Induction and distribution of damage in CHO-K1 and the X-ray-sensitive hamster cell line xrs5, measured by the cytochalasin-B-cytokinesis block micronucleus assay

1997 ◽  
Vol 385 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Peter J Johnston ◽  
Elizabeth Stoppard ◽  
Peter E Bryant
Keyword(s):  
Cell Line ◽  
Cytochalasin B ◽  
Micronucleus Assay ◽  
X Ray

scholarly journals Testing Strategies of the In Vitro Micronucleus Assay for the Genotoxicity Assessment of Nanomaterials in BEAS-2B Cells

Nanomaterials ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1929
Author(s):  
Tereza Cervena ◽  
Andrea Rossnerova ◽  
Tana Zavodna ◽  
Jitka Sikorova ◽  
Kristyna Vrbova ◽  
...  
Keyword(s):  
Cytochalasin B ◽  
Culture Media ◽  
Methodological Approach ◽  
Micronucleus Assay ◽  
Toxicity Testing ◽  
In Vitro Toxicity ◽  
Testing Strategies ◽  
Transmission Electron ◽  
The Impact

The evaluation of the frequency of micronuclei (MN) is a broadly utilised approach in in vitro toxicity testing. Nevertheless, the specific properties of nanomaterials (NMs) give rise to concerns regarding the optimal methodological variants of the MN assay. In bronchial epithelial cells (BEAS-2B), we tested the genotoxicity of five types of NMs (TiO2: NM101, NM103; SiO2: NM200; Ag: NM300K, NM302) using four variants of MN protocols, differing in the time of exposure and the application of cytochalasin-B combined with the simultaneous and delayed co-treatment with NMs. Using transmission electron microscopy, we evaluated the impact of cytochalasin-B on the transport of NMs into the cells. To assess the behaviour of NMs in a culture media for individual testing conditions, we used dynamic light scattering measurement. The presence of NMs in the cells, their intracellular aggregation and dispersion properties were comparable when tests with or without cytochalasin-B were performed. The genotoxic potential of various TiO2 and Ag particles differed (NM101 < NM103 and NM302 < NM300K, respectively). The application of cytochalasin-B tended to increase the percentage of aberrant cells. In conclusion, the comparison of the testing strategies revealed that the level of DNA damage induced by NMs is affected by the selected methodological approach. This fact should be considered in the interpretation of the results of genotoxicity tests.

The comparison of Zn(II) arginine dithiocarbamate cytotoxicity in T47D breast cancer and fibroblast cells

2021 ◽  
pp. 1-7
Author(s):  
Prihantono Prihantono ◽  
Rizal Irfandi ◽  
Indah Raya
Keyword(s):  
Breast Cancer ◽  
Cell Line ◽  
Breast Cancer Cell Line ◽  
Cancer Cell Line ◽  
Fibroblast Cell ◽  
Fibroblast Cells ◽  
X Ray ◽  
Dithiocarbamate Complex ◽  
T47d Breast Cancer Cell ◽  
Fibroblast Cell Lines

BACKGROUND: With essential metals being studied and developed as anticancer agents, this study aims to explore the anticancer activity of Zn(II) arginine dithiocarbamate in the T47D and fibroblast cell lines. METHOD: The Zn(II) arginine dithiocarbamate complex was prepared by the in situ method and characterized using infra-red spectroscopy, melting point, X-ray fluorescence, and X-ray diffraction instruments. The complex compound was tested for its cytotoxicity to the T47D breast cancer and fibroblast cell lines. RESULTS: The cytotoxicity of the Zn(II) arginine dithiocarbamate complex to the T47D breast cancer cell line obtained IC50 = 3.16 μg/mL, while cisplatin obtained IC50 = 28.18 μg/mL. The cytotoxicity of the Zn(II) arginine dithiocarbamate complex to fibroblast cells obtained IC50 = 8709.63 μg/mL. CONCLUSION: The Zn(II) arginine dithiocarbamate complex has increased active cytotoxicity compared to cisplatin in inducing morphological changes in the T47D breast cancer cell line and is relatively non-toxic to fibroblast cells.

