Although evidences from epidemiological suggested possible involvement of vitamin D in the prevention and treatment of cancers, it is not fully known how vitamin D inhibits cancer cell growth. Recent studies have shown that 1,25-(OH)2D inhibits cancer cell proliferation by binding to vitamin-D receptor (VDR). The vitamin D - VDR complex in turn (a) upregulate cell cycle inhibitors p21 and p27; (b) promote apoptosis mediators caspase-3 and 7, Bad, p53 and PTEN; (c) arrest cells in senescence phase; (d) elevate cell differentiation; and (e) inhibit IGF signaling. Moreover, vitamin D reduces reactive oxygen species (ROS) there by prevents the progression of cancer cells. However, it is currently unknown whether vitamin D induced cancer cell death is mediated by its effect on ROS destroying Nrf2 signaling. In addition, it is also not known whether withdrawal of glucose improves the efficacy of vitamin D as presence of excess glucose promotes ROS in cancer cells. Therefore, first, efficacy of vitamin D for inhibiting the growth of cell lines HCT116, HeLa and MCF-7 was determined. Next, the effect of vitamin D on Nrf2 expression and activity in the presence and absence of glucose was assessed. The data showed that vitamin D inhibited the growth of HCT116, HeLa and MCF-7 cells in a dose dependent manner with more potency toward HCT116. Vitamin D reduced the levels of Nrf2 and NQO1 expression when HCT116 cells were treated in glucose lacking medium. But, despite a significant reduction in cell viability, no change in the Nrf2 expression was observed if the HCT-116 cells were treated with vitamin D dissolved in high glucose (4.5g/L) containing DMEM. Therefore, it is concluded that the cell growth inhibition by vitamin D, observed in the presence of glucose, is not at least mediated by Nrf2 modulation in HCT116 cells.
Introduction: Oligella infections are rare and have been only rarely reported in the literature. This may be due to the misidentification of Oligella as a Moraxella -like organism. To the best of our knowledge, we present what we believe to be the first case report on Oligella urethralis bacteraemia in India. Case presentation: A 65-year-old female patient with compromising underlying illness presented with signs and symptoms of bacteraemia. The organism was initially identified as Fransciella tularensis by a bioMérieux colorimetric VITEK 2 Compact GN ID card, but 16S rRNA gene sequencing confirmed the isolate as O. urethralis . Conclusion: The case emphasizes the importance of O. urethralis as an emerging opportunistic pathogen. Although automated systems allow accurate and rapid identification of commonly isolated bacterial organisms, they are less likely to correctly identify slow-growing, fastidious, rare or biochemically inert organisms. Therefore, it is good to confirm such isolates with a second method such as 16S sequencing and/or matrix-assisted laser desorption/ionization time-of-flight MS.
Abstract The loss of natural teeth can be avoided by invoking the molecular signal behind teeth regeneration. The destruction of the connective tissues is mainly due to bacterial origin which reacts to dental caries, a multifactorial disease. Glycosyl transferase is the enzyme which is involved in the glycosidic linkage. Glucosyltransferase inactivation reduces dental caries. This enzyme is a crucial virulence factor of Streptococcus mutans , a major pathogen that causes dental caries. In this present work, screening was done with library of anti-oxidant and anti-inflammatory molecules against the crystal structure of the target protein. Based on the predicted binding affinities, small molecules were selected and evaluated for their activity. Further, attempts were done to evaluate the toxicity of the lead compounds and compounds with no toxicity and good binding affinity were subjected for simulation and compared with reference complex. The potential energy of Glycosyl transferase-Eudesmol (proposed compound) (−1500 kj/mol) indicates its higher stability as compared to Glycosyl tranferase-G43 (reference) complex (−1100kj/mol).The inactives and actives compound for Glycosyl transferase was predicted from DeepScreening server.
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