Expression and characterization of erythropoietin receptors on normal human bone marrow cells
We studied the specific binding of /sup 125/I-labeled bioactive recombinant human erythropoietin (Epo) to human bone marrow mononuclear cells (BMNC) obtained from normal subjects. The /sup 125/I-labeled Epo bound specifically to the BMNC. Scatchard analysis of the data showed two classes of binding sites; one high affinity (Kd 0.07 nM) and the other low affinity (Kd 0.38 nM). The number of Epo binding sites per BMNC was 46 +/- 16 high-affinity receptors and 91 +/- 51 low-affinity receptors. The specific binding was displaced by unlabeled Epo, but not by other growth factors. Receptor internalization was observed significantly at 37 degrees C, but was prevented by the presence of 0.2% sodium azide. These findings indicate that human BMNC possess two classes of specific Epo receptors with characteristics of a hormone-receptor association.
- Research Organization:
- Tokyo Women's Medical College (Japan)
- OSTI ID:
- 5879257
- Journal Information:
- Int. J. Cell Cloning; (United States), Vol. 7:3
- Country of Publication:
- United States
- Language:
- English
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MAN
MONOCYTES
TRACER TECHNIQUES
ANIMAL CELLS
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BETA DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
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ELECTRON CAPTURE RADIOISOTOPES
INTERMEDIATE MASS NUCLEI
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MEMBRANE PROTEINS
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ORGANIC COMPOUNDS
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550201* - Biochemistry- Tracer Techniques