Studies on the uptake of 67Ga and 59Fe and the binding of transferrin by cultured mouse tumour cells
| Autor: | Robert G. Sephton, Alan W. Harris |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Lymphoma
Iron T-Lymphocytes Cell Gallium Radioisotopes Receptors Cell Surface Transferrin receptor In Vitro Techniques Biology Ferric Compounds Iodine Radioisotopes Mice Receptors Transferrin medicine Animals Malignant cells Radiology Nuclear Medicine and imaging Receptor Cells Cultured chemistry.chemical_classification Iron Radioisotopes Mice Inbred BALB C Transferrin Neoplasms Experimental medicine.disease Molecular biology Culture Media Dissociation constant Blood medicine.anatomical_structure Biochemistry chemistry Cell culture Multiple Myeloma |
| Zdroj: | International Journal of Nuclear Medicine and Biology. 8:333-339 |
| ISSN: | 0047-0740 |
| DOI: | 10.1016/0047-0740(81)90040-1 |
| Popis: | Two cultured mouse tumour cell lines, HPC-108 (myeloma) and WEHI-22 (T lymphoma), were used in an investigation of transferrin promotion of 67Ga. and 59Fe uptake by malignant cells. The effectiveness of added human transferrin could be readily demonstrated on the cells in culture medium containing foetal calf serum, but transferrin-promoted uptake varied considerably between different batches of the serum. In serum-free medium, transferrin at concentrations as low as 1 μg ml−1 promoted substantial uptake of 67Ga and maximal uptake of 59Fe. Saturation of the transferrin with iron pre-empted its activity toward both tracers, indicating their transport requires binding to the same sites on transferrin. High affinity receptors for transferrin on the tumour cells were characterized by measurement of the binding of diferric 125I-labelled human transferrin to whole cells at 15°C. The HPC-108 line possessed 4 × 105 receptors per cell, WEHI-22 1.5 × 105 per cell, the EMT6 sarcoma line only 5 × 104 per cell, all with a dissociation constant of 1.4–2.3 nM. Some aspects of 67Ga. and 59Fe uptake were explained by the characteristics of this receptor and the previously demonstrated difference between the two tracers in affinity for transferrin. |
| Databáze: | OpenAIRE |
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