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Blood, 1 September 2004, Vol. 104, No. 5, pp. 1314-1323.
Prepublished online as a Blood First Edition Paper on May 13, 2004; DOI 10.1182/blood-2004-01-0046.
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HEMATOPOIESIS
Comparative proteomic analysis of all-trans-retinoic acid treatment reveals systematic posttranscriptional control mechanisms in acute promyelocytic leukemia
Michael N. Harris,
Bulent Ozpolat,
Fadi Abdi,
Sheng Gu,
Allison Legler,
Kwasi G. Mawuenyega,
Maribel Tirado-Gomez,
Gabriel Lopez-Berestein, and
Xian Chen
From the Biosciences Division, Los Alamos National Laboratory, Los Alamos, NM; the Department of Bioimmunotherapy, Section of Immunobiology and Drug Carriers, University of Texas MD Anderson Cancer Center, Houston, TX; and Applied Biosystems, Framingham, MA.
All-trans-retinoic acid (ATRA) induces growth inhibition, differentiation, and apoptosis in cancer cells, including acute promyelocytic leukemia (APL). In APL, expression of promyelocytic leukemia protein retinoic acid receptor– (PML-RAR) fusion protein, owing to the t(15; 17) reciprocal translocation, leads to a block in the promyelocytic stage of differentiation. Here, we studied molecular mechanisms involved in ATRA-induced growth inhibition and myeloid cell differentiation in APL. By employing comprehensive high-throughput proteomic methods of 2-dimensional (2-D) gel electrophoresis and amino acid–coded mass tagging coupled with electrospray ionization (ESI) mass spectrometry, we systematically identified a total of 59 differentially expressed proteins that were consistently modulated in response to ATRA treatment. The data revealed significant down-regulation of eukaryotic initiation and elongation factors, initiation factor 2 (IF2), eukaryotic initiation factor 4AI (eIF4AI), eIF4G, eIF5, eIF6, eukaryotic elongation factor 1A-1 (eEF1A-1), EF-1- , eEF1 , 14-3-3 , and 14-3-3 / (P < .05). The translational inhibitor DAP5/p97/NAT1 (death-associated protein 5) and PML isoform-1 were found to be up-regulated (P < .05). Additionally, the down-regulation of heterogeneous nuclear ribonucleoproteins (hnRNPs) C1/C2, UP2, K, and F; small nuclear RNPs (snRNPs) D3 and E; nucleoprotein tumor potentiating region (TPR); and protein phosphatase 2A (PP2A) were found (P < .05); these were found to function in pre-mRNA processing, splicing, and export events. Importantly, these proteomic findings were validated by Western blot analysis. Our data in comparison with previous cDNA microarray studies and our reverse transcription–polymerase chain reaction (RT-PCR) experiments demonstrate that broad networks of posttranscriptional suppressive pathways are activated during ATRA-induced growth inhibition processes in APL.
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