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rdf:type |
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lifeskim:mentions |
umls-concept:C0166825,
umls-concept:C0205164,
umls-concept:C0242275,
umls-concept:C0441655,
umls-concept:C1413246,
umls-concept:C1514562,
umls-concept:C1517050,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2259196
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pubmed:issue |
24
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pubmed:dateCreated |
2000-7-20
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pubmed:abstractText |
Heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) is a member of the EGF family of growth factors. The membrane-anchored form of HB-EGF (proHB-EGF) is mitogenically active to neighboring cells as well as being a precursor of the soluble form. In addition to its mitogenic activity, proHB-EGF has the property of binding to diphtheria toxin (DT), serving as the specific receptor for DT. Tetramembrane-spanning protein CD9, a member of the TM4 superfamily, is physically associated with proHB-EGF at the cell surface and up-regulates both mitogenic and DT binding activities of proHB-EGF. To understand this up-regulation mechanism, we studied essential regions of both CD9 and proHB-EGF for up-regulation. Immunoprecipitation experiments revealed that not only CD9 but also other TM4 proteins including CD63, CD81, and CD82 associate with proHB-EGF on the cell surface. However, these TM4 proteins did not up-regulate DT binding activity of proHB-EGF. Transfection of a series of chimeric constructs comprising CD9 and CD81 showed that the major extracellular domain of CD9 is essential for up-regulation. Assays of DT binding activity and juxtacrine mitogenic activity of the deletion mutants of proHB-EGF and chimeric molecules, derived from proHB-EGF and TGF-alpha, showed that the essential domain of proHB-EGF for up-regulation is the EGF-like domain. These results indicate that the interaction of the extracellular domains of both molecules is important for up-regulation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD63,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD81,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD82,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD9,
http://linkedlifedata.com/resource/pubmed/chemical/CD63 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CD81 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CD82 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CD9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cd63 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cd81 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cd82 antigen, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cd9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
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 |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18284-90
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10749879-Animals,
pubmed-meshheading:10749879-Antigens, CD,
pubmed-meshheading:10749879-Antigens, CD63,
pubmed-meshheading:10749879-Antigens, CD81,
pubmed-meshheading:10749879-Antigens, CD82,
pubmed-meshheading:10749879-Antigens, CD9,
pubmed-meshheading:10749879-Binding Sites,
pubmed-meshheading:10749879-Cercopithecus aethiops,
pubmed-meshheading:10749879-Epidermal Growth Factor,
pubmed-meshheading:10749879-Heparin,
pubmed-meshheading:10749879-Humans,
pubmed-meshheading:10749879-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:10749879-L Cells (Cell Line),
pubmed-meshheading:10749879-Membrane Glycoproteins,
pubmed-meshheading:10749879-Membrane Proteins,
pubmed-meshheading:10749879-Mice,
pubmed-meshheading:10749879-Platelet Membrane Glycoproteins,
pubmed-meshheading:10749879-Protein Binding,
pubmed-meshheading:10749879-Proto-Oncogene Proteins,
pubmed-meshheading:10749879-Receptors, Cell Surface,
pubmed-meshheading:10749879-Structure-Activity Relationship,
pubmed-meshheading:10749879-Up-Regulation,
pubmed-meshheading:10749879-Vero Cells
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pubmed:year |
2000
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pubmed:articleTitle |
Importance of the major extracellular domain of CD9 and the epidermal growth factor (EGF)-like domain of heparin-binding EGF-like growth factor for up-regulation of binding and activity.
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pubmed:affiliation |
Division of Cell Biology, Institute of Life Science, and Research Center for Innovative Cancer Therapy, Kurume University, Kurume, Fukuoka 839-0861, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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