THE CALCITONIN RECEPTOR ON T-47D BREAST-CANCER CELLS - EVIDENCE FOR GLYCOSYLATION
THE CALCITONIN RECEPTOR ON T-47D BREAST-CANCER CELLS - EVIDENCE FOR GLYCOSYLATION
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DOI:
10.1042/bj2120609
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发表时间:
1983-01-01
影响因子:
4.1
通讯作者:
MARTIN, TJ
中科院分区:
文献类型:
--
作者:
MOSELEY, JM;FINDLAY, DM;MARTIN, TJ
The glycosyl nature of the receptor for the peptide hormone calcitonin was investigated in a human breast cancer cell line, T 47D. Studies were carried out to assess the ability of various lectins and of the antibiotic tunicamycin to inhibit specific binding of calcitonin to the cells, to reduce cross-linking of photoactive calcitonin to a macromolecular receptor component and to influence calcitonin stimulation of cAMP. Pre-incubation of cells with low concentration of tunicamycin for 72 h resulted in a reduction of total specific binding by .apprx. 80% and a 40% reduction in calcitonin-stimulated adenylate cyclase; formation of the cross-linked receptor component was also inhibited. Wheat-germ lectin showed the most marked inhibition of total specific binding and cAMP production. However, cross-linking of photoactive calcitonin to receptor component was totally inhibited by this lectin. Soya-bean lectin brought about very little reduction in total specific binding but had more profound effects on calcitonin-stimulated cAMP production and cross-linking of photoactive calcitonin. Concanavalin A and lentil lectin showed some inhibition of all parameters. The calcitonin receptor in T 47D cells is associated with glycosyl moieties, the major contributors of which are N-acetyl-D-glucosamine residues, but N-acetyl-D-galactosamine and mannose residues are also associated.