Antigens, CD9,
pubmed-meshheading:9180898-Cell Division,
pubmed-meshheading:9180898-Cells, Cultured,
pubmed-meshheading:9180898-Epidermal Growth Factor,
pubmed-meshheading:9180898-Glycoproteins,
pubmed-meshheading:9180898-Growth Substances,
pubmed-meshheading:9180898-Humans,
pubmed-meshheading:9180898-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:9180898-Keratinocytes,
pubmed-meshheading:9180898-Membrane Glycoproteins,
pubmed-meshheading:9180898-Mice,
pubmed-meshheading:9180898-Receptor Aggregation
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pubmed:year |
1997
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pubmed:articleTitle |
Possible role of coexpression of CD9 with membrane-anchored heparin-binding EGF-like growth factor and amphiregulin in cultured human keratinocyte growth.
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pubmed:affiliation |
Department of Biochemistry, Osaka University Medical School, Japan.
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pubmed:publicationType |
Journal Article
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