Spectrophotometric determination of rosuvastatin in pharmaceutical formulations using quinalizarin

ABSTRACT This work presents the development of a methodology based on the formation of a charge transfer complex between quinalizarin and rosuvastatin, allowing for the spectrophotometric determination of rosuvastatin at 579 nm. The factors involved in the sensitivity of the technique were studied (nature and proportion of the solvent, reaction time, pH of aqueous phase and quinalizarin concentration). The proposed spectrophotometric procedures were validated with respect to linearity, ranges, precision, accuracy, detection and quantification limits. Calibration curves of the formed color products showed good linear relationships over the concentration range of 6-15 mg L-1. The proposed method has been successfully applied, which can be confirmed by interference test (comparison between the standard curves and addition of analyte), method precision (RSD 2.3% to 6 mg L-1), and by accuracy (statistically equivalent results between the proposed method and a chromatographic method of reference).

Effect of a protein kinase CK2 inhibitor on intracellular levels of reactive oxygen species and DNA double-stand break in H460 cells / 中华放射肿瘤学杂志

Objective To evaluate the effect of a protein kinase CK2 inhibitor on intracellular levels of reactive oxygen species and DNA double?stand break in human non?small cell lung cancer H460 cells. Methods H460 cells were exposed to 0, 12?5, 25.0, and 50.0μmol/L quinalizarin, a specific inhibitor of protein kinase CK2, for 24 hours. The changes in protein and mRNA levels of CK2 subunits were measured. Flow cytometry was used to measure changes in the intracellular levels of reactive oxygen species in H460 cells after 4 or 24 hours of quinalizarin treatment. Immunofluorescence assays were performed to determine the effect of the CK2 inhibitor onγ?H2 AX expression and the average fluorescent number ofγ?H2 AX foci in H460 cells. Comparison was made by analysis of variance and t test. Results There were no significant differences in protein or mRNA levels of CK2 subunits in H460 cells after quinalizarin treatment ( CK2α,0μmol vs. 12?5 μmol/L, P=0?966;0 μmol/L vs. 25 μmol/L, P=0?355;0 μmol/L vs. 50 μmol/L, P=0?864, CK2α’ , 0 μmol/L vs. 12?5μmol/L,P=0?409;0μmol/L vs. 25μmol/L,P=0?833;0μmol/L vs. 50 μmol/L, P=0?0. 746, CK2β, 0 μmol/L vs. 12?5 μmol/L, P=0?532;0 μmol/L vs. 25 μmol/L, P=0?830;0 μmol/L vs. 50 μmol/L, P= 0?061 ) . The intracellular levels of reactive oxygen species were substantially elevated in H460 cells with the increase in quinalizarin concentration and treatment time. Different concentrations of quinalizarin resulted in dose?and time?dependent increases in the numbers of γ?H2 AX foci after 4 and 24 hours of treatment ( treated by Quianlizarin for 4 or 24 h, 0 μmol/L vs. 12?5μmol/L,12?5 μmol/L vs. 25 μmol/L, 25 μmol/L vs. 50 μmol/L, all P=0?000, concentration is 12?5μmol/L,25 μmol/L or 50 μmol/L, 4 h vs. 24 h, all all P=0?000 ) . Conclusions Quinalizarin can increase the intracellular levels of reactive oxygen species and DNA double?stand break in H460 cells by inhibition of protein kinase CK2 activity. This study provides a theoretical basis for using quinalizarin as a potential radiosensitizer for lung cancer.

Quinalizarin, a specific CK2 inhibitor, reduces cell viability and suppresses migration and accelerates apoptosis in different human lung cancer cell lines.

BACKGROUND: Protein kinase CK2 is widely expressed in eukaryotic cells, and plays an important role in cell proliferation, migration, apoptosis, etc. The aim of the current study is to explore how Quinalizarin, a specific CK2 inhibitor, affects the cell proliferation, migration, and apoptosis of different pathological and genetic types of human lung cancer cell lines. MATERIALS AND METHODS: MTT assays were performed to evaluate the cell viability after being treated by Quinalizarin. Transwell migration assays were used to assess whether Quinalizarin could suppress cell migration. Flow cytometry was employed to test the apoptosis rate of different cells. RESULTS: After being treated by Quinalizarin, the viability of different pathological types of lung cancer cells (H446, H460, A549) were significantly suppressed in a time and dose‑dependent manner. More interestingly, in a serial of human lung adenocarcinoma cell lines with different epidermal growth factor receptor (EGFR) mutation status, Quinalizarin was shown to have a much better ability to reduce the viability of cells with EGFR sensitive mutation than those with resistance mutations. Meanwhile, we also found that the cell migration of different pathological types of lung cancer cells (H446, H460, A549) was significantly decreased by Quinalizarin dose‑dependently. In addition, the apoptosis rates in those cells were proved to be increased after exposed to Quinalizarin. CONCLUSIONS: Quinalizarin, the specific CK2 inhibitor, could reduce cell viability with emphasis on adenocarcinoma cells harboring EGFR sensitive mutation, suppresses migration, and accelerates apoptosis in different human lung cancer cell lines.