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3. 6-n-Butoxy-10-nitro-12,13-dioxa-11-azatricyclo[7.3.1.02,7]trideca-2,4,6,10-tetraene Improves the X-ray Sensitivity on Inhibiting Proliferation and Promoting Oxidative Stress and Apoptosis of Oral Cancer Cells

Author

Yang, Kun-Han, primary, Yen, Ching-Yu, additional, Wang, Sheng-Chieh, additional, Chang, Fang-Rong, additional, Chang, Meng-Yang, additional, Chan, Chieh-Kai, additional, Jeng, Jiiang-Huei, additional, Tang, Jen-Yang, additional, and Chang, Hsueh-Wei, additional

Published
2024
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5. Ferroptosis-Regulated Natural Products and miRNAs and Their Potential Targeting to Ferroptosis and Exosome Biogenesis.

Author

Chuang, Ya-Ting, Yen, Ching-Yu, Chien, Tsu-Ming, Chang, Fang-Rong, Tsai, Yi-Hong, Wu, Kuo-Chuan, Tang, Jen-Yang, and Chang, Hsueh-Wei

Subjects
NATURAL products, EXOSOMES, MICRORNA, EXTRACELLULAR vesicles, TREATMENT effectiveness
Abstract

Ferroptosis, which comprises iron-dependent cell death, is crucial in cancer and non-cancer treatments. Exosomes, the extracellular vesicles, may deliver biomolecules to regulate disease progression. The interplay between ferroptosis and exosomes may modulate cancer development but is rarely investigated in natural product treatments and their modulating miRNAs. This review focuses on the ferroptosis-modulating effects of natural products and miRNAs concerning their participation in ferroptosis and exosome biogenesis (secretion and assembly)-related targets in cancer and non-cancer cells. Natural products and miRNAs with ferroptosis-modulating effects were retrieved and organized. Next, a literature search established the connection of a panel of ferroptosis-modulating genes to these ferroptosis-associated natural products. Moreover, ferroptosis-associated miRNAs were inputted into the miRNA database (miRDB) to bioinformatically search the potential targets for the modulation of ferroptosis and exosome biogenesis. Finally, the literature search provided a connection between ferroptosis-modulating miRNAs and natural products. Consequently, the connections from ferroptosis–miRNA–exosome biogenesis to natural product-based anticancer treatments are well-organized. This review sheds light on the research directions for integrating miRNAs and exosome biogenesis into the ferroptosis-modulating therapeutic effects of natural products on cancer and non-cancer diseases. [ABSTRACT FROM AUTHOR]

Published
2024
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8. Demethoxymurrapanine, an indole‐naphthoquinone alkaloid, inhibits the proliferation of oral cancer cells without major side effects on normal cells.

Author

Chuang, Ya‐Ting, Yen, Ching‐Yu, Shiau, Jun‐Ping, Chang, Fang‐Rong, Duh, Chang‐Yih, Sung, Ping‐Jyun, Chen, Kuan‐Liang, Tsai, Yi‐Hong, Tang, Jen‐Yang, Jeng, Jiiang‐Huei, Sheu, Jyh‐Horng, and Chang, Hsueh‐Wei

Subjects
CANCER cell proliferation, ORAL mucosa, ORAL cancer, REACTIVE oxygen species, SUPEROXIDES, CANCER cells, DNA damage, ALKALOIDS
Abstract

Antioral cancer drugs need a greater antiproliferative impact on cancer than on normal cells. Demethoxymurrapanine (DEMU) inhibits proliferation in several cancer cells, but an in‐depth investigation was necessary. This study evaluated the proliferation‐modulating effects of DEMU, focusing on oral cancer and normal cells. DEMU (0, 2, 3, and 4 μg/mL) at 48 h treatments inhibited the proliferation of oral cancer cells (the cell viability (%) for Ca9‐22 cells was 100.0 ± 2.2, 75.4 ± 5.6, 26.0 ± 3.8, and 15.4 ± 1.4, and for CAL 27 cells was 100.0 ± 9.4, 77.2 ± 5.9, 57.4 ± 10.7, and 27.1 ± 1.1) more strongly than that of normal cells (the cell viability (%) for S‐G cells was 100.0 ± 6.6, 91.0 ± 4.6, 95.0 ± 2.6, and 95.8 ± 5.5), although this was blocked by the antioxidant N‐acetylcysteine. The presence of oxidative stress was evidenced by the increase of reactive oxygen species and mitochondrial superoxide and the downregulation of the cellular antioxidant glutathione in oral cancer cells, but these changes were minor in normal cells. DEMU also caused greater induction of the subG1 phase, extrinsic and intrinsic apoptosis (annexin V and caspases 3, 8, and 9), and DNA damage (γH2AX and 8‐hydroxy‐2‐deoxyguanosine) in oral cancer than in normal cells. N‐acetylcysteine attenuated all these DEMU‐induced changes. Together, these data demonstrate the preferential antiproliferative function of DEMU in oral cancer cells, with the preferential induction of oxidative stress, apoptosis, and DNA damage in these cancer cells, and low cytotoxicity toward normal cells. [ABSTRACT FROM AUTHOR]

