Synthetic wastewaters treatment by electrocoagulation to remove silver nanoparticles produced by different routes.

Nanoscience is a field that has stood out in recent years. The accurate long-term health and environmental risks associated with these emerging materials are unknown. Therefore, this work investigated how to eliminate silver nanoparticles (AgNPs) from synthetic effluents by electrocoagulation (EC) due to the widespread use of this type of nanoparticle (NP) in industry and its potential inhibition power over microorganisms responsible for biological treatment in effluent treatment plants. Synthesized AgNPs were studied via four different routes by chemical reduction in aqueous solutions to simulate the chemical variations of a hypothetical industrial effluent, and efficiency conditions of the EC treatment were determined. All routes used silver nitrate as the source of silver ions, and two synthesis routes were studied with sodium citrate as a stabilizer. In route I, sodium citrate functioned simultaneously as the reducing agent and stabilizing agent, whereas route II used sodium borohydride as a reducing agent. Route III used D-glucose as the reducing agent and sodium pyrophosphate as the stabilizer; route IV used sodium pyrophosphate as the stabilizing agent and sodium borohydride as the reducing agent. The efficiency of the EC process of the different synthesized solutions was studied. For route I, after 85 min of treatment, a significant decrease in the plasmon resonance peak of the sample was observed, which reflects the efficiency in the mass reduction of AgNPs in the solution by 98.6%. In route II, after 12 min of EC, the absorbance results reached the detection limit of the measurement instrument, which indicates a minimum reduction of 99.9% of AgNPs in the solution. During the 4 min of treatment in route III, the absorbance intensities again reached the detection limit, which indicates a minimum reduction of 99.8%. In route IV, after 10 min of treatment, a minimum AgNP reduction of 99.9% was observed. Based on these results, it was possible to verify that the solutions containing citrate considerably increased the necessary times required to eliminate AgNPs from the synthesized effluent, whereas solutions free of this reagent showed better results on floc formation and, therefore, are best for the treatment. The elimination of AgNPs from effluents by EC proved effective for the studied routes.

Anxiolytic-like effects of standardized extract of Justicia pectoralis (SEJP) in mice: Involvement of GABA/benzodiazepine in receptor.

Justicia pectoralis (Acanthaceae) is used as an antiinflammatory, antimicrobial and bronchodilator, and its extract exerts an anxiolytic-like effect profile in animal models. This work presents the behavioral effects of an aqueous standardized extract of Justicia pectoralis (SEJP) in animal models, such as the elevated plus maze (EPM), light/dark, open field, rota rod and pentobarbital sleep time. The extract was administered intragastrically to male mice at single doses of 50, 100 and 200 mg/kg, while diazepam 1 or 2 mg/kg was used as a standard drug and flumazenil 2.5 mg/kg was used to evaluate the participation of benzodiazepinic receptors. The results showed that, similar to diazepam (1 mg/kg), SEJP significantly modified all the observed parameters in the EPM test, without altering the general motor activity in the open field, rota rod and pentobarbital sleep time tests. Flumazenil reversed not only the diazepam effect but also the SEJP effect. In the same way, all doses of SEJP increased the time of permanence in the light box in the light/dark test. The results showed that SEJP presented an anxiolytic-like effect, disproving sedative effects.

C-reactive protein and other markers of inflammation among patients undergoing HELP LDL apheresis.

Studies reveal important prognostic relationships between C-reactive protein (CRP) and atherosclerotic complications. A prospective trial of familial hypercholesterolemic patients treated with Heparin-induced Extra-corporeal Low-Density Lipoprotein Precipitation (HELP, B. Braun Melsungen) therapy was undertaken to evaluate the short- and long-term effects on CRP. Four patients received LDL apheresis therapy on an alternate week basis for 6 months. Pre- and post-treatment serum high sensitivity (hs) CRP levels (IMx(R), Abbott Laboratories), LDL-C, triglycerides, and fibrinogen were measured. Pre- and post-treatment mean serum levels of LDL-C were 281+/-76 and 98+/-34 mg/dl; triglycerides 191+/-64 and 123+/-50 mg/dl; fibrinogen 332+/-46 and 117+/-31 mg/dl, respectively. Before and after apheresis mean serum levels of hsCRP were 8.99+/-7.88 and 3.15+/-3.16 mg/ml, respectively, representing a 65% decrease. After 6 months of therapy, pre-treatment hsCRP showed an overall mean level decrease of 49%. Preliminary results indicate that LDL apheresis results in a rapid and long-term decrease of serum hsCRP levels.

