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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
48
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pubmed:dateCreated |
1997-1-7
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pubmed:abstractText |
Human heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) expressed on Chinese hamster ovary (CHO) cells is synthesized as a 19-kDa major, and 22- and 27-kDa minor, membrane-anchored precursors (proHB-EGF). In contrast, the 27-kDa species is major and the 19- and 22-kDa ones are minor in mouse proHB-EGF. The juxtacrine growth factor activities of human and mouse proHB-EGFs on CHO cells toward EP170.7 cells in co-culture are significantly different. To investigate the relationship between the juxtacrine growth factor activities and the molecular species, we prepared human-mouse chimeras. Chimeras that have the human amino-terminal sequence with a mouse EGF-like domain showed approximately 8-fold up-regulation of the juxtacrine growth factor activity and the predominance of a 19-22-kDa major species. In contrast, chimeras that have the mouse amino-terminal sequence with a human EGF-like domain showed approximately 5-fold down-regulation of the juxtacrine activity and the predominance of the 27-kDa major species. A Gly32.HB-EGF (117-amino acid form), which is amino-terminally extended, induced the same mitogenic activity as that of Arg73.HB-EGF (75-amino acid form), which is amino-terminally truncated. These results strongly suggested that amino-terminal processing of human proHB-EGF would be required for up-regulation of its juxtacrine growth factor activity, but not for its paracrine activity.
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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, 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/Furin,
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/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Subtilisins,
http://linkedlifedata.com/resource/pubmed/chemical/heparin-binding EGF-like growth...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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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 |
29
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30858-63
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:8940069-Amino Acid Sequence,
pubmed-meshheading:8940069-Animals,
pubmed-meshheading:8940069-Antigens, CD,
pubmed-meshheading:8940069-Antigens, CD9,
pubmed-meshheading:8940069-CHO Cells,
pubmed-meshheading:8940069-Cell Division,
pubmed-meshheading:8940069-Cricetinae,
pubmed-meshheading:8940069-Epidermal Growth Factor,
pubmed-meshheading:8940069-Furin,
pubmed-meshheading:8940069-Growth Substances,
pubmed-meshheading:8940069-Humans,
pubmed-meshheading:8940069-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:8940069-Membrane Glycoproteins,
pubmed-meshheading:8940069-Mice,
pubmed-meshheading:8940069-Molecular Sequence Data,
pubmed-meshheading:8940069-Protein Processing, Post-Translational,
pubmed-meshheading:8940069-Receptors, Cell Surface,
pubmed-meshheading:8940069-Recombinant Fusion Proteins,
pubmed-meshheading:8940069-Structure-Activity Relationship,
pubmed-meshheading:8940069-Subtilisins
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pubmed:year |
1996
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pubmed:articleTitle |
Amino-terminal processing of cell surface heparin-binding epidermal growth factor-like growth factor up-regulates its juxtacrine but not its paracrine growth factor activity.
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pubmed:affiliation |
Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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