Highly Selective Extraction of Lithium from Spent NCM Cathode Powder Reconstructive Electrode by Acid-Free Electrochemical Process

The environmentally friendly and efficient recovery of valuable metals from spent lithium-ion batteries (LIBs) can mitigate environmental pollution and enhance resource utilization efficiency. This study proposed a process for coating spent NCM cathode powder (LiNixCoyMnzO2) on graphite sheets for the electrochemical leaching of lithium. Direct electrooxidation method for leaching from the prepared electrode sheets can achieve the selective leaching rate of Li+ close to 100% in Na2CO3 solution. In addition, the electron transfer mechanism was investigated during the electrooxidation process. Under optimal conditions, the same electrolyte solution was electrolyzed 40 times to enrich lithium by replacing fresh electrode sheets. Since there was almost no leaching of other metals, there was no need to add precipitants to obtain battery-grade Li2CO3 through evaporation and concentration. This strategy not only circumvents the risk of secondary pollution caused by the use of a large number of leaching agents but also shortens the lithium recycling process

TNF increases expression of RelB mRNA and prevents RelB protein degradation.

<p>(A) M-, R-, and T- OCPs generated as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135728#pone.0135728.g001" target="_blank">Fig 1B</a> were treated with PBS (P), R, T or R+T for 8 hr or for 48 hr by which time mature OCs had formed. Cell lysates were subjected to Western blot analysis of RelB and β-actin. (B) M-OCPs were treated with P, R, T or R+T for 4 and 24 hr (left panel), or M-, R- and T-OCPs were treated with P, R, T or R+T for 48 hr by which time mature OCs had formed (right panel). Total RNA was extracted to test mRNA expression of NFATc1 normalized to β-actin. **p < 0.01 vs. the respective PBS-treated cells. (C) M-OCPs were serum-starved for 2 hr followed by treatment of P, R or T in the presence of 10 μM MG-132 for 3 hr. Protein levels of RelB and β-actin were tested by Western blot. The data are the band levels measured densitometrically, normalized to β-actin.</p

TNF-induced macrophages express M1 markers.

<p>Ly6C⁺Gr1^- and Ly6C^-Gr1^- cells were sorted from cultured M-, T- and R-OCPs from 3-month-old C57Bl6 mice, as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135728#pone.0135728.g002" target="_blank">Fig 2A</a> (A). Total RNA was extracted from these sorted cells and mRNA expression levels of the M1 macrophage genes, TNF-α, iNOS, IL-1β and TGFβ1 as well as the M2 macrophage marker genes, PPAR-γ and IL-10, were tested by real-time PCR, normalized to β-actin (B). The data are representative of two independent experiments. *p < 0.05, **p < 0.01.</p

Over-expression of RelB inhibits RANKL-, but enhances TNF-induced OC differentiation.

<p>(A) BMCs from 3-month-old C57Bl6 mice were cultured with M-CSF for 2 days followed by treatment of ¼ volume of pMX-GFP or pMX-GFP-RelB retroviral supernatant in the presence of 2 ng/ml of polybrene for 3 days. GFP⁺F4/80⁺ cells were analyzed by flow cytometry (left panel) and RelB protein levels in GFP or RelB expressing cells that had been treated with P, R or T for 8 hr were tested by Western blot (right panel). (B) M-OCPs were infected with pMX-GFP or pMX-GFP-RelB retrovirus as above. After 24 hr of infection, the cells were treated with RANKL or TNF for 3 days or 4 days in the presence of M-CSF when mature OCs were observed under inverted microscopy. TRAP staining was performed to evaluate OC numbers and area, 4 wells per group, *p< 0.05, **p< 0.01. (C) M-OCPs were infected with GFP or GFP-RelB retrovirus and cultured with P, R or T for 3 or 4 days as above (B). Total RNA was extracted from these cells using Trizol reagent, and mRNA expression of NFATc1 normalized to β-actin was tested by real-time PCR. *p< 0.05, **p< 0.01 vs. GFP. The in vitro experiment was repeated twice with similar results.</p

RelB deficiency prevents TNF-induced M1 macrophage differentiation.

