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

Wenxiao Xu | Zendy; Sheng-Zhi Liu | Zendy; Di Wu | Zendy; GuoFen Qiao | Zendy; Jinglong Yan | Zendy

Open Access

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

Author(s) -

Wenxiao Xu,

Sheng-Zhi Liu,

Di Wu,

GuoFen Qiao,

Jinglong Yan

Publication year - 2015

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.1159/000438525

Subject(s) - sumo protein , arsenic trioxide , acute promyelocytic leukemia , promyelocytic leukemia protein , chemistry , rnf4 , transfection , microbiology and biotechnology , cancer research , retinoic acid , apoptosis , biology , biochemistry , ubiquitin , zinc finger , transcription factor , gene

Promyelocytic leukemia (PML) protein is a tumor suppressor that fuses with retinoic acid receptor-α (PML-RARα) to contribute to the initiation of acute promyelocytic leukemia (APL). Arsenic trioxide (ATO) upregulates expression of TGF-β1, promoting collagen synthesis in osteoblasts, and ATO binds directly to PML to induce oligomerization, sumoylation, and ubiquitination. However, how ATO upregulates TGF-β1 expression is uncertain. Thus, we suggested that PML sumoylation is responsible for regulation of TGF-β1 protein expression.

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