Published
2024
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9. 6- n -Butoxy-10-nitro-12,13-dioxa-11-azatricyclo[7.3.1.0 2,7 ]trideca-2,4,6,10-tetraene Improves the X-ray Sensitivity on Inhibiting Proliferation and Promoting Oxidative Stress and Apoptosis of Oral Cancer Cells.

Author

Yang, Kun-Han, Yen, Ching-Yu, Wang, Sheng-Chieh, Chang, Fang-Rong, Chang, Meng-Yang, Chan, Chieh-Kai, Jeng, Jiiang-Huei, Tang, Jen-Yang, and Chang, Hsueh-Wei

Subjects
ORAL cancer, CANCER cells, OXIDATIVE stress, REACTIVE oxygen species, APOPTOSIS
Abstract

This in vitro study examines the anti-oral cancer effects and mechanisms of a combined X-ray/SK2 treatment, i.e., X-ray and 6-n-butoxy-10-nitro-12,13-dioxa-11-azatricyclo[7.3.1.02,7]trideca-2,4,6,10-tetraene (SK2). ATP cell viability and flow cytometry-based cell cycle, apoptosis, oxidative stress, and DNA damage assessments were conducted. The X-ray/SK2 treatment exhibited lower viability in oral cancer (Ca9-22 and CAL 27) cells than in normal (Smulow–Glickman, S-G) cells, i.e., 32.0%, 46.1% vs. 59.0%, which showed more antiproliferative changes than with X-ray or SK2 treatment. Oral cancer cells under X-ray/SK2 treatment showed slight subG1 and G2/M increments and induced high annexin V-monitored apoptosis compared to X-ray or SK2 treatment. The X-ray/SK2 treatment showed higher caspase 3 and 8 levels for oral cancer cells than other treatments. X-ray/SK2 showed a higher caspase 9 level in CAL 27 cells than other treatments, while Ca9-22 cells showed similar levels under X-ray and/or SK2. The X-ray/SK2 treatment showed higher reactive oxygen species (ROS) generation and mitochondrial membrane potential (MMP) depletion than other treatments. Meanwhile, the mitochondrial superoxide (MitoSOX) and glutathione levels in X-ray/SK2 treatment did not exhibit the highest rank compared to others. Moreover, oral cancer cells had higher γH2AX and/or 8-hydroxy-2-deoxyguanosine levels from X-ray/SK2 treatment than others. All these measurements for X-ray/SK2 in oral cancer cells were higher than in normal cells and attenuated by N-acetylcysteine. In conclusion, X-ray/SK2 treatment showed ROS-dependent enhanced antiproliferative, apoptotic, and DNA damage effects in oral cancer cells with a lower cytotoxic influence on normal cells. [ABSTRACT FROM AUTHOR]

Published
2024
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14. The neddylation inhibitor MLN4924 inhibits proliferation and triggers apoptosis of oral cancer cells but not for normal cells.

Author

Chen, Yan‐Ning, Chan, Yu‐Hsuan, Shiau, Jun‐Ping, Farooqi, Ammad Ahmad, Tang, Jen‐Yang, Chen, Kuan‐Liang, Yen, Ching‐Yu, and Chang, Hsueh‐Wei

Subjects
ORAL cancer, ORAL mucosa, APOPTOSIS inhibition, APOPTOSIS, REACTIVE oxygen species, CANCER cells, MITOCHONDRIAL membranes, MEMBRANE potential
Abstract

