Elemene as a binding stabilizer of microRNA-145-5p suppresses the growth of non-small cell lung cancer.

Meirong ZHOU; Jiayue WANG; Yulin PENG; Xiangge TIAN; Wen ZHANG; Junlin CHEN; Yue WANG; Yu WANG; Youjian YANG; Yongwei ZHANG; Xiaokui HUO; Yuzhuo WU; Zhenlong YU; Tian XIE; Xiaochi MA

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Elemene as a binding stabilizer of microRNA-145-5p suppresses the growth of non-small cell lung cancer.

Author: Meirong ZHOU ¹ ; Jiayue WANG ¹ ; Yulin PENG ¹ ; Xiangge TIAN ¹ ; Wen ZHANG ¹ ; Junlin CHEN ¹ ; Yue WANG ¹ ; Yu WANG ² ; Youjian YANG ² ; Yongwei ZHANG ² ; Xiaokui HUO ¹ ; Yuzhuo WU ¹ ; Zhenlong YU ³ ; Tian XIE ⁴ ; Xiaochi MA ¹
Author Information

1. Second Affiliated Hospital, Dalian Medical University, Dalian, Liaoning, 116000, China.
2. Research & Production Department, Dalian Huali Jingang Pharmaceutical Co., Ltd., Dalian, Liaoning, 116110, China.
3. College of Pharmacy, Dalian Medical University, Dalian, Liaoning, 116044, China.
4. Key Laboratory of Elemene Class Anti-Cancer Chinese Medicines, College of Pharmacy, Hangzhou Normal University, Hangzhou, 311121, China.
Publication Type:Journal Article
Keywords: Elemene; Inflammatory; Non-small cell lung cancer; Nuclear factor kappaB; microRNA-145-5p
From: Journal of Pharmaceutical Analysis 2025;15(3):101118-101118
CountryChina
Language:English
Abstract: Elemene is widely recognized as an effective anti-cancer compound and is routinely administered in Chinese clinical settings for the management of several solid tumors, including non-small cell lung cancer (NSCLC). However, its detailed molecular mechanism has not been adequately demonstrated. In this research, it was demonstrated that elemene effectively curtailed NSCLC growth in the patient-derived xenograft (PDX) model. Mechanistically, employing high-throughput screening techniques and subsequent biochemical validations such as microscale thermophoresis (MST), microRNA-145-5p (miR-145-5p) was pinpointed as a critical target through which elemene exerts its anti-tumor effects. Interestingly, elemene serves as a binding stabilizer for miR-145-5p, demonstrating a strong binding affinity (dissociation constant (K _D) = 0.39 ± 0.17 μg/mL) and preventing its degradation both in vitro and in vivo, while not interfering with the synthesis of the primary microRNA transcripts (pri-miRNAs) and precursor miRNAs (pre-miRNAs). The stabilization of miR-145-5p by elemene resulted in an increased level of this miRNA, subsequently suppressing NSCLC progression through the miR-145-5p/mitogen-activated protein kinase kinase kinase 3 (MAP3K3)/nuclear factor kappaB (NF-κB) pathway. Our findings provide a new perspective on revealing the interaction patterns between clinical anti-tumor drugs and miRNAs.