Identification of the poly (C) binding protein in the complex associated with the 3′ untranslated region of erythropoietin messenger RNA
MF Czyzyk-Krzeska… - Blood, The Journal of the …, 1999 - ashpublications.org
MF Czyzyk-Krzeska, AC Bendixen
Blood, The Journal of the American Society of Hematology, 1999•ashpublications.orgHypoxia 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 …
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 …
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.
ashpublications.org