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Changes in redox affect the activity of erythropoietin RNA binding protein
Author(s) -
Rondon Isaac J.,
Scandurro Aline B.,
Wilson Russell B.,
Beckman Barbara S.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00066-i
Subject(s) - redox , erythropoietin , affect (linguistics) , chemistry , rna binding protein , rna , biochemistry , microbiology and biotechnology , biophysics , biology , endocrinology , psychology , inorganic chemistry , communication , gene
We have previously identified a cytosolic protein, erythropoietin RNA binding protein (ERBP), which is up‐regulated in certain tissues in response to hypoxia. To further characterize the interaction of ERBP and erythropoietin (EPO) mRNA, we have examined the role of reduction‐oxidation in the EPO mRNA binding mechanism of ERBP isolated from human hepatoma cells (Hep3B). Reducing agents dithiothreitol (DTT) and 2‐mercaptoethanol (2‐ME) increased ERBP binding activity in a concentration‐dependent manner, whereas the oxidizing agent, diamide, abolished ERBP binding activity. In addition, treatment of Hep3B cell lysates with the irreversible sulfhydryl alkylating agent N ‐ethylmaleimide resulted in inhibition of the EPO mRNA‐ERBP complex. Taken together, these findings suggest that sulfhydryl groups may play a role in vivo in the regulation of EPO production through the modulation of ERBP binding activity.