<p>BMCs from 4-month-old RelB-/- and WT littermate mice were cultured to produce M-, R- and T-OCPs, as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135728#pone.0135728.g001" target="_blank">Fig 1B</a>. Cells were subjected to flow cytometry to analyze expression of CD11b and F4/80 (A), Ly6C and Gr1 cells in the CD11b⁺F4/80⁺ population (B), and CD11c⁺ cells in the Ly6C⁺Gr1^- and Ly6C^-Gr1^- populations (C), as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135728#pone.0135728.g001" target="_blank">Fig 1B</a>. The experiment was repeated twice with similar results.</p

Conjugated Microporous Polymers with Rose Bengal Dye for Highly Efficient Heterogeneous Organo-Photocatalysis

Rose Bengal dye has been successfully integrated into the skeleton of a conjugated microporous polymer via palladium-catalyzed Sonogashira–Hagihara cross-coupling polycondensation. These polymers are stable in various solvents, including concentrated hydrochloric acid, and are thermally stable. The resulting polymers show substantial porosity and are highly active for heterogeneous photocatalytic aza-Henry reactions at room temperature for a wide range of substrates. Moreover, this noble-metal-free photocatalyst shows robust recycling capability with good retention of photoactivity over 10 cycles without significant loss of conversion (<10%). These data show that dye-functionalized conjugated microporous polymers are stable, highly active, and reusable noble-metal-free heterogeneous photo-organocatalysts

TNF Induction of NF-κB RelB Enhances RANKL-Induced Osteoclastogenesis by Promoting Inflammatory Macrophage Differentiation but also Limits It through Suppression of NFATc1 Expression

<div><p>TNF induces bone loss in common bone diseases by promoting osteoclast formation directly and indirectly, but it also limits osteoclast formation by inducing expression of NF-κB p100. Osteoclast precursors (OCPs) are derived from M1 (inflammatory) and M2 (resident) macrophages. However, it is not known if TNF stimulates or limits osteoclast formation through regulation of M1 or M2 differentiation or if RelB, a partner of p100, is involved. To investigate these questions, we treated bone marrow cells (BMCs) with M-CSF alone or in combination with TNF to enrich for OCPs, which we called M-OCPs and T-OCPs, respectively. We found that TNF switched CD11b⁺F4/80⁺ M-OCPs from Ly6C^-Gr1^- M2 to Ly6C⁺Gr1^-CD11c⁺ and Ly6C^-Gr1^-CD11c⁺ M1 cells. RANKL induced osteoclast formation from both Ly6C⁺Gr1^- and Ly6C^-Gr1^- T-OCPs, but only from Ly6C⁺Gr1^- M-OCPs, which formed significantly fewer osteoclasts than T-OCPs. Importantly, Ly6C⁺Gr1^- cells from both M- and T-OCPs have increased expression of the M1 marker genes, iNOS, TNF, IL-1β and TGFβ1, compared to Ly6C^-Gr1^- cells, and Ly6C^-Gr1^- cells from T-OCPs also have increased expression of iNOS and TGFβ1 compared to cells from M-OCPs. Both RANKL and TNF increased RelB mRNA expression. TNF significantly increased RelB protein levels, but RANKL did not because it also induced RelB proteasomal degradation. TNF inhibited RANKL-induced NFATc1 mRNA expression and osteoclast formation from M-OCPs, but not from T-OCPs, and it did not induce Ly6C⁺Gr1^-CD11c⁺ or Ly6C^-Gr1^-CD11c⁺ M1 macrophages from RelB-/- BMCs. Furthermore, overexpression of RelB in M-OCPs reduced RANKL-induced osteoclast formation and NFATc1 mRNA expression, but it increased TNF-induced OC formation without affecting NFATc1 levels. Thus, TNF induction of RelB directly mediates terminal osteoclast differentiation independent of NFATc1 and limits RANKL-induced osteoclastogenesis by inhibiting NFATc1 activation. However, the dominant role of TNF is to expand the OCP pool by switching the differentiation of M-CSF-induced M2 to M1 macrophages with enhanced osteoclast forming potential. Strategies to degrade RelB could prevent TNF-induced M2/M1 switching and reduce osteoclast formation.</p></div

