Linked Life Data

9487987

Source:http://linkedlifedata.com/resource/pubmed/id/9487987

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-3-9
pubmed:abstractText
Amylin, calcitonin (CT) and calcitonin gene-related peptide (CGRP) share limited structural homology including amino-terminal ring structures linked by a disulfide bridge and amidated carboxy-termini. Here, we have compared [125I]Bolton-Hunter-[Lys1] rat amylin ([125I]amylin) binding and the stimulation of cyclic AMP accumulation by human (h) amylin, hCT and hCGRP-I in the human breast carcinoma cell lines MCF-7 and T47D, which predominantly express hCT1a and hCT1b receptor isoforms (hCTR1a, hCTR1b) at a similar total number of hCT-binding sites. In MCF-7 cells, half-maximal inhibition (IC50) of [125I]amylin binding by human amylin was observed at 3.6 +/- 0.8 nM (n = 6). hCT and hCGRP-I displaced [125I]amylin binding with 22 and 66 times higher IC50. [125I]hCT binding was inhibited by hCT with an IC50 of 8.1 +/- 1.9 nM (n = 5), and human amylin and hCGRP-I were over 100 times less potent. In T47D cells, on the other hand, specific binding of [125I]amylin was not observed, but hCT inhibited [125I]hCT binding with an IC50 of 3.2 +/- 0.4 nM (n = 3), and human amylin and hCGRP-I had over 200 times higher IC50. In MCF-7 cells, half-maximal stimulation (EC50) of cyclic AMP accumulation by human amylin, hCT and hCGRP-I occurred at 1.4 +/- 0.2, 1.7 +/- 0.4 and 6.3 +/- 1.3 nM respectively. In T47D cells, the EC50 of hCT was 0.32 +/- 0.02 nM (n = 3), and 30- and 1900-fold higher with human amylin and hCGRP-I. In conclusion, the expression of hCTR1a and hCTR1b and [125I]hCT binding were indistinguishable in MCF-7 and T47D cells. Yet, [125I]amylin binding was only recognized in MCF-7 cells, consistent with a distinct amylin receptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-0795
pubmed:author
pubmed:issnType
Print
pubmed:volume
155
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
423-31
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9487987-Amyloid, pubmed-meshheading:9487987-Binding, Competitive, pubmed-meshheading:9487987-Binding Sites, pubmed-meshheading:9487987-Breast Neoplasms, pubmed-meshheading:9487987-Calcitonin Gene-Related Peptide, pubmed-meshheading:9487987-Cyclic AMP, pubmed-meshheading:9487987-Female, pubmed-meshheading:9487987-Humans, pubmed-meshheading:9487987-Iodine Radioisotopes, pubmed-meshheading:9487987-Islet Amyloid Polypeptide, pubmed-meshheading:9487987-Polymerase Chain Reaction, pubmed-meshheading:9487987-Radioligand Assay, pubmed-meshheading:9487987-Receptors, Calcitonin, pubmed-meshheading:9487987-Receptors, Islet Amyloid Polypeptide, pubmed-meshheading:9487987-Receptors, Peptide, pubmed-meshheading:9487987-Stimulation, Chemical, pubmed-meshheading:9487987-Tumor Cells, Cultured
pubmed:year
1997
pubmed:articleTitle
Coexistence of novel amylin-binding sites with calcitonin receptors in human breast carcinoma MCF-7 cells.
pubmed:affiliation
Research Laboratory for Calcium Metabolism, Department of Orthopaedic Surgery, Zurich, Switzerland.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't