Estimation of low-dose radiation-responsive proteins in the absence of genomic instability in normal human fibroblast cells

2017 ◽  
Vol 93 (11) ◽  
pp. 1197-1206 ◽  
Author(s):  
Ji-Hye Yim ◽  
Jung Mi Yun ◽  
Ji Young Kim ◽  
Seon Young Nam ◽  
Cha Soon Kim
2017 ◽  
Vol 58 (3) ◽  
pp. 329-340 ◽  
Author(s):  
Ji-Hye Yim ◽  
Jung Mi Yun ◽  
Ji Young Kim ◽  
In Kyung Lee ◽  
Seon Young Nam ◽  
...  

Abstract Ionizing radiation causes biological damage that leads to severe health effects. However, the effects and subsequent health implications caused by exposure to low-dose radiation are unclear. The objective of this study was to determine phosphoprotein profiles in normal human fibroblast cell lines in response to low-dose and high-dose γ-radiation. We examined the cellular response in MRC-5 cells 0.5 h after exposure to 0.05 or 2 Gy. Using 1318 antibodies by antibody array, we observed ≥1.3-fold increases in a number of identified phosphoproteins in cells subjected to low-dose (0.05 Gy) and high-dose (2 Gy) radiation, suggesting that both radiation levels stimulate distinct signaling pathways. Low-dose radiation induced nucleic acid–binding transcription factor activity, developmental processes, and multicellular organismal processes. By contrast, high-dose radiation stimulated apoptotic processes, cell adhesion and regulation, and cellular organization and biogenesis. We found that phospho-BTK (Tyr550) and phospho-Gab2 (Tyr643) protein levels at 0.5 h after treatment were higher in cells subjected to low-dose radiation than in cells treated with high-dose radiation. We also determined that the phosphorylation of BTK and Gab2 in response to ionizing radiation was regulated in a dose-dependent manner in MRC-5 and NHDF cells. Our study provides new insights into the biological responses to low-dose γ-radiation and identifies potential candidate markers for monitoring exposure to low-dose ionizing radiation.


2004 ◽  
Vol 104 (1-4) ◽  
pp. 211-215 ◽  
Author(s):  
T. Kawata ◽  
H. Ito ◽  
T. Uno ◽  
M. Saito ◽  
S. Yamamoto ◽  
...  

2004 ◽  
Vol 45 (1) ◽  
pp. 105-110 ◽  
Author(s):  
Mitsuaki OJIMA ◽  
Hiroki HAMANO ◽  
Masatoshi SUZUKI ◽  
Keiji SUZUKI ◽  
Seiji KODAMA ◽  
...  

2020 ◽  
Vol 76 (7) ◽  
pp. 663-672
Author(s):  
Charmaine Arderne ◽  
Kyle Fraser Batchelor ◽  
Bhawna Uprety ◽  
Rahul Chandran ◽  
Heidi Abrahamse

The reactivity of the cobalt(III) complexes dichlorido[tris(2-aminoethyl)amine]cobalt(III) chloride, [CoCl2(tren)]Cl, and dichlorido(triethylenetetramine)cobalt(III) chloride, [CoCl2(trien)]Cl, towards different amino acids (L-proline, L-asparagine, L-histidine and L-aspartic acid) was explored in detail. This study presents the crystal structures of three amino acidate cobalt(III) complexes, namely, (L-prolinato-κ2 N,O)[tris(2-aminoethyl)amine-κ4 N,N′,N′′,N′′′]cobalt(III) diiodide monohydrate, [Co(C5H8NO2)(C6H18N4)]I2·H2O, I, (L-asparaginato-κ2 N,O)[tris(2-aminoethyl)amine-κ4 N,N′,N′′,N′′′]cobalt(III) chloride perchlorate, [Co(C4H7N2O3)(C6H18N4)](Cl)(ClO4), II, and (L-prolinato-κ2 N,O)(triethylenetetramine-κ4 N,N′,N′′,N′′′)cobalt(III) chloride perchlorate, [Co(C4H7N2O3)(C6H18N4)](Cl)(ClO4), V. The syntheses of the complexes were followed by characterization using UV–Vis spectroscopy of the reaction mixtures and the initial rates of reaction were obtained by calculating the slopes of absorbance versus time plots. The initial rates suggest a stronger reactivity and hence greater affinity of the cobalt(III) complexes towards basic amino acids. The biocompatibility of the complexes was also assessed by evaluating the cytotoxicity of the complexes on cultured normal human fibroblast cells (WS1) in vitro. The compounds were found to be nontoxic after 24 h of incubation at concentrations up to 25 mM.


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