Specific binding of ferric bovine transferrin to the human transferrin receptor was investigated using K562 cells propagated in serum-free medium without transferrin supplemented with elemental iron. Affinit chromatography of solubilized extracts of K562 cells surface-labeled with 5l was performed u
Demonstration of the transferrin receptor in human breast cancer tissue. Potential marker for identifying dividing cells
✍ Scribed by Jeffrey E. Shindelman; Ann E. Ortmeyer; Howard H. Sussman
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- French
- Weight
- 495 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0020-7136
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✦ Synopsis
Abstract
A transferrin receptor was demonstrated in tumor tissue from 10 patients with breast carcinoma and one patient with breast sarcoma. Binding studies were conducted by measuring the amount of ^125^I‐transferrin binding to microsomal preparations of the tumor tissue. Elevated levels of specific transferrin binding were found in the tumors with a range of 11–35% of bound transferrin, whereas microsomes prepared from non‐neoplastic breast tissue samples bound only 2.3% and 2.4% of the transferrin. Scatchard analysis of binding studies conducted with tissues from a breast cancer and from a breast sarcoma indicate that the receptor has a Ka = 9.0 × 10^8^M. The binding site is specific for transferrin, as studies show that non‐radioactive transferrin displaced labelled transferrin, while human IgG and human albumin did not. The receptor‐transferrin complex was precipitated from a detergent extract of the breast sarcoma with antiserum to human transferrin. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis of the immunoprecipitate gave a polypeptide of M~r~ 90,000 daltons, which is of similar molecular weight found for the putative transferrin receptor in all of a series of human cultured cell lines previously examined.
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