Increased neddylation benefits the survival of several types of cancer cells. The inhibition of neddylation has the potential to exert anticancer effects but is rarely assessed in oral cancer cells. This study aimed to investigate the antiproliferation potential of a neddylation inhibitor MLN4924 (pevonedistat) for oral cancer cells. MLN4924 inhibited the cell viability of oral cancer cells more than that of normal oral cells (HGF‐1) with 100% viability, that is, IC50 values of oral cancer cells (CAL 27, OC‐2, and Ca9‐22) are 1.8, 1.4, and 1.9 μM. MLN4924 caused apoptotic changes such as the subG1 accumulation, activation of annexin V, pancaspase, and caspases 3/8/9 of oral cancer cells at a greater rate than in normal oral cells. MLN4924 induced greater oxidative stress in oral cancer cells compared to normal cells by upregulating reactive oxygen species and mitochondrial superoxide and depleting the mitochondrial membrane potential and glutathione. In oral cancer cells, preferential inductions also occurred for DNA damage (γH2AX and 8‐oxo‐2′‐deoxyguanosine). Therefore, this investigation demonstrates that MLN4924 is a potential anti‐oral‐cancer agent showing preferential inhibition of apoptosis and promotion of DNA damage with fewer cytotoxic effects on normal cells. [ABSTRACT FROM AUTHOR]

Published
2024
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46. Sequential Phosphorylation of Hepatitis C Virus NS5A Protein Requires the ATP-Binding Domain of NS3 Helicase

Author

Chun-Chiao Yu, Pei-Chen Lin, Cho-Han Chiang, Shu-Tang Jen, Yen-Ling Lai, Shih-Chin Hsu, Lee-Chiang Lo, Jing-Jer Lin, Nei-Li Chan, and Ming-Jiun Yu

Subjects
Adenosine Triphosphatases, viruses, Immunology, Casein Kinase Ialpha, virus diseases, Hepacivirus, Viral Nonstructural Proteins, biochemical phenomena, metabolism, and nutrition, RNA-Dependent RNA Polymerase, Hepatitis C, Microbiology, digestive system diseases, Virus-Cell Interactions, Protein Domains, Virology, Insect Science, Humans, Phosphorylation, Polyproteins
Abstract

The propagation of the hepatitis C virus (HCV) is regulated in part by the phosphorylation of its nonstructural protein NS5A that undergoes sequential phosphorylation on several highly conserved serine residues and switches from a hypo- to a hyperphosphorylated state. Previous studies have shown that NS5A sequential phosphorylation requires NS3 encoded on the same NS3-NS4A-NS4B-NS5A polyprotein. Subtle mutations in NS3 without affecting its protease activity could affect NS5A phosphorylation. Given the ATPase domain in the NS3 COOH terminus, we tested whether NS3 participates in NS5A phosphorylation similarly to the nucleoside diphosphate kinase-like activity of the rotavirus NSP2 nucleoside triphosphatase (NTPase). Mutations in the NS3 ATP-binding motifs blunted NS5A hyperphosphorylation and phosphorylation at serines 225, 232, and 235, whereas a mutation in the RNA-binding domain did not. The phosphorylation events were not rescued with wild-type NS3 provided in trans. When provided with an NS3 ATPase-compatible ATP analog, N(6)-benzyl-ATP-γ-S, thiophosphorylated NS5A was detected in the cells expressing the wild-type NS3-NS5B polyprotein. The thiophosphorylation level was lower in the cells expressing NS3-NS5B with a mutation in the NS3 ATP-binding domain. In vitro assays with a synthetic peptide and purified wild-type NS3 followed by dot blotting and mass spectrometry found weak NS5A phosphorylation at serines 222 and 225 that was sensitive to an inhibitor of casein kinase Iα but not helicase. When casein kinase Iα was included in the assay, much stronger phosphorylation was observed at serines 225, 232, and 235. We concluded that NS5A sequential phosphorylation requires the ATP-binding domain of the NS3 helicase and that casein kinase Iα is a potent NS5A kinase. IMPORTANCE For more than 20 years, NS3 was known to participate in NS5A sequential phosphorylation. In the present study, we show for the first time that the ATP-binding domain of NS3 is involved in NS5A phosphorylation. In vitro assays showed that casein kinase Iα is a very potent kinase responsible for NS5A phosphorylation at serines 225, 232, and 235. Our data suggest that ATP binding by NS3 probably results in conformational changes that recruit casein kinase Iα to phosphorylate NS5A, initially at S225 and subsequently at S232 and S235. Our discovery reveals intricate requirements of the structural integrity of NS3 for NS5A hyperphosphorylation and HCV replication.

Published
2022

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