Lithium chloride (LiCl)-modified polyethersulfone (PES) substrate surface pore architectures on thin poly(dimethylsiloxane) (PDMS) dense layer formation and the composite membrane's performance in gas separation.

The use of pore forming agents has been notable for improving the water flux in a water-based separation membrane but are rarely being studied as a methodology to influence the substrate's surface architectures for composite membrane fabrication in gas separation. In this study, the influence of lithium chloride (LiCl) on the surface pore architectures and hence, the gas permeance, has been studied in both bare and composite forms with poly(dimethylsiloxane) (PDMS). 1-4 wt% of LiCl was mixed with the dope solution of PES/NMP in the ratio 0.19 and was casted via the dry-wet phase inversion method. Bare substrates were noted to possess increasingly larger surface pore sizes but at a diminishing surface pore density with maximum surface porosity at 2 wt% LiCl. The permeances were, however, significantly reduced with the increase in the LiCl content from 105 300 to 4300 GPU for N2 gas, presumably due to the thicker skin layer. Nevertheless, the porous surface morphology was confirmed and exhibited Knudsen selectivity with a CO2/N2 selectivity of about 0.8, signifying minimal gas flow resistance by the substrates. Upon coating with a similar amount of thin PDMS layer, the composite permeances retain the same trend with values from 361.9 GPU for 0 wt% LiCl substrates to 68.8 GPU for 4 wt% LiCl substrates for CO2 gas at a consistent selectivity of about 14. As the PDMS layer of the same volumes were used and no significant difference in the coating thickness was noted, the mixed influence of pore intrusion and lateral diffusion is hypothesised at the substrate-coating interface owing to the different surface pore architectures of the substrates.

alpha-Tocopherol disturbs macrophage LXRalpha regulation of ABCA1/G1 and cholesterol handling.

Based on the oxidation hypothesis high doses of alpha-tocopherol have been advocated to prevent atherosclerosis, but clinical trials failed to demonstrate a benefit. As specific oxylipids activate PPARgamma and LXRalpha, master regulators of lipid metabolism and cholesterol exporters, we hypothesized, that high dose alpha-tocopherol might interfere with reverse cholesterol transport out of the vessel wall. Human THP-1 cells, a foam cell model, were preincubated with alpha-tocopherol or carrier before exposure to oxidized LDL, delipidated HDL or control buffer. Specific mRNAs were quantified by real-time RT-PCR, LXRalpha activation by a reporter gene assay and cellular cholesterol homeostasis by oxLDL and dHDL facilitated uptake and efflux assays. alpha-Tocopherol significantly reduced baseline expression and stimulation by oxLDL of LXRalpha activity, CD36, ABCA1, and ABCG1. alpha-Tocopherol also reversed the suppression of CD36 and ABCA1 by dHDL. Thus alpha-Tocopherol compromises cellular lipid scavenging and channelling of cholesterol into reverse transport out of the vessel wall.

HybF, a zinc-containing protein involved in NiFe hydrogenase maturation.

HypA and HypB are maturation proteins required for incorporation of nickel into the hydrogenase large subunit. To examine the functions of these proteins in nickel insertion, the hybF gene, which is a homolog of hypA essential for maturation of hydrogenases 1 and 2 from Escherichia coli, was overexpressed, and the product was purified. This protein behaves like a monomer in gel filtration and contains stoichiometric amounts of zinc but insignificant or undetectable amounts of nickel and iron. In filter binding assays radioactively labeled nickel binds to HybF with a K(D) of 1.87 microM and in a stoichiometric ratio. To identify amino acid residues of HybF involved in nickel and/or zinc binding, variants in which conserved residues were replaced were studied. An H2Q replacement eliminated both in vivo activity and in vitro binding of nickel. The purified protein, however, contained zinc at the level characteristic of the wild-type protein. When E3 was replaced by Q, activity was retained, but an E3L exchange was detrimental. Replacement of each of the four conserved cysteine residues of a zinc finger motif reduced the cellular amount of HybF protein without a loss of in vivo activity, indicating that these residues play a purely structural role. A triple mutant deficient in the synthesis or activity of HypA, HybF, and HypB was constructed, and it exhibited the same responsiveness for phenotypic complementation by high nickel as mutants with a single lesion in one of the genes exhibited. The results are interpreted in terms of a concerted action of HypB and HybF in nickel insertion in which HybF (as well as its homolog, HypA) functions as a metallochaperone and HypB functions as a regulator that controls the interaction of HybF with the target protein.