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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
1993-6-8
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pubmed:abstractText |
Epithelin 1 and 2 are cysteine-rich proteins that act as growth modulators of epithelial cells. In this report, we have characterized the epithelins receptors of MDA-MB-468 human breast carcinoma cells using both binding and cross-linking techniques. Equilibrium binding studies of iodinated epithelin 1 indicated that two classes of binding sites are expressed at the surface of breast carcinoma cells. The high affinity sites had a dissociation constant of approximately 2 x 10(-10) M, with approximately 290 receptors/cell. The low affinity sites had a dissociation constant of approximately 10(-8) M, with approximately 32,000 receptors/cell. Binding of iodinated epithelin 1 was specifically inhibited by unlabeled epithelin 1, 2, or 3, but not by other growth factors tested. We also performed competition binding studies of 125I-epithelin 1 to cell surface receptors in the presence of unlabeled epithelin 1, 2, or 3. Binding results analyzed by the method of Scatchard suggested that all three epithelins interact with a same receptor. A 140-145-kDa epithelin 1-binding protein complex was identified by chemical cross-linking of 125I-epithelin 1 to breast cancer cells. Formation of such a complex was prevented by coincubation of 125I-epithelin 1 with an excess of unlabeled epithelin 1, 2, or 3.
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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/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/granulin 3,
http://linkedlifedata.com/resource/pubmed/chemical/granulin 4
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10458-62
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:8387520-Binding, Competitive,
pubmed-meshheading:8387520-Binding Sites,
pubmed-meshheading:8387520-Breast Neoplasms,
pubmed-meshheading:8387520-Cell Division,
pubmed-meshheading:8387520-Cytokines,
pubmed-meshheading:8387520-Female,
pubmed-meshheading:8387520-Growth Inhibitors,
pubmed-meshheading:8387520-Growth Substances,
pubmed-meshheading:8387520-Humans,
pubmed-meshheading:8387520-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:8387520-Kinetics,
pubmed-meshheading:8387520-Receptors, Cell Surface,
pubmed-meshheading:8387520-Tumor Cells, Cultured
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pubmed:year |
1993
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pubmed:articleTitle |
Biochemical analysis of the epithelin receptor.
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pubmed:affiliation |
Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121.
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pubmed:publicationType |
Journal Article
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