mouse leukemia
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2020 ◽  
Vol 36 (1) ◽  
pp. 77-85
Author(s):  
Hung‐Sheng Shang ◽  
Chiung‐Ju Chen ◽  
Yung‐Luen Shih ◽  
Shu‐Fen Peng ◽  
Yung‐Liang Chen ◽  
...  

2020 ◽  
Vol 35 (9) ◽  
pp. 911-921
Author(s):  
Zheng‐Yu Cheng ◽  
Fu‐Shin Chueh ◽  
Shu‐Fen Peng ◽  
Chia‐Hsin Lin ◽  
Chao‐Lin Kuo ◽  
...  

2019 ◽  
Vol 2 (2) ◽  
pp. 114 ◽  
Author(s):  
Purwantiningsih Sugita ◽  
Dina Anggraini ◽  
Gustini Syahbirin ◽  
Dyah Utami Cahayaning Rahayu ◽  
Auliya Ilmiawati

From the fruit of Kigelia africana three fractions of secondary metabolites were isolated. Fraction 1 (CD-1) was characterized by using UV-Vis, FTIR, 1D and 2D NMR and MS, meanwhile fraction 2 (CD-2) and 3 (B-1) were characterized by LCMS and compared with literature. All these fractions were screened for anticancer activity by using (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) method to calculate IC50 toward Michigan Cancer Foundation-7 MCF-7 breast cancer and menogaril-resistant mouse leukemia P388 cells. Based on spectroscopic data, CD-1 fraction was identified as methyl ferulate (1). On the other hand, the B-1 and CD-2 fraction did not pure, yet. Based on LCMS data that analyzed by chemspider and masslink software, CD-2 fraction was estimated as compound mixture with dominant compounds like viscumside (2), specioside (3), caffeic acid glucoside (4), ferulic acid (5), meanwhile B-1 fraction was estimated as compound mixture with dominant warfarin alcohol (6), p-Coumaroyl glucose (7) and β - Sitosterol (8) compounds. Nevertheless, all isolated fractions did not show anticancer activity towards both the cancer cells since it had different constituent compared with previous results.


2019 ◽  
Vol 35 (4) ◽  
pp. 457-467
Author(s):  
Nien‐Chieh Liao ◽  
Yung‐Luen Shih ◽  
Ming‐Tak Ho ◽  
Tai‐Jung Lu ◽  
Ching‐Hsiao Lee ◽  
...  

2019 ◽  
Vol 47 (03) ◽  
pp. 635-656 ◽  
Author(s):  
Nien-Chieh Liao ◽  
Yung-Luen Shih ◽  
Jiann-Shang Chou ◽  
Kuo-Wei Chen ◽  
Yung-Liang Chen ◽  
...  

Cardamonin, the chalcone class, is one of the natural components from the spicy herbaceous plant (Alpinia conchigera Griff) and has anticancer activities in many human cancer cell lines. There is, however, no information to show that cardamonin induces cell apoptosis and alters apoptosis associated gene expressions in mouse leukemia cells. Thus, we investigated the effects of cardamonin on the apoptotic cell death and associated gene expression in mouse leukemia WEHI-3 cells in vitro. Results indicated that cardamonin decreased total viable cell number via induced cell morphological changes and apoptotic cell death in WEHI-3 cells that were assay by contrast-phase microscopy and flow cytometry examinations, respectively. The flow cytometry assay indicated that cardamonin increased reactive oxygen species (ROS) and Ca[Formula: see text] production, decreased the levels of mitochondrial membrane potential ([Formula: see text] and increased caspase-3, -8 and -9 activities in WEHI-3 cells. Western blotting was performed to analyze expression of relevant pro- and anti-apoptotic proteins and results showed that cardamonin decreased anti-apoptotic protein of Bcl-2 but increased pro-apoptotic protein of Bax in WEHI-3 cells. Furthermore, cardamonin increased cytochrome c, AIF and Endo G release, increased GRP78, caspase-12 that were associated with ER stress and increased Fas, Fas-Ligand and FADD expression. Furthermore, cardamonin increased the gene expressions of DAP (death-associated protein), TMBIM4 transmembrane (BAX inhibitor motif containing 4), ATG5 (autophagy related 5) but decreased the gene expression of DDIT3 (DNA-damage inducible transcript 3), DDIT4 (DNA-damage-inducible transcript 4), BAG6 (BCL2-associated athanogene 6), BCL2L13 [BCL2-like 13 (apoptosis facilitator)] and BRAT1 (BRCA1-associated ATM activator 1) that are associated with apoptosis pathways. Based on those findings, we may suggest cardamonin induced apoptotic cell death through Fas and Fas-Ligand-, caspase- and mitochondria-dependently pathways and also affects the apoptotic gene expression in WEHI-3 cells in vitro.


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