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P53 becomes transcriptionally active during erythropoietin induced differentiation Identification of p53-regulated genes


, : P53 becomes transcriptionally active during erythropoietin induced differentiation Identification of p53-regulated genes. Blood 96(11 Part 1): 672a, November 16

Available evidence suggests that p53 participates in hematopoiesis although the biochemical pathways and downstream effectors of this process are unknown. We have observed significantly higher RBC, hematocrit, and platelet counts in p53 wild type animals compared to p53 null litter mates. Furthermore, this difference appeared specific for the erythroid and megakaryocytic lineages, as no significant difference in WBC counts was observed. These findings prompted us to investigate the role of p53 in erythropoiesis. A well-characterized model of normal terminal erythroid differentiation was used. Primary erythroblasts were purified from the spleens of p53 wild type and null mice infected with the anemia-inducing strain of Friend virus. Western blot analysis demonstrated that, during Epo-induced differentiation, p53 protein accumulated steadily, and subsequent electrophoretic mobility shift assays (EMSA) indicated that the protein was transcriptionally active. To characterize further the transcriptional activity of p53, we sought to identify p53-responsive genes expressed in differentiating erythroblasts. Poly (A+) RNA from p53 wild type and null erythroblasts was isolated after the cells had been cultured in the presence of Epo for 6 hours (the time of maximal p53 transcriptional activity as determined by EMSA experiments). Representational difference analysis of cDNA was used to identify gene products that were differentially expressed in the two populations. Those genes identified as targets of p53 mediated trans-activation included matrilin-4 (an extracellular matrix protein) and Bcap 37 (a homolog of the antiproliferative protein, prohibitin). Additionally, expression of two novel transcripts (one of which contained regions of both protease and integrin homology) was upregulated by p53. Targets of p53-mediated repression included the p85 regulatory subunit of PI-3-kinase and at least two novel genes. PI-3-kinase mediated signal transduction is known to be involved in the biochemical response to Epo. Furthermore, p85 has been shown to interact directly with the Epo receptor. Repression of p85, along with induction of a prohibitin homology, suggests that p53 may restrict Epo-induced erythroid proliferation. This study provides insight into the role of p53 in erythropoiesis and is the first to characterize the pattern of p53-regulated gene expression during normal hematopoietic differentiation.

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