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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1986-9-16
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pubmed:abstractText |
Swiss 3T3 cells respond to picomolar concentrations of type beta transforming growth factor (TGF-beta) with a dose-dependent increase in the formation of colonies in soft agar, a decrease in the growth of cells in monolayer culture, and changes in morphology. This indicates that these cells have functional TGF-beta receptors able to mediate a biological response. Binding analysis revealed a single class of TGF-beta binding sites (80 000 per cell) with a Kd approximately 50 pM. Receptors were affinity-labeled by covalent attachment to 125I-TGF-beta with bis(sulfosuccinimidyl) suberate (BS3). The complexes formed were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the presence of 100 mM dithiothreitol and migrated as Mr approximately 180 000 complexes in 3-10% linear gradient gels. The apparent size of these complexes was larger in gels with a higher percentage of acrylamide. The labeling of the 125I-TGF-beta-receptor complexes was inhibited by the presence of excess unlabeled TGF-beta but was unaffected by other growth factors. These complexes could be formed by cross-linking whole cells, intact membranes, or solubilized membranes, demonstrating that the TGF-beta receptor is located on the plasma membrane and can be solubilized without destruction of its ability to bind TGF-beta. A larger Mr approximately 360 000 complex was present in 3-10% linear gradient gels without reduction or after extensive cross-linking, suggesting that the receptor consists of two subunits of similar size attached by disulfide bonds. Since BS3 is membrane-impermeable, at least a portion of both subunits is located on the outer surface of the plasma membrane.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3083-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2873833-Animals,
pubmed-meshheading:2873833-Blood Platelets,
pubmed-meshheading:2873833-Cell Division,
pubmed-meshheading:2873833-Cell Membrane,
pubmed-meshheading:2873833-Cell Transformation, Neoplastic,
pubmed-meshheading:2873833-Cells, Cultured,
pubmed-meshheading:2873833-Growth Substances,
pubmed-meshheading:2873833-Humans,
pubmed-meshheading:2873833-Kinetics,
pubmed-meshheading:2873833-Macromolecular Substances,
pubmed-meshheading:2873833-Mice,
pubmed-meshheading:2873833-Molecular Weight,
pubmed-meshheading:2873833-Peptides,
pubmed-meshheading:2873833-Receptors, Cell Surface,
pubmed-meshheading:2873833-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:2873833-Transforming Growth Factors
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pubmed:year |
1986
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pubmed:articleTitle |
Structure and properties of the cellular receptor for transforming growth factor type beta.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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