Functional role of alpha 2/beta 1 and alpha 4/beta 1 integrins in leukocyte intercellular adhesion induced through the common beta 1 subunit.

Whereas all of the integrins in the VLA protein subfamily are involved in cell-extracellular matrix interactions, only VLA-4 (through the alpha 4 subunit) has been implicated in the triggering of intercellular adhesion. Here we describe that the VLA protein beta 1 subunit (CD29) is also involved in the induction of homotypic cell aggregation. We have obtained three novel anti-beta 1 monoclonal antibodies (mAb) with the ability to induce cell aggregation on different leukocyte cell types. These mAb recognize an antigenic site on the common beta 1 chain of VLA proteins which is topographically and/or functionally distinct from other epitopes previously defined by several prototype anti-beta 1 mAb. Induction of cell aggregation by anti-beta 1 mAb is epitope specific, isotype and Fc independent, and displays kinetics similar to alpha 4-mediated aggregation. This cell aggregation requires an intact cellular metabolism, the presence of divalent cations in the extracellular medium, and the integrity of the cytoskeleton. We also have found that the Na+/H+ antiporter may be essential for this process. For Ramos cells, which bear only the VLA alpha 4/beta 1 heterodimer, intercellular adhesion induced through the VLA-beta 1 chain could be selectively inhibited by other anti-beta 1 mAb as well as by anti-alpha 4 mAb. Interestingly, anti-beta 1 mAb which induced strong aggregation of VLA-alpha 2- or VLA-alpha 4-transfected K562 cells, had minimal effect on the alpha 2- alpha 4- alpha 5+ K562 cell line. Furthermore, the beta 1-mediated induction of cell aggregation on alpha 2-K562- and alpha 4-K562-transfected cells was blocked by preincubation with either anti-alpha 2 or anti-alpha 4 mAb, respectively, as well as by other anti-beta 1 mAb. Interestingly, parental K562 cells were able to interact with both alpha 2- and alpha 4-transfected K562 cells, thus suggesting that counter-receptors for both integrins (VLA-2 and VLA-4) might exist on these cells. Together these results provide strong evidence supporting the involvement of alpha 2/beta 1 and alpha 4/beta 1 heterodimers in intercellular interactions and underline the pivotal role of the common beta 1 chain of VLA proteins in the integrin-mediated induction of cell aggregation.

Identification and characterization of new antigenic fragments related to carcinoembryonic antigen in adult feces.

Antigens in human adult feces related to carcinoembryonic antigen (CEA) were analyzed with respect to their molecular masses, CEA domain compositions, and N-terminal amino acid sequences. By avoiding perchloric acid treatment, new fecal antigens related to CEA were identified. The fecal antigens revealed by Western blot were M(r) 78,000, 70,000, 60,000, 50,000, 44,000, 36,000, 33,000, and 25,000 and a species M(r) less than or equal to 14,000. Unlike native CEA, all of the fecal antigens were very poorly soluble in perchloric acid and did not bind to concanavalin A, suggesting that they had undergone significant deglycosylation in the digestive tract. The major fecal antigens were purified by immunoaffinity chromatography and their N-terminal amino acid sequences determined. FA78, FA60, FA33, and the M(r) less than or equal to 14,000 antigen had the N-terminal amino acid sequence of the CEA N-domain, and FA44 and FA25, the sequence of the CEA A2 domain. The CEA domain compositions of the fecal antigens were investigated by probing them with anti-CEA monoclonal antibodies of known domain specificities. The N-terminal amino acid sequences, immunoreactivities with anti-CEA monoclonal antibodies, and apparent molecular masses of the fecal antigens allowed the following domain assignments (based on CEA as N-A1B1-A2B2-A3B3): FA78, N-A1B1-A2B2-A3B3; FA60, N-A1B1-A2B2; FA44, A2B2-A3B3; FA33, N-A1B1; and FA25, A2B2. The M(r) less than or equal to 14,000 antigen was shown to be the N-domain of CEA or nonspecific cross-reacting antigen. FA36 was assigned the N-AB domain structure of nonspecific cross-reacting antigen. The results suggested that FA78, FA60, FA44, FA33, and FA25 were degradation products (including deglycosylation and proteolysis) of CEA and that FA36 was a degradation product of nonspecific cross-reacting antigen.