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1.
Environmental Health Engineering and Management Journal. 2015; 2 (4): 193-197
in English | IMEMR | ID: emr-179213

ABSTRACT

Background: Co[II] constitutes a part of vitamin B12, hence, it is necessary for human health. However, at concentrations higher than the permissible limits, humans and animals suffer adverse chronic effects. It is necessary to reduce the concentration to a permissible level. In the present study, pre-purification and thermal modification of chicken's feather increased their porosity and they were used to adsorb Co[II] ions from aqueous solutions


Methods: Chicken feather was procured from a slaughter house, washed with detergent and dried at laboratory temperature. To increase the porosity and remove the organic pollutants attached to the feather, feathers were heated in the oven for 1 hour at 165 degree C. Some batch experiments were conducted to optimize the parameters affecting the adsorption process, such as solution pH, initial concentration of Co[II] and contact time, at a constant agitating speed and temperature


Results: The pH[zpc] of chicken's feather granules obtained was 5.3. The results showed that a time of 60 minutes, pH value of 9 and initial concentration of 10 mg/l were the optimum conditions for Co[II] removal by the adsorption process. Increasing the initial concentration of Co[II] from 10 to 50 decreased the removal efficiency from 52% to 26%. The pseudo-first order kinetic model provided the best correlation [R[2] = 0.998] for adsorption of Co[II] on chicken's feather granules


Conclusion: The increase in electrostatic repulsion forces between positive charges of Co[II] ions decreased the removal efficiency at higher concentrations of Co[II] ions. The maximum efficiency of Co[II] adsorption was obtained at pH= 9, which is higher than the pH[zpc] of the adsorbent

2.
AJMB-Avicenna Journal of Medical Biotechnology. 2014; 6 (3): 169-177
in English | IMEMR | ID: emr-147356

ABSTRACT

Our preliminary data on the protein expression of SORT1 in ovarian carcinoma tissues showed that sortilin was overexpressed in ovarian carcinoma patients and cell lines, while non-malignant ovaries expressed comparably lower amount of this protein. In spite of diverse ligands and also different putative functions of sortilin [NTR3], the function of overexpressed sortilin in ovarian carcinoma cells is an intriguing subject of inquiry. The aim of this study was, therefore, to investigate the functional role of sortilin in survival of ovarian carcinoma cell line. Expression of sortilin was knocked down using RNAi technology in the ovarian carcinoma cell line, Caov-4. Silencing of SORT1 expression was assessed using real-time qPCR and Western blot analyses. Apoptosis induction was evaluated using flow cytometry by considering annexin-V FITC binding. [3H]-thymidine incorporation assay was also used to evaluate cell proliferation capacity. Real-time qPCR and Western blot analyses showed that expression of sortilin was reduced by nearly 70-80% in the siRNA transfected cells. Knocking down of sortilin expression resulted in increased apoptosis [27.5 +/- 0.48%] in siRNA-treated ovarian carcinoma cell line. Sortilin silencing led to significant inhibition of proliferation [40.1%] in siRNA-transfected Caov-4 cells as compared to mock control-transfected counterpart [p<0.05]. As it was suspected from overexpression of sortilin in ovarian tumor cells, a cell survival role for sortilin can be deduced from these results. In conclusion, the potency of apoptosis induction via silencing of sortilin expression in tumor cells may introduce sortilin as a potential candidate for developing a novel targeted therapy in patients with ovarian carcinoma

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