Anticancer effect of X-Ray triggered methotrexate conjugated albumin coated bismuth sulfide nanoparticles on SW480 colon cancer cell line

2020 ◽  
Vol 582 ◽  
pp. 119320
Author(s):  
Mohammad Hasan Faghfoori ◽  
Hamed Nosrati ◽  
Hamed Rezaeejam ◽  
Jalil Charmi ◽  
Saeed Kaboli ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cell Line ◽  
Cancer Cell ◽  
Cancer Cell Line ◽  
Colon Cancer Cell Line ◽  
Colon Cancer Cell ◽  
Bismuth Sulfide ◽  
Anticancer Effect ◽  
X Ray

Potent Anticancer Activities of Beauvericin against KB cells In Vitro by Inhibiting the Expression of ACAT1 and Exploring Binding Affinity

2021 ◽  
Vol 21 ◽  
Author(s):  
Haiming Zhou ◽  
Jing Zhang ◽  
Xiaoqing Chen ◽  
Shili Guo ◽  
Huimei Lin ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Cell Line ◽  
Binding Affinity ◽  
X Ray Diffraction ◽  
Kb Cells ◽  
Anticancer Activities ◽  
Monoclinic Crystal ◽  
X Ray ◽  
Multiple Tumor

Background and Objective: Beauvericin (BEA), a cyclic hexadepsipeptide mycotoxin, is a potent inhibitor of the acyl-CoA: cholesterol acyltransferase enzyme 1 (ACAT1) which involved in multiple tumor-correlated pathways. However, the binding mechanisms between BEA and ACAT1 were not elucidated. Methods: BEA was purified from a mangrove entophytic Fusarium sp. KL11. Single-crystal X-ray diffraction was used to determine the structure of BEA. Wound healing assays of BEA against KB cell line and MDA-MB-231 cell line were evaluated. Inhibitory potency of BEA against ACAT1 was determined by ELISA assays. Molecular docking was carried out to illuminate the bonding mechanism between BEA and ACAT1. Results: The structure of BEA was confirmed by X-ray diffraction, indicating a monoclinic crystal system with P21 space group (α = 90°, β = 92.2216(9)o, γ= 90o). BEA displayed migration-inhibitory activities against KB cells and MDA-MB-231 cells in vitro. ELISA assays revealed the protein expression level of ACAT1 in KB cells was significantly decreased after BEA treatment (P ＜0.05). Molecular docking demonstrated that BEA formed hydrogen bond with His425 and pi-pi staking with Tyr429 in ACAT1. Conclusions: BEA sufficiently inhibited the proliferation and migration of KB cells and MDA-MB-231 cells by downregulating ACAT1 expression. In addition, BEA potentially possessed a strong binding affinity with ACAT1. BEA may serve as a potential lead compound for the development of a new ACAT1-targeted anticancer drug.

scholarly journals Homogeneously N-glycosylated proteins derived from the GlycoDelete HEK293 cell line enable diffraction-quality crystallogenesis

2020 ◽  
Vol 76 (12) ◽  
pp. 1244-1255
Author(s):  
Sandra Kozak ◽  
Yehudi Bloch ◽  
Steven De Munck ◽  
Aleksandra Mikula ◽  
Isabel Bento ◽  
...  
Keyword(s):  
Cell Line ◽  
Protein Interactions ◽  
Successful Implementation ◽  
Structural Studies ◽  
Protein Fragments ◽  
X Ray ◽  
X Ray Crystallography ◽  
Cryo Electron Microscopy ◽  
Acid Protein ◽  
Stimulating Factor

Structural studies of glycoproteins and their complexes provide critical insights into their roles in normal physiology and disease. Most glycoproteins contain N-linked glycosylation, a key post-translation modification that critically affects protein folding and stability and the binding kinetics underlying protein interactions. However, N-linked glycosylation is often an impediment to yielding homogeneous protein preparations for structure determination by X-ray crystallography or other methods. In particular, obtaining diffraction-quality crystals of such proteins and their complexes often requires modification of both the type of glycosylation patterns and their extent. Here, we demonstrate the benefits of producing target glycoproteins in the GlycoDelete human embryonic kidney 293 cell line that has been engineered to produce N-glycans as short glycan stumps comprising N-acetylglucosamine, galactose and sialic acid. Protein fragments of human Down syndrome cell-adhesion molecule and colony-stimulating factor 1 receptor were obtained from the GlycoDelete cell line for crystallization. The ensuing reduction in the extent and complexity of N-glycosylation in both protein molecules compared with alternative glycoengineering approaches enabled their productive deployment in structural studies by X-ray crystallography. Furthermore, a third successful implementation of the GlycoDelete technology focusing on murine IL-12B is shown to lead to N-glycosylation featuring an immature glycan in diffraction-quality crystals. It is proposed that the GlycoDelete cell line could serve as a valuable go-to option for the production of homogeneous glycoproteins and their complexes for structural studies by X-ray crystallography and cryo-electron microscopy.

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