Analysis of factors associated with sterile inflammation in women with pe receiving different antihypertensive treatment strategies

Systemic inflammation alongside endothelial dysfunction is considered to play a crucial role in PE pathogenesis. Endothelial dysfunction can be assessed by endothelial glycocalyx (eGC) damage. eGC is a superficial layer of cells associated with endothelial membrane that provides all endothelial cells functions. Its damage can be evaluated by the levels of its circulating components in blood. Patients with PE generally receive methyldopa (Dopegyt) solely or in combination with nifedipine (Cordaflex), and there is no understanding of their effect on proinflammatory state of blood vessels. Our study aimed to assess levels of IL-6, IL-18, TNFα, galektin-3 and homocysteine as well as levels of syndecan-1, eCG structural component, representing system inflammatory response and endothelial dysfunction development in blood of women with early- and late-onset PE receiving different antihypertensive treatment strategies. Eighty-two patients were enrolled into this interventional longitudinal pilot study. The comparison group included 15 patients before 34 gestational weeks and 15 patients after 34 weeks. Study subgroup 1 included 12 patients with early- onset PE receiving Dopegyt solely and 16 patients with early-onset PE receiving Dopegyt together with Cordaflex. Study subgroup 2 included 12 patients with late-onset PE receiving Dopegyt solely and 12 patients with late-onset PE receiving combined therapy. As for early-onset PE, only IL-6 demonstrated statistically significant differences in patients receiving both treatment strategies compared to control. Proinflammatory state was more profound in late-onset PE. IL-6 levels were significantly increased in late-onset PE treated with Dopegyt. IL-6 and TNFa levels were significantly higher in late-onset PE patients treated with Dopegyt + Cordaflex compared to control. Syndecan-1 levels were statistically significantly higher in patients with early-onset PE treated with Dopegyt solely. There were no statistically significant differences between the groups despite elevated mean values of syndecan-1 in late-onset PE. Galectin-3 and homocysteine levels did not differ significantly between the groups, representing lack of pronounced inflammatory response and endothelial dysfunction

Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

© 2015, Pleiades Publishing, Ltd. Immunochemical analysis of the following purified preparations of Bacillus pumilus RNase (binase) was carried out: industrially manufactured enzyme (Institute of Organic Synthesis, Riga, Latvia) and the enzymes isolated from the culture liquid of the native B. pumilus producer and from the Escherichia coli BL21 recombinant strain bearing the pGEMGX1/ent/Bi plasmid. Electrophoresis of all three samples of purified binase revealed two protein fractions with ribonuclease activity possessing molecular masses of ∼12 and 25 kDa. The possible presence of binase II, a second secreted RNase, was ruled out. Both high- and low-molecular mass proteins interacted with binase-specific antibodies in the immunoblotting reaction, which indicated their antigenic identity. The difference in molecular mass between these proteins indicated the possible presence of two forms of binase in solution, a monomer and a dimer

Three-step procedure for preparation of pure Bacillus altitudinis ribonuclease

© 2015 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.Ribonucleases are considered as promising tools for anticancer treatment due to their selective cytotoxicity against tumor cells. We investigated a new RNase from Bacillus altitudinis termed BALNASE (B. altitudinisRNase). Balnase is a close homolog of the well-known cytotoxic binase, differing by only one amino acid residue: nonpolar hydrophobic alanine at position 106 in the balnase molecule is replaced by a polar uncharged threonine in binase. The most exciting question is how the physico-chemical properties and biological effects of RNase might be changed by A106T substitution. Here, we have developed a chromatography-based rapid and modern technique for the purification of this new RNase which allowed us to get a protein sample of high quality with specific activity of 1.2 × 106 units in preparative amounts, suitable for further investigation of its biological properties

Binase Immobilized on halloysite nanotubes exerts enhanced cytotoxicity toward human colon adenocarcinoma cells

© 2017 Khodzhaeva, Makeeva, Ulyanova. Many ribonucleases (RNases) are considered as promising tools for antitumor therapy because of their selective cytotoxicity toward cancer cells. Binase, the RNase from Bacillus pumilus, triggers apoptotic response in cancer cells expressing RAS oncogene which is mutated in a large percentage of prevalent and deadly malignancies including colorectal cancer. The specific antitumor effect of binase toward RAS-transformed cells is due to its direct binding of RAS protein and inhibition of downstream signaling. However, the delivery of proteins to the intestine is complicated by their degradation in the digestive tract and subsequent loss of therapeutic activity. Therefore, the search of new systems for effective delivery of therapeutic proteins is an actual task. This study is aimed to the investigation of antitumor effect of binase immobilized on natural halloysite nanotubes (HNTs). Here, we have developed the method of binase immobilization on HNTs and optimized the conditions for the enzyme loading and release (i); we have found the non-toxic concentration of pure HNTs which allows to distinguish HNTs- and binase-induced cytotoxic effects (ii); using dark-field and fluorescent microscopy we have proved the absorption of binase-loaded HNTs on the cell surface (iii) and demonstrated that binase-halloysite nanoformulations possessed twice enhanced cytotoxicity toward tumor colon cells as compared to the cytotoxicity of binase itself (iv). The enhanced antitumor activity of biocompatible binase-HNTs complex confirms the advisability of its future development for clinical practice

