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Friend erythroleukemia cell membrane transferrin receptors
Canadian Journal of Biochemistry
|October 1, 1980
Summary
Induced Friend erythroleukemia cells exhibit transferrin uptake similar to reticulocytes. This suggests a shared mechanism for iron transport in differentiating erythroid cells, involving specific transferrin-binding proteins.
Area of Science:
- Cell Biology
- Hematology
- Biochemistry
Background:
- Transferrin is the primary iron transport protein in serum.
- Erythroid differentiation involves significant iron uptake.
- Friend erythroleukemia cells are a model for studying erythroid development.
Purpose of the Study:
- To compare transferrin uptake in induced and uninduced murine Friend erythroleukemia cells with murine reticulocytes.
- To identify and characterize transferrin-binding components in erythroid cells.
Main Methods:
- Dimethyl sulfoxide (DMSO) induction of erythroid differentiation in Friend cells.
- Measurement of transferrin uptake via radiolabeling.
- Detergent extraction of cell membranes.
- Immunoprecipitation using anti-transferrin antibody.
- Electrophoresis on sodium dodecyl sulfate (SDS) gels.
Main Results:
- Induced Friend cells showed transferrin uptake quantitatively and qualitatively similar to reticulocytes.
- Uninduced Friend cells exhibited negligible transferrin uptake.
- Specific transferrin-binding activity was detected in membranes of induced cells.
- A single protein with transferrin-binding activity was isolated and characterized.
Conclusions:
- Erythroid differentiation in Friend cells upregulates transferrin uptake.
- A specific transferrin-binding protein, similar to that in reticulocytes, is involved in iron transport during erythropoiesis.