1.Soluble sortilin is released by activated platelets and its circulating levels are associated with cardiovascular risk factors.
Ogawa K1, Ueno T2, Iwasaki T3, Kujiraoka T3, Ishihara M3, Kunimoto S4, Takayama T4, Kanai T4, Hirayama A4, Hattori H3. Atherosclerosis. 2016 Apr 1;249:110-115. doi: 10.1016/j.atherosclerosis.2016.03.041. [Epub ahead of print]
OBJECTIVE: Sortilin is involved multilaterally in the development of atherosclerosis. Here, we examine the release of soluble sortilin (sSortilin) from platelets and assess the association between circulating levels of sSoritlin and atherothrombosis such as coronary artery disease (CAD).
2.A Pycnoporus sanguineus laccase for denim bleaching and its comparison with an enzymatic commercial formulation.
Iracheta-Cárdenas MM1, Rocha-Peña MA2, Galán-Wong LJ3, Arévalo-Niño K4, Tovar-Herrera OE5. J Environ Manage. 2016 Apr 13;177:93-100. doi: 10.1016/j.jenvman.2016.04.008. [Epub ahead of print]
A laccase from the basidiomycete Pycnoporus sanguineus strain RVAN5 was evaluated for its ability to decolorize synthetic dyes and denim bleaching. Dye color reduction and denim bleaching were monitored at different dye concentrations and incubation times. Dye decolorization by Pycnoporus sanguineus fungal crude extract (FCE) ranged from 80 to 96% within 2-4 h at 25-65 °C. Comparable results were obtained when violuric acid (VA) was added as mediator to the FCE, however, the number of decolorized dyes increased significantly. Dye decolorization rates with VA varied of initial and final optical density (595 nm) values of 2.5-3.0 and 0.2-0.02, respectively. P. sanguineus FCE had no substantial effect on denim bleaching when used alone, notwithstanding, the mixture of FCE with VA (10 mM) showed significant denim color reduction values and considerably higher than those obtained with a bleaching enzyme from a commercial formulation; CIElab values obtained with FCE/VA mixture were of ΔL = 6.
3.Chlorination of oxybenzone: Kinetics, transformation, disinfection byproducts formation, and genotoxicity changes.
Zhang S1, Wang X1, Yang H2, Xie YF3. Chemosphere. 2016 Apr 13;154:521-527. doi: 10.1016/j.chemosphere.2016.03.116. [Epub ahead of print]
UV filters are a kind of emerging contaminant, and their transformation behavior in water treatment processes has aroused great concern. In particular, toxic products might be produced during reaction with disinfectants during the disinfection process. As one of the most widely used UV filters, oxybenzone has received significant attention, because its transformation and toxicity changes during chlorine oxidation are a concern. In our study, the reaction between oxybenzone and chlorine followed pseudo-first-order and second-order kinetics. Three transformation products were detected by LC-MS/MS, and the stability of products followed the order of tri-chloro-methoxyphenoyl > di-chlorinated oxybenzone > mono-chlorinated oxybenzone. Disinfection byproducts (DBPs) including chloroform, trichloroacetic acid, dichloroacetic acid and chloral hydrate were quickly formed, and increased at a slower rate until their concentrations remained constant.
4.Hemagglutinin of influenza A virus binds specifically to cell surface nucleolin and plays a role in virus internalization.
Chan CM1, Chu H1, Zhang AJ1, Leung LH2, Sze KH1, Kao RY1, Chik KK3, To KK1, Chan JF1, Chen H1, Jin DY4, Liu L2, Yuen KY5. Virology. 2016 Apr 13;494:78-88. doi: 10.1016/j.virol.2016.04.008. [Epub ahead of print]
The hemagglutinin (HA) protein of influenza A virus initiates cell entry by binding to sialic acids on target cells. In the current study, we demonstrated that in addition to sialic acids, influenza A/Puerto Rico/8/34 H1N1 (PR8) virus HA specifically binds to cell surface nucleolin (NCL). The interaction between HA and NCL was initially revealed with virus overlay protein binding assay (VOPBA) and subsequently verified with co-immunoprecipitation. Importantly, inhibiting cell surface NCL with NCL antibody, blocking PR8 viruses with purified NCL protein, or depleting endogenous NCL with siRNA all substantially reduced influenza virus internalization. We further demonstrated that NCL was a conserved cellular factor required for the entry of multiple influenza A viruses, including H1N1, H3N2, H5N1, and H7N9. Overall, our findings identified a novel role of NCL in influenza virus life cycle and established NCL as one of the host cell surface proteins for the entry of influenza A virus.
