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- SourceAvailable from: Dr. Rohan Meshram[Show abstract] [Hide abstract]
ABSTRACT: Formation of new blood vessels (angiogenesis) has been demonstrated to be a basic prerequisite for sustainable growth and proliferation of tumor. Several growth factors, cytokines, small peptides and enzymes support tumor growth either independently or in synergy. Decoding the crucial mechanisms of angiogenesis in physiological and pathological state has remained a subject of intense interest during the past three decades. Currently, the most widely preferred approach for arresting tumor angiogenesis is the blockade of vascular endothelial growth factor (VEGF) pathway; however, the clinical usage of this modality is still limited by several factors like adverse effects, toxicity, acquired drug resistance, non availability of valid biomarkers etc. Nevertheless, angiogenesis, being a normal physiological process imposes limitations in maneuvering it as therapeutic target for tumor angiogenesis. The present review offers an updated relevant literature describing the role of well-characterized angiogenic factors, such as VEGF, basic fibroblast growth factor (bFGF), platelet derived growth factor (PDGF), placenta growth factor (PLGF), hepatocyte growth factor/scatter factor (HGF/SF) and angiopoetins (ANGs) in regulating tumor angiogenesis. We have also attempted to discuss tumor angiogenesis with a perspective of ‘an attractive target with emerging challenges’, along with the limitations and present status of anti-angiogenic therapy in the current state-of-the-art.Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 05/2014; 1846(1). DOI:10.1016/j.bbcan.2014.05.002
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ABSTRACT: Efficient alkaline protease producer was isolated from hyper alkaline-saline Lonar Soda Lake and identified as Bacillus alcalophilus LW8 using culture dependent techniques like morphological characters, microscopic features, biochemical pattern, physiological characters and molecular analysis. The 16S rRNA gene sequence was submitted in GenBank nucleotide repository under the accession number KC689353. Alkaline protease production was optimized by adopting one-variable-at-a-time approach using submerged fermentation system in modified fermentation medium (MFM). The optimized components of MFM were (w/w) casein (1%), sugarcane molasses (1%), NaCl (1%), ammonium sulphate (0.5%), KH2PO4 (0.05%), K2HPO4 (0.05%) and Na2CO3 (1%). The optimized culture conditions were used for alkaline protease production. Final yield of partially purified alkaline protease was achieved 53.35% after dialysis. The molecular weight of the dialyzed alkaline protease was determined by SDS–PAGE as 27 kDa. As per Lineweaver-Burk plot, calculated Km and Vmax values were 24 mg/mL and 1000 U/mg respectively. The enzyme was remarkably stable at the pH range of 7.0–12.0 with optimum activity at pH 10.0. LW8 alkaline protease was completely inhibited by PMSF at 10 mM concentration, indicating that the enzyme belongs to class serine protease. The metal ions viz. Ca2+, Ba2+, Mg2+, Zn2+, Fe3+, Cu2+, Mn2+ had increased catalytic activity of partially purified alkaline protease. Partially purified LW8 alkaline protease effectively decomposed gelatinous coating on X-ray film, hydrolyzed blood clot, removed blood stain from a piece of cotton fabric and hairs from a piece of goat skin.05/2014; 8(4). DOI:10.1016/j.jtusci.2014.04.002
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ABSTRACT: During a screening program for bioactive natural products, a potential Streptomyces sp was isolated from soil. On the basis of biochemical, cultural, physiological and 16S rRNA gene analysis, it was identified as Streptomyces purpurascens. The isolate was grown in liquid medium and the crude antibiotic complex was obtained by ethyl acetate extraction. Seven purified fractions were obtained by preparative Thin Layer Chromatography (TLC). Acid hydrolysis of each fraction and subsequent TLC led to the identification of aglycones and sugars indicating these compounds to be Rhodomycin and its analogues. The identity of these compounds was established on the basis of UV-visible and FT-IR spectra and comparison with published data. The compounds were active against Gram-positive bacteria. Compound E, identified as Rhodomycin B, was found to be the most potent compound with an MIC of 2 μg/ml against Bacillus subtilis. Compounds A and F identified as α2-Rhodomycin II and Obelmycin respectively, and Compound E exhibited an IC50 of 8.8 μg/ml against HeLa cell line but no cytotoxicity was found against L929. Electronic supplementary material The online version of this article (doi:10.1186/2193-1801-2-93) contains supplementary material, which is available to authorized users.SpringerPlus 12/2013; 2(1):93. DOI:10.1186/2193-1801-2-93
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