Dendrimer Enhanced Ultrafiltration. 1. Recovery of Cu(II) from Aqueous Solutions Using PAMAM Dendrimers with Ethylene Diamine Core and Terminal NH_2 Groups

This article discusses the feasibility of using dendrimer enhanced ultrafiltration (DEUF) to recover Cu(II) from aqueous solutions. Building upon the results of fundamental investigations of Cu(II) binding to PAMAM dendrimers with ethylenediamine (EDA) core and terminal NH_2 groups, we combine (i) dead-end ultrafiltration (UF) experiments with (ii) atomic force microscopy (AFM) characterization of membrane fouling to assess the feasibility of using DEUF to recover Cu(II) from aqueous solutions. On a mass basis, the Cu(II) binding capacities of the EDA core PAMAM dendrimers are much larger and more sensitive to solution pH than those of linear polymers with amine groups. The dendrimer−Cu(II) complexes can be efficiently separated from aqueous solutions by ultrafiltration. The metal ion laden dendrimers can be regenerated by decreasing the solution pH to 4.0; thus enabling the recovery of the bound Cu(II) ions and recycling of the dendrimers. The UF measurements and AFM characterization studies show that EDA core PAMAM dendrimers with terminal NH_2 groups have very low tendency to foul the commercially available regenerated cellulose (RC) membranes evaluated in this study. The overall results of these experiments suggest that DEUF is a promising process for recovering metal ions such as Cu(II) from aqueous solutions

Dendritic Chelating Agents. 1. Cu(II) Binding to Ethylene Diamine Core Poly(amidoamine) Dendrimers in Aqueous Solutions

This paper describes an investigation of the uptake of Cu(II) by poly(amidoamine) (PAMAM) dendrimers with an ethylenediamine (EDA) core in aqueous solutions. We use bench scale measurements of proton and metal ion binding to assess the effects of (i) metal ion−dendrimer loading, (ii) dendrimer generation/terminal group chemistry, and (iii) solution pH on the extent of binding of Cu(II) in aqueous solutions of EDA core PAMAM dendrimers with primary amine, succinamic acid, glycidol, and acetamide terminal groups. We employ extended X-ray absorption fine structure (EXAFS) spectroscopy to probe the structures of Cu(II) complexes with Gx-NH_2 EDA core PAMAM dendrimers in aqueous solutions at pH 7.0. The overall results of the proton and metal ion binding measurements suggest that the uptake of Cu(II) by EDA core PAMAM dendrimers involves both the dendrimer tertiary amine and terminal groups. However, the extents of protonation of these groups control the ability of the dendrimers to bind Cu(II). Analysis of the EXAFS spectra suggests that Cu(II) forms octahedral complexes involving the tertiary amine groups of Gx-NH_2 EDA core PAMAM dendrimers at pH 7.0. The central Cu(II) metal ion of each of these complexes appears to be coordinated to 2−4 dendrimer tertiary amine groups located in the equatorial plane and 2 axial water molecules. Finally, we combine the results of our experiments with literature data to formulate and evaluate a phenomenological model of Cu(II) uptake by Gx-NH_2 PAMAM dendrimers in aqueous solutions. At low metal ion−dendrimer loadings, the model provides a good fit of the measured extent of binding of Cu(II) in aqueous solutions of G4-NH_2 and G5-NH_2 PAMAM dendrimers at pH 7.0

Goodbye Hartmann trial: a prospective, international, multicenter, observational study on the current use of a surgical procedure developed a century ago

Background: Literature suggests colonic resection and primary anastomosis (RPA) instead of Hartmann's procedure (HP) for the treatment of left-sided colonic emergencies. We aim to evaluate the surgical options globally used to treat patients with acute left-sided colonic emergencies and the factors that leading to the choice of treatment, comparing HP and RPA. Methods: This is a prospective, international, multicenter, observational study registered on ClinicalTrials.gov. A total 1215 patients with left-sided colonic emergencies who required surgery were included from 204 centers during the period of March 1, 2020, to May 31, 2020. with a 1-year follow-up. Results: 564 patients (43.1%) were females. The mean age was 65.9 ± 15.6 years. HP was performed in 697 (57.3%) patients and RPA in 384 (31.6%) cases. Complicated acute diverticulitis was the most common cause of left-sided colonic emergencies (40.2%), followed by colorectal malignancy (36.6%). Severe complications (Clavien-Dindo ≥ 3b) were higher in the HP group (P < 0.001). 30-day mortality was higher in HP patients (13.7%), especially in case of bowel perforation and diffused peritonitis. 1-year follow-up showed no differences on ostomy reversal rate between HP and RPA. (P = 0.127). A backward likelihood logistic regression model showed that RPA was preferred in younger patients, having low ASA score (≤ 3), in case of large bowel obstruction, absence of colonic ischemia, longer time from admission to surgery, operating early at the day working hours, by a surgeon who performed more than 50 colorectal resections. Conclusions: After 100 years since the first Hartmann's procedure, HP remains the most common treatment for left-sided colorectal emergencies. Treatment's choice depends on patient characteristics, the time of surgery and the experience of the surgeon. RPA should be considered as the gold standard for surgery, with HP being an exception

Measuring the impact of sales on earnings and equity price

Sales, Earnings, Equity price, M41,

Importin beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function

Protein conjugation with small ubiquitin-related modifier (SUMO) is a post-translational modification that modulates protein interactions and localisation. RANBP2 is a large nucleoporin endowed with SUMO E3 ligase and SUMO-stabilising activity, and is implicated in some cancer types. RANBP2 is part of a larger complex, consisting of SUMO-modified RANGAP1, the GTP-hydrolysis activating factor for the GTPase RAN. During mitosis, the RANBP2–SUMO-RANGAP1 complex localises to the mitotic spindle and to kinetochores after microtubule attachment. Here, we address the mechanisms that regulate this localisation and how they affect kinetochore functions. Using proximity ligation assays, we find that nuclear transport receptors importin-β and CRM1 play essential roles in localising the RANBP2–SUMO-RANGAP1 complex away from, or at kinetochores, respectively. Using newly generated inducible cell lines, we show that overexpression of nuclear transport receptors affects the timing of RANBP2 localisation in opposite ways. Concomitantly, kinetochore functions are also affected, including the accumulation of SUMO- conjugated topoisomerase-IIα and stability of kinetochore fibres. These results delineate a novel mechanism through which nuclear transport receptors govern the functional state of kinetochores by regulating the timely deposition of RANBP2