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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1990-9-17
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pubmed:abstractText |
The binding of 125I-Tyr4 bombesin was investigated on plasma membranes of 8 human breast cancer cell lines and 2 long-term cultures of normal human breast epithelial cells. Scatchard plots were compatible with high-affinity, single-site class of receptors in 3 cell lines (KD of 0.75 x 10(-9) and 10(-9) M, Bmax of 0.75 x 10(-13) and 9.7 x 10(-13) M/mg protein in MDA-MB231 and in T47D cells, respectively) while no binding was observed in 5 other cell lines and normal epithelial cells. The neuropeptide and its structural analogues (natural or synthetic) inhibited the binding of 125I-Tyr4 bombesin in the following order of potency: gastrin-releasing peptide (GRP, EC50 = 1.7 x 10(-10) M) greater than BIM 26159 greater than bombesin, Tyr4 bombesin greater than BIM 26147 greater than litorin greater than neuromedin C. In contrast, 125I-Tyr4 bombesin binding was not displaced by neuromedin B, somatostatin, bradykinin and insulin. In agreement with our binding data, SDS-PAGE of the complex 125I-Tyr4 bombesin-receptor covalently linked by ethylene glycol-bis succinimidyl succinate (EGS) identified after autoradiography a single band with a molecular weight of 75,000, which disappeared in the presence of bombesin in excess. No transcription of either GRP or neuromedin B mRNA could be shown in tumor or normal cells. Exogenous gastrin-releasing peptide had no effect on growth of the cell lines when a serum-free medium was used, implicating that in breast cancer cell lines this receptor does not mediate growth but has a functional role.
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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/Bombesin,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Gastrin-Releasing Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Bombesin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Neurotransmitter
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0020-7136
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
293-8
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:2166713-Blotting, Northern,
pubmed-meshheading:2166713-Bombesin,
pubmed-meshheading:2166713-Breast,
pubmed-meshheading:2166713-Breast Neoplasms,
pubmed-meshheading:2166713-Cell Line,
pubmed-meshheading:2166713-Cell Membrane,
pubmed-meshheading:2166713-Cells, Cultured,
pubmed-meshheading:2166713-Cross-Linking Reagents,
pubmed-meshheading:2166713-Epithelium,
pubmed-meshheading:2166713-Female,
pubmed-meshheading:2166713-Gastrin-Releasing Peptide,
pubmed-meshheading:2166713-Humans,
pubmed-meshheading:2166713-Peptides,
pubmed-meshheading:2166713-Radioligand Assay,
pubmed-meshheading:2166713-Receptors, Bombesin,
pubmed-meshheading:2166713-Receptors, Neurotransmitter,
pubmed-meshheading:2166713-Tumor Cells, Cultured
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pubmed:year |
1990
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pubmed:articleTitle |
Characterization, in some human breast cancer cell lines, of gastrin-releasing peptide-like receptors which are absent in normal breast epithelial cells.
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pubmed:affiliation |
Laboratory of Pharmacology, Hopital Saint-Louis, Paris, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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