Iron Catalyzed Asymmetric Hydrogenation of Ketones

Chiral molecules, such as alcohols, are vital for the manufacturing of fine chemicals, pharmaceuticals, agrochemicals, fragrances, and novel materials. These molecules need to be produced in high yield and high optical purity and preferentially catalytically. Among all the asymmetric catalytic reactions, asymmetric hydrogenation with H₂ (AH) is the most widely used in the industry. With few exceptions, these AH processes use catalysts based on the three critical metals, rhodium, ruthenium, and iridium. Herein we describe a simple, industrially viable iron catalyst that allows for the AH of ketones, a process currently dominated by ruthenium and rhodium catalysts. By combining a chiral, 22-membered macrocyclic ligand with the cheap, readily available Fe₃(CO)₁₂, a wide variety of ketones have been hydrogenated under 50 bar H₂ at 45–65 °C, affording highly valuable chiral alcohols with enantioselectivities approaching or surpassing those obtained with the noble metal catalysts. In contrast to AH by most noble metal catalysts, the iron-catalyzed hydrogenation appears to be heterogeneous

TNF-induced macrophages have higher OC forming potential than M-CSF-induced macrophages.

<p>(A) M-, T-, and R-OCPs cultured from BMCs from a 4-month-old C57Bl6 mouse were stained with the fluorescent-labeled antibodies as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135728#pone.0135728.g001" target="_blank">Fig 1</a>. Ly6C⁺Gr1^- and Ly6C^-Gr1^- populations from CD11b^<b>+</b>F4/80^<b>+</b> cells were sorted by flow cytometry. (B) The sorted cell populations were seeded in 96-well plates (4x10⁴ cells/well) and treated with RANKL or TNF in the presence of M-CSF for 2 additional days to generate mature OCs, which were stained for TRAP activity. (C) Quantitation of numbers of OCs formed from each sorted population in (B), 4 wells per group, *p < 0.05, **p < 0.01. The experiment was repeated twice with similar results. M = M-CSF, P = PBS, R = RANKL, T = TNF, R+T = RANKL+TNF.</p

TNF promotes the differentiation of Ly6C⁺Gr1^-CD11c⁺ M1 macrophages.

<p>(A) Freshly isolated bone marrow cells (BMCs) from 3-month-old C57Bl6 mice were stained with anti-mouse APC-Ly6C, PEcy7-CD11b, PE-Gr1, FITC-CD11c and PEcy5-F4/80 antibodies and expression levels of these cell surface markers were analyzed by flow cytometry. (B) BMCs (2x10⁶) from the mice in (A) were cultured with M-CSF, M-CSF+TNF (20ng/ml) or M-CSF+RANKL (10ng/ml) in 60 mm-dishes for 3 days to recruit OCPs, which we called M-CSF-induced OCPs (M-OCPs), TNF-induced OCPs (T-OCPs), and RANKL-induced OCPs (R-OCPs), respectively. IFN-γ (1ng/ml) was also added to M-CSF-treated cells as a positive control for M1 macrophage recruitment. Cells attached to the dishes were collected and stained with the above antibodies to analyze expression of cell surface markers by flow cytometry: CD11b⁺F4/80⁺ cells in the total cultured OCPs (upper panel), Ly6C⁺Gr1^- and Ly6C^-Gr1^- cells in the CD11b⁺F4/80⁺ population (middle panel) and CD11c⁺ cells in the Ly6C⁺Gr1^- and Ly6C^-Gr1^- populations (lower panel). The experiment was repeated three times with similar results.</p