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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1985-7-9
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pubmed:abstractText |
The clonal cell line UMR 106, which was originally derived from a rat transplantable osteogenic sarcoma with an osteoblastic phenotype, was subcloned after the emergence of a calcitonin-responsive adenylate cyclase was noted in late passages. Detailed studies on the stimulation of adenylate cyclase and activation profile of the cyclic AMP-dependent protein kinase isoenzymes in response to parathyroid hormone (PTH) and salmon calcitonin (SCT) were conducted on two subclones (UMR 106-01 and UMR 106-06). Both subclones responded in an identical manner to PTH, which stimulated adenylate cyclase and activated both isoenzyme I and isoenzyme II of cyclic AMP-dependent protein kinase. In contrast, only UMR 106-06 cells responded to calcitonin. At 3 X 10(-8)M SCT, there was a sevenfold stimulation of adenylate cyclase, 84% activation of isoenzyme I, and 44% activation of isoenzyme II. The activation profiles of the isoenzymes to PTH and SCT in UMR 106-06 were similar. Furthermore, their response to SCT correlates with the presence of specific, saturable binding of 125I-labeled SCT. Binding parameters indicate apparent Kd = 0.8 nM and 6,000 receptors/cell. These data point to a significant phenotypic change having taken place in this clonal cell line with prolonged maintenance in culture, with the emergence of a calcitonin receptor linked to adenylate cyclase and protein kinase activation.
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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/Acid Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Parathyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0171-967X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:3922597-Acid Phosphatase,
pubmed-meshheading:3922597-Adenylate Cyclase,
pubmed-meshheading:3922597-Alkaline Phosphatase,
pubmed-meshheading:3922597-Animals,
pubmed-meshheading:3922597-Calcitonin,
pubmed-meshheading:3922597-Cell Line,
pubmed-meshheading:3922597-Clone Cells,
pubmed-meshheading:3922597-Enzyme Activation,
pubmed-meshheading:3922597-Isoenzymes,
pubmed-meshheading:3922597-Osteoblasts,
pubmed-meshheading:3922597-Osteosarcoma,
pubmed-meshheading:3922597-Parathyroid Hormone,
pubmed-meshheading:3922597-Phenotype,
pubmed-meshheading:3922597-Protein Kinases,
pubmed-meshheading:3922597-Rats
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pubmed:year |
1985
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pubmed:articleTitle |
Characterization of an osteoblast-like clonal cell line which responds to both parathyroid hormone and calcitonin.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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