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J. Biol. Chem., Vol. 266, Issue 24, 16015-16020, 08, 1991
N Casadevall, C Lacombe, O Muller, S Gisselbrecht and P Mayeux
In erythroleukemia cells infected with the polycythemia strain of the
Friend virus complex, erythropoietin could be cross-linked mainly to a
protein of 63 kDa when using disuccinimidyl suberate. In contrast,
erythropoietin in other erythroleukemia cells cross-linked to two proteins
of 85 and 100 kDa. When native erythropoietin receptor complexes were
immunoprecipitated, the 63-kDa erythropoietin-cross- linked protein could
be precipitated both by antibodies directed against the intracellular part
of the cloned chain of the erythropoietin receptor and by antibodies
directed against the envelope proteins of the Friend virus. However, after
denaturation of the complexes, the 63-kDa protein was only precipitated by
antibodies directed against the envelope proteins of the Friend virus.
Enzymatic deglycosylation confirmed that erythropoietin was cross-linked
with the envelope protein of the defective virus and bidimensional diagonal
gel electrophoresis analyses showed that some of the erythropoietin cross-
linked envelope proteins were dimerized by disulfide bonds. Thus, the main
erythropoietin-receptor complex in the plasma membrane of these cells
consisted of a molecule of the cloned chain of the erythropoietin receptor
noncovalently associated with one or two disulfide-bonded molecule(s) of
the envelope protein of the defective virus. Moreover, our results also
showed that the viral envelope protein associated with the cloned chain of
the erythropoietin receptor at a site distinct from the erythropoietin
binding site.
Multimeric structure of the membrane erythropoietin receptor of murine erythroleukemia cells (Friend cells). Cross-linking of erythropoietin with the spleen focus-forming virus envelope protein
ICGM, INSERM U 152, Hopital Cochin, Paris, France.
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