Measurement of OH, O, and NO densities and their correlations with mouse melanoma cell death rate treated by a nanosecond pulsed streamer discharge

2015 ◽  
Vol 48 (42) ◽  
pp. 424006 ◽  
Author(s):  
Ippei Yagi ◽  
Yuki Shirakawa ◽  
Kenta Hirakata ◽  
Taketoshi Akiyama ◽  
Seiya Yonemori ◽  
...  
2004 ◽  
Vol 1030 (1) ◽  
pp. 384-392 ◽  
Author(s):  
LELA B. KORIĆANAC ◽  
DANIJELA V. TODOROVIĆ ◽  
NATAŠA M. POPOVIĆ ◽  
MIROSLAV A. DEMAJO ◽  
SABERA D. RUŽDIJIĆ ◽  
...  

1995 ◽  
Vol 5 ◽  
pp. 16
Author(s):  
B. Loir ◽  
M-C. Carrière ◽  
G. Ghanem ◽  
J. Drouin ◽  
L. Roselli-Rehfuss

2016 ◽  
Vol 81 (6) ◽  
pp. 697-705 ◽  
Author(s):  
Xuepeng Yang ◽  
Yan Ji ◽  
Fangfang Wang ◽  
Jia Xu ◽  
Xiangzhen Liu ◽  
...  

Vibrio fischeri bioluminescence inhibition has been widely used to test acute toxicities of metals and organics contaminants. However, the differences of metals and organics acute toxicities to V. fischeri have not been compared. Here, four heavy metals (Zn2+, Cu2+, Cd2+, Cr6+) and five organics (phenol, benzoic acid, p-hydroxy benzoic acid, nitro-benzene and benzene) acute toxicities to V. fischeri were investigated. Heavy metals toxicities to V. fischeri were increased along with the reaction time, while the organics toxicities kept the same level in different reaction times. In order to explain the difference, the relative cell death rate of V. fischeri was detected. In metals toxicities tests, the bioluminescence inhibition rate of V. fischeri was found to be significantly higher than the relative cell death rate (P<0.05), while for the organics toxicities tests, the cell death rate was similar to the bioluminescence inhibition rate. These results indicated that organics acute toxicities to V. fischeri could reflect the death of cell, but metals acute toxicities to V. fischeri may not lead to the death of cell, just represent the bioluminescence inhibition.


2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Tae Hyuk Kim ◽  
Mi Ja Chung ◽  
Dae Jung Kim ◽  
Jin Kyoun You ◽  
Dong Joo Seo ◽  
...  

2020 ◽  
Vol 25 (1) ◽  
pp. 83-91
Author(s):  
Maryam Malek ◽  
◽  
Maedeh Ghasemi ◽  
Golnaz Vaseghi ◽  
Ahmad Ghasemi ◽  
...  

Introduction: Tamoxifen has been used in the treatment of metastatic malignant melanoma more common with other agents in the combined therapy. Up-regulated activity of the mevalonate pathway has been shown in a range of different cancers. Atorvastatin is the most commonly used statin approved for cholesterol reduction by inhibiting the mevalonate pathway and has been shown to inhibit tumor growth. In the present study, we used atorvastatin and tamoxifen combination therapy on B16f10 mouse melanoma cell lines to study whether atorvastatin could increase the sensitivity of melanoma cells to the chemotherapeutic agent such as tamoxifen. Methods: The cell line was treated with different concentrations of tamoxifen and/or atorvastatin for 24 and 48h and the effects of treatment on p53 and RhoA were investigated using quantitative RT-PCR. Results: The combination of atorvastatin and tamoxifen resulted in a potentiation antitumor effect via up-regulation of p53 and down-regulation of RhoA expression against melanoma tumors in vitro. Furthermore, we demonstrated the combination of atorvastatin with tamoxifen could reduce tamoxifen dose to minimize possible detrimental side effects in melanoma. Conclusion: Our results suggested that atorvastatin as a combined therapy with tamoxifen may provide a new approach for improving the efficacy and treating against melanoma cancer but needs further exploration in clinical trials.


2012 ◽  
Vol 38 (3) ◽  
pp. 419-425 ◽  
Author(s):  
Guilherme Fartes ◽  
Fábio Lorenzetti ◽  
Larissa Beloti Salvador ◽  
Valdemar Ortiz ◽  
Miriam Dambros

2007 ◽  
Vol 13 (1-2) ◽  
pp. 14-21 ◽  
Author(s):  
Zhi Yao ◽  
Xu-chun Che ◽  
Rong Lu ◽  
Min-na Zheng ◽  
Zhi-feng Zhu ◽  
...  

1992 ◽  
Vol 117 (6) ◽  
pp. 1331-1341 ◽  
Author(s):  
SL Drake ◽  
DJ Klein ◽  
DJ Mickelson ◽  
TR Oegema ◽  
LT Furcht ◽  
...  

Cell surface heparan sulfate proteoglycan (HSPG) from metastatic mouse melanoma cells initiates cell adhesion to the synthetic peptide FN-C/H II, a heparin-binding peptide from the 33-kD A chain-derived fragment of fibronectin. Mouse melanoma cell adhesion to FN-C/H II was sensitive to soluble heparin and pretreatment of mouse melanoma cells with heparitinase. In contrast, cell adhesion to the fibronectin synthetic peptide CS1 is mediated through an alpha 4 beta 1 integrin and was resistant to heparin or heparitinase treatment. Mouse melanoma cell HSPG was metabolically labeled with [35S]sulfate and extracted with detergent. After HPLC-DEAE purification, 35S-HSPG eluted from a dissociative CL-4B column with a Kav approximately 0.45, while 35S-heparan sulfate (HS) chains eluted with a Kav approximately 0.62. The HSPG contained a major 63-kD core protein after heparitinase digestion. Polyclonal antibodies generated against HSPG purified from mouse melanoma cells grown in vivo also identified a 63-kD core protein. This HSPG is an integral plasma membrane component by virtue of its binding to Octyl Sepharose affinity columns and that anti-HSPG antibody staining exhibited a cell surface localization. The HSPG is anchored to the cell surface through phosphatidylinositol (PI) linkages, as evidenced in part by the ability of PI-specific phospholipase C to eliminate binding of the detergent-extracted HSPG to Octyl Sepharose. Furthermore, the mouse melanoma HSPG core protein could be metabolically labeled with 3H-ethanolamine. The involvement of mouse melanoma cell surface HSPG in cell adhesion to fibronectin was also demonstrated by the ability of anti-HSPG antibodies and anti-HSPG IgG Fab monomers to inhibit mouse melanoma cell adhesion to FN-C/H II. 35S-HSPG and 35S-HS bind to FN-C/H II affinity columns and require 0.25 M NaCl for elution. However, heparitinase-treated 125I-labeled HSPG failed to bind FN-C/H II, suggesting that HS, and not HSPG core protein, binds FN-C/H II. These data support the hypothesis that a phosphatidylinositol-anchored HSPG on mouse melanoma cells (MPIHP-63) initiates recognition to FN-C/H II, and implicate PI-associated signal transduction pathways in mediating melanoma cell adhesion to this defined ligand.


BMC Cancer ◽  
2006 ◽  
Vol 6 (1) ◽  
Author(s):  
Osamu Hashimoto ◽  
Masako Shinkawa ◽  
Takuji Torimura ◽  
Toru Nakamura ◽  
Karuppaiyah Selvendiran ◽  
...  

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