Sumoylation of the Tumor Suppressor Promyelocytic Leukemia Protein Regulates Arsenic Trioxide-Induced Collagen Synthesis in Osteoblasts

• DOI: 10.1159/000438525
• Publication Date: 2015-10-30T22:01:37Z
• Authors: Wen-Xiao Xu; Sheng-Zhi Liu; Di Wu; Guo-Fen Qiao; Jinglong Yan
• Keywords: Arsenic Trioxide; Promyelocytic leukemia protein; RNF4

Background/Aims: Promyelocytic leukemia (PML) protein is a tumor suppressor that fuses with retinoic acid receptor-α (PML-RARα) to contribute the initiation of acute promyelocytic (APL). Arsenic trioxide (ATO) upregulates expression TGF-β1, promoting collagen synthesis in osteoblasts, and ATO binds directly PML induce oligomerization, sumoylation, ubiquitination. However, how TGF-β1 uncertain. Thus, we suggested sumoylation responsible for regulation expression. Methods: Kunming mice were treated ATO, osteoblasts counted under scanning electron microscopy. Masson's staining was used quantify content. hFOB1.19 cells transfected siRNA against UBC9 or RNF4, then FBS. expression, quantified Western blot, via immunocytochemistry. Results: enhanced osteoblast accumulation, synthesis, PML-NB formation vivo. Knocking down inhibited ATO- FBS-induced synthesis. Conversely, knocking RNF4 Conclusion: These data suggest required ATO-induced osteoblasts.