The toxicity of selenium (Se) as an antioxidant supplement in the treatment of arthritis is debatable. In this study, Dextrin stabilized Se nanoparticles (SeNP) of size 64 nm ± 0.158 were used to explore its effects as a potent antioxidant with reduced toxicity in both in vitro and in vivo. In vitro toxicity of SeNP was determined using cytotoxicity assay. In vitro interactions of SeNP with DNA and protein was established. Subacute toxicity of SeNP was studied. Wistar rats with complete freunds adjuvant induced arthritis were used. Various concentrations of SeNP per kg body weight were fed orally daily upto to 21 days. Arthritic profile based on paw swelling, histopathological changes in joints, blood indices, and antioxidant enzymes level in organs such as liver, kidney, and spleen were investigated. Dextrin-SeNP when interacted with NIH-3T3 cells showed 15% cytotoxicity at 100 µg/mL whereas, bulk Se showed 95% at the same concentration. SeNP at 250 µg/mL showed protective effect on DNA. Interaction of SeNP with BSA showed increase in quenching of BSA fluorescence. SeNP did not show any subacute toxicity at concentration as high as 5 mg/kg b.w. in Wistar rats. SeNP at a concentration of 250 µg/kg b.w. acted as potent anti-inflammatory agent and significantly reduced (p < 0.05) arthritis induced parameters. The enzymatic antioxidant levels in liver, kidney, and spleen were restored significantly (p < 0.05) at 500 µg/kg b.w. while CRP was regained to normal at concentration of 100 µg/kg b.w. concluding SeNP at 500 µg/kg b.w. can be a potential antiarthritic drug supplement. © 2015 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 104B: 993-1003, 2016.
Allicin, an extremely active constituent of freshly crushed garlic, is produced upon reaction of substrate alliin with the enzyme alliinase (EC 4.4.1.4). Allicin has been shown to be toxic to several mammalian cells in vitro in a dose-dependent manner. In the present study this cytotoxicity was taken to advantage to develop a novel approach to cancer treatment, based on site directed generation of allicin. Alliinase was chemically conjugated to a monoclonal antibody (mAb) which was directed against a specific pancreatic cancer marker, CA19-9. After the CA19-9 mAb-alliinase conjugate was bound to targeted pancreatic cancer cells (MIA PaCa-2 cells), on addition of alliin, the cancer cell-localized alliinase produced allicin, which effectively induced apoptosis in MIA PaCa-2 cells. Specificity of anticancer activity of in situ generated allicin was demonstrated using a novel in vitro system-integrated discrete multiple organ co-culture technique. Further, allicin-induced caspase-3 expression, DNA fragmentation, cell cycle arrest, p21(Waf1/Cip1) cyclin-dependent kinase inhibitor expression, ROS generation, GSH depletion, and led to various epigenetic modifications which resulted in stimulation of apoptosis. This approach offers a new therapeutic strategy, wherein alliin and alliinase-bound antibody work together to produce allicin at targeted locations which would reverse gene silencing and suppress cancer cell growth, suggesting that combination of these targeted agents may improve pancreatic cancer therapy.
This article is about spirulina and how it can be used as a nutrient supplement, a therapeutic agent, trace metal supplement, antioxidant, pigments, enviroment protector and a source of enzymes.
Spirulina platensis :have been studied for several biological activities. In the current study C-phycocyanin containing protein extract (C-PC extract) of Spirulina platensis have been studied for its effect on human matrix metalloproteinases (MMP-1, MMP-2 and MMP-9) and tissue inhibitors of MMPs (TIMP-1 and TIMP-2). In the present study, breast cancer cell line (MDA-MB 231) and hepatocellular cancer cell line (HepG2) were examined for inhibition of MMPs at different levels of expression after C-PC extract treatment. Herein, we have demonstrated that C-PC extract significantly reduced activity of MMP-2 by 55.13% and MMP-9 by 57.9% in HepG2 cells at 15 μg concentration. Additionally, the treatment has reduced mRNA expression of MMP-2 and MMP-9 at 20 μg concentration by 1.65-folds and 1.66-folds respectively. The C-PC extract treatment have also downregulated a mRNA expression of TIMP-2 by 1.12 folds at 20 μg concentration in HepG2 cells. Together, these results indicate that C-PC, extract successfully inhibited MMP-2 and -9 at different levels of expression and TIMP-2 at a mRNA expression level; however, extract did not have any effect on MMP-1 expressed in MDA-MB231 and TIMP-1 expressed in HepG2 cells as well as the exact mechanism of inhibition of MMP-2, MMP-9 and TIMP-2 remained unclear.
A new thermostable and solvent-tolerant lipase was isolated from newly isolated Staphylococcus warneri from oil-contaminated soil. Optimization of the fermentation media for production of thermostable and organic solvent-tolerant lipase was carried out using two statistical methods, i.e., Plackett-Burman design (PBD) and central composite design (CCD) were used for the optimization of the media components. PBD was used to efficiently select important medium components affecting the lipase production. Out of 15 medium components screened, four components, i.e., olive oil, peptone, maltose, and K2HPO4 were found to contribute positively to lipase production. CCD and response surface methodology (RSM) were used to determine the optimum levels of the selected components using Design-Expert 8.0 software. Production medium with olive oil (1.45 %), peptone (0.28 %), maltose (0.054 %), and K2HPO4 (0.091 %) was optimized with a maximum lipase production of 10.43 IU/ml/min. Similarly, production conditions for the lipase production were optimized by using CCD and RSM. Optimized conditions were found to have an incubation temperature of 55 °C, medium pH of 8.0, agitation of 120 rpm, and inoculum volume of 2 %. RSM revealed the maximum lipase production of 17.21 IU/ml using these optimized production conditions. Crude lipase showed enhanced activity in organic solvents such as diethyl ether, hexane, and cyclohexane.
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