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Subunit structure of the erythropoietin receptor analyzed by 125I-Epo
cross-linking in cells expressing wild-type or mutant receptors
O Miura and JN Ihle
Department of Biochemistry, St Jude Children's Research Hospital, Memphis,
TN 38105.
To analyze the structure of the murine erythropoietin receptor (EpoR),
wild-type or mutant EpoR cDNAs were expressed in cell lines, and the
proteins that cross-linked with 125I-labeled erythropoietin (Epo) were
analyzed by immunoprecipitation using an antibody against the intracellular
region of the cloned EpoR. COS-7 cell transfectants expressing the
wild-type EpoR showed two major cross-linked species of 145 and 110 Kd,
both of which were recognized by the antibody against the cloned EpoR after
denaturation under reducing conditions. Furthermore, a reduction in sizes
of both cross-linked bands was observed in COS-7 transfectants expressing a
mutant receptor with an internal deletion, thus indicating that both
species contain the cloned EpoR. COS-7 cells expressing mutant receptors
with carboxy-terminal deletions showed cross-linked bands corresponding to
the smaller species of the two observed in cells expressing the wild-type
receptor. In contrast to COS-7 cell transfectants, DA3 cells expressing
wild-type or mutant EpoR cDNAs showed an additional cross-like species of
130 Kd. The size of this species was not altered by deletions in EpoR,
showing that it did not contain EpoR. The 130-Kd cross-linked band, which
would contain a 95-Kd protein, was also observed in a murine
erythroleukemia cell line, D1B. These results suggest that Epo associates
with a second component of 95 Kd, which is specifically expressed in
hematopoietic cells.
Volume 81,
Issue 7,
pp. 1739-1744,
04/01/1993
Copyright © 1993 by The American Society of Hematology
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