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Paris saponin VII promotes TRIP12-mediated SOD1 degradation to synergize with idarubicin in ROS-dependent acute myeloid leukemia cell death.

Created on 06 Aug 2026

Authors

Runfeng Ni, Ning Ding, Yirong Shi, Milin Liu, Jing Wang, Yuchen Tao, Jizhang Bao, Yuanfei Mao, Jiahui Lu

Published in

Phytomedicine : international journal of phytotherapy and phytopharmacology. Volume 160. Pages 158662. Jul 29, 2026. Epub Jul 29, 2026.

Abstract

Acute myeloid leukemia (AML) cells evade apoptosis through antioxidant mechanisms. Paris saponin VII (PS VII), a steroidal saponin, exhibits antitumor activity in solid malignancies, but its role in AML remains unclear.
This study investigated the antileukemic effects of PS VII on AML and the underlying mechanism, and evaluated its synergy with idarubicin (Ida).
Using human SKM-1 and murine C1498 AML cell lines, we assessed antileukemic effects of PS VII in vitro. Subcutaneous and systemic leukemia mouse models were employed for in vivo validation. Mechanistic studies integrated DIA-based proteomics, co-immunoprecipitation, surface plasmon resonance, and ubiquitination assays to elucidate the molecular basis.
PS VII bound to superoxide dismutase 1 (SOD1) and promoted its proteasomal degradation. This process was mediated by TRIP12-dependent K48-linked polyubiquitination at lysine residues 10 and 37. SOD1 degradation elevated reactive oxygen species (ROS) levels and induced mitochondrial dysfunction. High SOD1 expression was associated with poor prognosis in AML patients. PS VII and Ida synergistically induced ROS-dependent apoptosis in vitro and in vivo.
PS VII functions as a natural compound SOD1 degrader that triggers ROS-dependent AML cell death through TRIP12-mediated ubiquitin-proteasomal degradation. Its synergy with Ida provides a potential combination strategy that increases cellular sensitivity to oxidative stress and cell death.

PMID:
42555990
Bibliographic data and abstract were imported from PubMed on 06 Aug 2026.

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