Reelin is an extracellular glycoprotein that is highly conserved in mammals. In addition to its expression in the nervous system, Reelin is present in erythroid cells but its function there is unknown. We report in this study that Reelin is up-regulated during erythroid differentiation of human erythroleukemic K562 cells and is expressed in the erythroid progenitors of murine bone marrow. Reelin deficiency promotes erythroid differentiation of K562 cells and augments erythroid production in murine bone marrow. In accordance with these findings, Reelin deficiency attenuates AKT phosphorylation of the Ter119(+)CD71(+) erythroid progenitors and alters the cell number and frequency of the progenitors at different erythroid differentiation stages. A regulatory role of Reelin in erythroid differentiation is thus defined.
Keywords: 3,3′,5,5′-tetramethylbenzidine; EPO; Erythroid differentiation; FBS; HRP; Hb; Hct; K562 cell; MCH; MCHC; MCV; NFAT; NaB; PAGE; PBS; PVDF; RDW; RPMI; Reeler mice; Reelin; Roswell Park Memorial Institute; SDS; Sodium butyrate; TMB; erythropoietin; fetal bovine serum; hematocrit; hemoglobin; horseradish peroxidase; mean corpuscular hemoglobin; mean corpuscular hemoglobin concentration; mean corpuscular volume; nuclear factor of activated T cells; phosphate-buffered saline; polyacrylamide gel electrophoresis; polyvinylidene fluoride; red blood cell distribution width; sodium butyrate; sodium dodecyl sulfate.
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