Notes for genera: basal clades of Fungi (including Aphelidiomycota, Basidiobolomycota, Blastocladiomycota, Calcarisporiellomycota, Caulochytriomycota, Chytridiomycota, Entomophthoromycota, Glomeromycota, Kickxellomycota, Monoblepharomycota, Mortierellomycota, Mucoromycota, Neocallimastigomycota, Olpidiomycota, Rozellomycota and Zoopagomycota)

Compared to the higher fungi (Dikarya), taxonomic and evolutionary studies on the basal clades of fungi are fewer in number. Thus, the generic boundaries and higher ranks in the basal clades of fungi are poorly known. Recent DNA based taxonomic studies have provided reliable and accurate information. It is therefore necessary to compile all available information since basal clades genera lack updated checklists or outlines. Recently, Tedersoo et al. (MycoKeys 13:1--20, 2016) accepted Aphelidiomycota and Rozellomycota in Fungal clade. Thus, we regard both these phyla as members in Kingdom Fungi. We accept 16 phyla in basal clades viz. Aphelidiomycota, Basidiobolomycota, Blastocladiomycota, Calcarisporiellomycota, Caulochytriomycota, Chytridiomycota, Entomophthoromycota, Glomeromycota, Kickxellomycota, Monoblepharomycota, Mortierellomycota, Mucoromycota, Neocallimastigomycota, Olpidiomycota, Rozellomycota and Zoopagomycota. Thus, 611 genera in 153 families, 43 orders and 18 classes are provided with details of classification, synonyms, life modes, distribution, recent literature and genomic data. Moreover, Catenariaceae Couch is proposed to be conserved, Cladochytriales Mozl.-Standr. is emended and the family Nephridiophagaceae is introduced

Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

© 2015, Pleiades Publishing, Ltd. Immunochemical analysis of the following purified preparations of Bacillus pumilus RNase (binase) was carried out: industrially manufactured enzyme (Institute of Organic Synthesis, Riga, Latvia) and the enzymes isolated from the culture liquid of the native B. pumilus producer and from the Escherichia coli BL21 recombinant strain bearing the pGEMGX1/ent/Bi plasmid. Electrophoresis of all three samples of purified binase revealed two protein fractions with ribonuclease activity possessing molecular masses of ∼12 and 25 kDa. The possible presence of binase II, a second secreted RNase, was ruled out. Both high- and low-molecular mass proteins interacted with binase-specific antibodies in the immunoblotting reaction, which indicated their antigenic identity. The difference in molecular mass between these proteins indicated the possible presence of two forms of binase in solution, a monomer and a dimer

Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

© 2015, Pleiades Publishing, Ltd. Immunochemical analysis of the following purified preparations of Bacillus pumilus RNase (binase) was carried out: industrially manufactured enzyme (Institute of Organic Synthesis, Riga, Latvia) and the enzymes isolated from the culture liquid of the native B. pumilus producer and from the Escherichia coli BL21 recombinant strain bearing the pGEMGX1/ent/Bi plasmid. Electrophoresis of all three samples of purified binase revealed two protein fractions with ribonuclease activity possessing molecular masses of ∼12 and 25 kDa. The possible presence of binase II, a second secreted RNase, was ruled out. Both high- and low-molecular mass proteins interacted with binase-specific antibodies in the immunoblotting reaction, which indicated their antigenic identity. The difference in molecular mass between these proteins indicated the possible presence of two forms of binase in solution, a monomer and a dimer

Preparations of Bacillus pumilus secreted RNase: One enzyme or two?

© 2015, Pleiades Publishing, Ltd. Immunochemical analysis of the following purified preparations of Bacillus pumilus RNase (binase) was carried out: industrially manufactured enzyme (Institute of Organic Synthesis, Riga, Latvia) and the enzymes isolated from the culture liquid of the native B. pumilus producer and from the Escherichia coli BL21 recombinant strain bearing the pGEMGX1/ent/Bi plasmid. Electrophoresis of all three samples of purified binase revealed two protein fractions with ribonuclease activity possessing molecular masses of ∼12 and 25 kDa. The possible presence of binase II, a second secreted RNase, was ruled out. Both high- and low-molecular mass proteins interacted with binase-specific antibodies in the immunoblotting reaction, which indicated their antigenic identity. The difference in molecular mass between these proteins indicated the possible presence of two forms of binase in solution, a monomer and a dimer