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Blood, Vol. 93 No. 6 (March 15), 1999:
pp. 2111-2120
Identification of the Poly(C) Binding Protein in the Complex
Associated With the 3' Untranslated Region of Erythropoietin
Messenger RNA
Maria F. Czyzyk-Krzeska and
Amy C. Bendixen
From the Department of Molecular and Cellular Physiology, University
of Cincinnati, College of Medicine, Cincinnati, OH.
Hypoxia regulates expression of erythropoietin (EPO), a glycoprotein
that stimulates erythrocytosis, at the level of transcription and also
possibly at the level of messenger RNA (mRNA) stability. A
pyrimidine-rich region within the EPO mRNA 3' untranslated region was implicated in regulation of EPO mRNA stability element and shown to
bind protein factors. In the present study we wished to identify the
protein factor binding to the pyrimidine-rich sequence in the EPO mRNA
stability element. Using mobility shift assays, ultraviolet light
cross-linking, and sodium dodecyl sulfate-polyacrylamide gel
electrophoresis (SDS-PAGE), and electroelution of protein factors from
the gel slices corresponding to the ribonucleoprotein complexes, we
found that two isoforms of a 40 kD poly(C) binding protein (PCBP, also
known as  CP or hnRNPE), PCBP1, and PCBP2 are
present in that complex. In Hep3B or HepG2 cells hypoxia induces neither expression of PCBP nor formation of the ribonucleoprotein complex associated with EPO mRNA that involves PCBP.
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