Extremely low-frequency electromagnetic field induces a change in proliferative capacity and redox homeostasis of human lung fibroblast cell line MRC-5

2020 ◽  
Vol 27 (31) ◽  
pp. 39466-39473
Author(s):  
Maida H. Lekovic ◽  
Nerkesa E. Drekovic ◽  
Nihat Dz. Granica ◽  
Elvis H. Mahmutovic ◽  
Natasa Z. Djordjevic
2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Sok-Lai Hong ◽  
Guan-Serm Lee ◽  
Syarifah Nur Syed Abdul Rahman ◽  
Omer Abdalla Ahmed Hamdi ◽  
Khalijah Awang ◽  
...  

Curcuma purpurascensBl., belonging to the Zingiberaceae family, is known astemu tisin Yogyakarta, Indonesia. In this study, the hydrodistilled dried ground rhizome oil was investigated for its chemical content and antiproliferative activity against selected human carcinoma cell lines (MCF7, Ca Ski, A549, HT29, and HCT116) and a normal human lung fibroblast cell line (MRC5). Results from GC-MS and GC-FID analysis of the rhizome oil oftemu tisshowed turmerone as the major component, followed by germacrone,ar-turmerone, germacrene-B, and curlone. The rhizome oil oftemu tisexhibited strong cytotoxicity against HT29 cells (IC50value of 4.9 ± 0.4 μg/mL), weak cytotoxicity against A549, Ca Ski, and HCT116 cells (with IC50values of 46.3 ± 0.7, 32.5 ± 1.1, and 35.0 ± 0.3 μg/mL, resp.), and no inhibitory effect against MCF7 cells. It exhibited mild cytotoxicity against a noncancerous human lung fibroblast cell line (MRC5), with an IC50value of 25.2 ± 2.7 μg/mL. This is the first report on the chemical composition of this rhizome’s oil and its selective antiproliferative effect on HT29. The obtained data provided a basis for further investigation of the mode of cell death.


2002 ◽  
Vol 128 (Suppl. 1) ◽  
pp. 12-17 ◽  
Author(s):  
Etsuro Sato ◽  
Masayuki Haniuda ◽  
Hiroki Numanami ◽  
Toshiki Ushiyama ◽  
Akihiro Tsukadaira ◽  
...  

2000 ◽  
Vol 106 (1) ◽  
pp. 117-123 ◽  
Author(s):  
Etsuro Sato ◽  
Dan K. Nelson ◽  
Sekiya Koyama ◽  
Jeffrey C. Hoyt ◽  
Richard A. Robbins

1990 ◽  
Vol 126 (3) ◽  
pp. 497-506 ◽  
Author(s):  
B. Forbes ◽  
F. J. Ballard ◽  
J. C. Wallace

ABSTRACT We have identified a novel insulin-like growth factor (IGF)-binding protein secreted into the culture medium of a human lung fibroblast cell line (He[39]L). This binding protein was purified by S-Sepharose cation exchange chromatography, IGF affinity chromatography and reverse-phase high-performance liquid chromatography. Analysis of the He[39]L-binding protein on silver-stained polyacrylamide gels and by ligand blotting showed that it had a molecular weight of 32 kDa under non-reducing conditions. In charcoal competition binding assays, IGF-II competed at lower concentrations than IGF-I for binding to the He[39]L-binding protein and the more potent form of IGF-I (des-(1–3)-IGF-I) was not bound. This is a similar IGF binding pattern to that of the bovine IGF-binding protein-2 (bIGFBP-2). However, immunoblotting with an antibody to bIGFBP-2 demonstrated that the He[39]L-binding protein is not immunochemically related to bIGFBP-2. It is a glycosylated protein, having N-acetyl-glucosaminyl sugars detected by wheatgerm agglutinin affinity chromatography. Of the first 15 N-terminal amino acids of the He[39]L-binding protein, 13 are identical to the 15 amino acid sequence of a recently sequenced cerebrospinal fluid-binding protein. However, the total He[39]L-binding protein sequence (25 amino acids) showed no homology to other previously sequenced binding proteins (IGFBP-1, IGFBP-2 and IGFBP-3). We conclude that the He[39]L-binding protein is a novel binding protein. Journal of Endocrinology (1990) 126, 497–506


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