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Momordicine I induces ER stress and inhibits OSCC by targeting ribosomal proteins
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Jianlu KONG, Ziyu ZHU, Yijie HU, Siyi ZHOU, Tianyi GU, Xiao SHEN, Huiming WANG, Mengfei YU, Yu LIU. Momordicine I induces ER stress and inhibits OSCC by targeting ribosomal proteins[J]. Journal of Zhejiang University Science B, 1998, -1(-1): .
@article{title="Momordicine I induces ER stress and inhibits OSCC by targeting ribosomal proteins",
author="Jianlu KONG, Ziyu ZHU, Yijie HU, Siyi ZHOU, Tianyi GU, Xiao SHEN, Huiming WANG, Mengfei YU, Yu LIU",
journal="Journal of Zhejiang University Science B",
volume="-1",
number="-1",
pages="",
year="1998",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B2500142"
}
%0 Journal Article
%T Momordicine I induces ER stress and inhibits OSCC by targeting ribosomal proteins
%A Jianlu KONG
%A Ziyu ZHU
%A Yijie HU
%A Siyi ZHOU
%A Tianyi GU
%A Xiao SHEN
%A Huiming WANG
%A Mengfei YU
%A Yu LIU
%J Journal of Zhejiang University SCIENCE B
%V -1
%N -1
%P
%@ 1673-1581
%D 1998
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B2500142
TY - JOUR
T1 - Momordicine I induces ER stress and inhibits OSCC by targeting ribosomal proteins
A1 - Jianlu KONG
A1 - Ziyu ZHU
A1 - Yijie HU
A1 - Siyi ZHOU
A1 - Tianyi GU
A1 - Xiao SHEN
A1 - Huiming WANG
A1 - Mengfei YU
A1 - Yu LIU
J0 - Journal of Zhejiang University Science B
VL - -1
IS - -1
SP -
EP -
%@ 1673-1581
Y1 - 1998
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B2500142
Abstract: oral squamous cell carcinoma (OSCC) is one of the most common malignant tumors worldwide. This necessitates the development of innovative drugs with high efficiency, low toxicity, and good tolerance. Bitter melon extract has been reported to have potent anticancer activity against OSCC. We evaluated the effects of nine triterpenoids from bitter melon extract on OSCC using CCK8 proliferation and Transwell migration assays. Among the nine triterpenoids, momordicine I (MI) exhibited the strongest anticancer activity against OSCC. Animal experiments also showed that MI inhibited OSCC cell growth in vivo. Additionally, MI decreased the mitochondrial membrane potential and promoted apoptosis in OSCC. RNA-seq analysis revealed that MI induced an unfolded protein response (UPR) and endoplasmic Reticulum (ER) stress, which was confirmed by western blotting and RT-qPCR. Cellular thermal shift assay (CETSA) and mass spectrometry (MS) analysis, combined with molecular docking, identified ribosomal proteins (RPL7, RPL11, RPL12, RPL18, RPL30, RPL38, RPS13, RPS25) as MI targets. By targeting ribosomal proteins, MI likely disrupts ribosome-mediated protein folding, leading to UPR and ER stress. In summary, MI targets ribosomal proteins to induce ER stress and inhibit OSCC, highlighting its therapeutic potential.
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