LD-110, a potent LSD1 PROTAC degrader, suppresses tumor growth by inducing ER stress and apoptosis

Lysine-specific demethylase 1 (LSD1, also known as KDM1A) is frequently overexpressed in multiple cancer types and associated with poor prognosis of cancer patients. While LSD1 represents a compelling therapeutic target, clinical development of small-molecule inhibitors has been hampered by dose-limiting toxicities and off-target effects. In this study, we reported the discovery of LD-110 as a potent proteolysis targeting chimera (PROTAC) specifically engineered for LSD1 degradation. LD-110 effectively degrades LSD1 via the ubiquitin-proteasome system and significantly suppresses the growth and survival of breast and lung cancer cells. Mechanistically, LD-110 triggers endoplasmic reticulum stress by activating the ATF4-CHOP signal to increase NOXA levels, but decrease MCL1 levels, along with increasing ROS production and prolonged DNA damage to trigger phosphorylation of GCN2 and eIF2α for enhanced ATF4 translation, ultimately inducing apoptotic cell death. Importantly, LD-110 demonstrated a good in vivo pharmacokinetic profile and effectively inhibited in vivo tumor growth in breast and lung xenograft tumor models. Collectively, we discovered a potent PROTAC degrader targeting LSD1 with effective anti-cancer activity for future development as a promising anti-cancer agent.

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Publication Details

Journal
Science Bulletin
Published
2025-10-21
DOI
https://doi.org/10.1016/j.scib.2025.10.024
Citations
3
Primary Topic
Protein Degradation and Inhibitors
Type
article
Field-Weighted Citation Impact
2.42
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article

LD-110, a potent LSD1 PROTAC degrader, suppresses tumor growth by inducing ER stress and apoptosis

Xiufang Xiong, Yi Sun, Xin Han, Mengting Liang et al.
3 citations
Science Bulletin
Protein Degradation and Inhibitors
2.42
article

LD-110, a potent LSD1 PROTAC degrader, suppresses tumor growth by inducing ER stress and apoptosis

Xiufang Xiong, Yi Sun, Xin Han, Mengting Liang, Danyi Zhai, Lihua Liu, Lan Li, Li Chen, Yu Yang, Xin Zhou, Yan Yin, Jiezhen Zhuo
article en
3 citations

Abstract

Lysine-specific demethylase 1 (LSD1, also known as KDM1A) is frequently overexpressed in multiple cancer types and associated with poor prognosis of cancer patients. While LSD1 represents a compelling therapeutic target, clinical development of small-molecule inhibitors has been hampered by dose-limiting toxicities and off-target effects. In this study, we reported the discovery of LD-110 as a potent proteolysis targeting chimera (PROTAC) specifically engineered for LSD1 degradation. LD-110 effectively degrades LSD1 via the ubiquitin-proteasome system and significantly suppresses the growth and survival of breast and lung cancer cells. Mechanistically, LD-110 triggers endoplasmic reticulum stress by activating the ATF4-CHOP signal to increase NOXA levels, but decrease MCL1 levels, along with increasing ROS production and prolonged DNA damage to trigger phosphorylation of GCN2 and eIF2α for enhanced ATF4 translation, ultimately inducing apoptotic cell death. Importantly, LD-110 demonstrated a good in vivo pharmacokinetic profile and effectively inhibited in vivo tumor growth in breast and lung xenograft tumor models. Collectively, we discovered a potent PROTAC degrader targeting LSD1 with effective anti-cancer activity for future development as a promising anti-cancer agent.

Science BulletinVol. 70(23)
Zhejiang Cancer Hospital (CN), EduInnovation (US)
Openalex Percentile: Top 10%
Protein Degradation and Inhibitors
2.42
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