Lithium-sensitive calcium activity in the germination of apple (Malus domestica Borkh.), tobacco (Nicotiana tabacum L.), and potato (Solanum tuberosum L.) pollen

We have investigated Ca²⁺ activity during pollen germinationand the possibility that it may be responding to a phosphoinositidesignal transduction pathway, by employing inhibitors of Ca²⁺channels (verapamil and TMB-8), EGTA as a Ca²⁺ scavenger andthe inositol 1-phosphatase inhibitor lithium chloride. We havefound that at least two Ca²⁺ pools are utilized during pollengermination. Influx of extracellular Ca²⁺ appears to be necessaryfor the germination of apple and tobacco pollen, but it doesnot appear to be required for the germination of potato pollen.Conversely, activation of intracellularly stored Ca²⁺ was necessaryfor optimal germination of all three pollen species. LiCI hadstrong effects on pollen germination. At 5 mM LiCI, pollen germinationwas inhibited by 78% for apple, 84% for tobacco, and 74% forpotato. Li⁺ inhibition was overcome by the addition of Ca²⁺,which restores germination of all three species to 85–100%of that observed in controls, myo-lnositol also partially overcomesLi⁺ inhibition of pollen germination, thus providing some evidencefor a link between Li⁺ inhibition and Ca²⁺ rescue, myo-lnositolrescue of Li⁺ inhibition was most effective for potato pollen.Chlorotetracycline (CTC) spectroscopy revealed a higher levelof membrane-Ca²⁺ in Li ⁺ -treated pollen grains than in controls,and the short pollen tubes which did emerge did not accumulatemembrane-associated Ca²⁺. The results suggest that Li⁺ inhibitionmay interfere with the release (activation) or partitioningof membrane-Ca²⁺ during pollen germination and that this Ca²⁺activity may be responding, at least in part, with a phosphoinositidesignal transduction pathway. Key words: Pollen germination, lithium inhibition, calcium, inositol, calcium inhibitors     

Lithium inhibits glycogen synthase kinase-3 activity and mimics Wingless signalling in intact cells

Background Exposing eukaryotic cells to lithium ions (Li⁺) during development has marked effects on cell fate and organization. The phenotypic consequences of Li⁺ treatment on Xenopus embryos and sporulating Dictyostelium are similar to the effects of inhibition or disruption, respectively, of a highly conserved protein serine/threonine kinase, glycogen synthase kinase-3 (GSK-3). In Drosophila, the GSK-3 homologue is encoded by zw3^sgg, a segment-polarity gene involved in embryogenesis that acts downstream of wg. In higher eukaryotes, GSK-3 has been implicated in signal transduction pathways downstream of phosphoinositide 3-kinase and mitogen-activated protein kinases.Results We investigated the effect of Li⁺ on the activity of the GSK-3 family. At physiological doses, Li⁺ inhibits the activity of human GSK-3β and Drosophila Zw3^Sgg, but has no effect on other protein kinases. The effect of Li⁺ on GSK-3 is reversible in vitro. Treatment of cells with Li⁺ inhibits GSK-3-dependent phosphorylation of the microtubule-associated protein Tau. Li⁺ treatment of Drosophila S2 cells and rat PC12 cells induces accumulation of cytoplasmic Armadillo/β-catenin, demonstrating that Li⁺ can mimic Wingless signalling in intact cells, consistent with its inhibition of GSK-3.Conclusions Li⁺ acts as a specific inhibitor of the GSK-3 family of protein kinases in vitro and in intact cells, and mimics Wingless signalling. This reveals a possible molecular mechanism of Li⁺ action on development and differentiation.     

Lithium Enhances Muscarinic Receptor–Stimulated CDP-Diacylglycerol Formation in Inositol-Depleted SK-N-SH Neuroblastoma Cells

Abstract: The psychotherapeutic action of Li⁺ in brain has been proposed to result from the depletion of cellular inositol secondary to its block of inositol monophosphatase. This action is thought to slow phosphoinositide resynthesis, thereby attenuating stimulated phosphoinositidase-mediated signal transduction in affected cells. In the present study, the effect of Li⁺ on muscarinic receptor–stimulated formation of the immediate precursor of phosphatidylinositol, CDP-diacylglycerol (CDP-DAG), has been examined in human SK-N-SH neuroblastoma cells that have been cultured under conditions that alter the cellular content of myo-inositol. Resting neuroblastoma cells, like brain cells in vivo, were found to concentrate inositol from the culture medium, achieving an intracellular level of 60.0 ± 4 nmol/mg of protein. The addition of carbachol to [³H]cytidine-prelabeled cells elicited a four- to fivefold increase in the accumulation of labeled CDP-DAG. This stimulated formation of [³H]CDP-DAG was completely blocked by the addition of 10 μM atropine, was not dependent on the presence of Li⁺, nor was it affected by co-incubation with myo-inositol. This result was in sharp contrast to findings in rat brain slices, in which carbachol-stimulated formation of [³H]CDP-DAG was potentiated ～ 10-fold by Li⁺ and substantially reduced by coincubation with inositol. The formation of [³H]CDP-DAG in labeled SK-N-SH cells by carbachol was both concentration and time dependent. The order of efficacy of muscarinic ligands in stimulating [³H]-CDP-DAG accumulation paralleled that established in these cells for inositol phosphate accumulation, i.e., carbachol ≥ oxotremorine-M > bethanecol ≥ arecoline > oxotremorine > pilocarpine. Extended culture of the SK-N-SH cells in an inositol-free chemically defined growth medium progressively reduced the intracellular inositol content to <5 nmol/mg of protein, a level comparable with that seen in cortical slices. In these inositol-depleted cells, Li⁺ potentiated carbachol-stimulated [³H]CDP-DAG formation, and this effect was completely reversed by coincubation with inositol (EC₅₀ 0.2 mM). The present study thus demonstrates, in the same cultured cell line, the effects of normal and reduced intracellular inositol levels on the ability of Li⁺ to attenuate phosphoinositide resynthesis, as inferred from [³H]CDP-DAG accumulation. The results indicate that Li⁺ can lead to a slowing of stimulated phosphoinositide turnover in neuroblastoma cells, provided that the intracellular inositol content has been significantly reduced.     

Li+-regulated 1-aminocyclopropane-1-carboxylate synthase gene expression in Arabidopsis thaliana

In Arabidopsis thaliana, 1-aminocyclopropane-1-carboxylate synthase (ACS) is encoded by a multigene family consisting of at least five members whose expression is induced by hormones, developmental signals, and protein synthesis inhibition. Li⁺, known to interfere with the phosphoinositide (PI) second messenger system by inhibiting the activity of inositol-phosphate phosphatases, is one of the strongest inducers of ACC synthase activity in plants. Treatment of etiolated Arabidopsis seedlings with LiCl results in a rapid induction of the ACS5 gene. Also, LiCl represses the cycloheximide (CHX)-induced accumulation of the ACS2 mRNA. The effects of Li⁺ on the expression of ACS5 and ACS2 are specific, dose-dependent, and can be reversed by Ca²⁺ and mimicked by the protein kinase inhibitor K-252a. The results suggest that the regulation of some ACS genes by various inducers may involve protein kinase activity, which in turn may be controlled through an inositol 1,4,5-triphosphate (IP₃)-mediated Ca²⁺ mobilization. Since plants contain no Li⁺, the cation appears to unmask pre-existing biochemical capacity that may be utilized by various unknown transducers during plant growth and development.     

Absence of an effect of the lithium-induced increase in cyclic GMP on the cyclic GMP-stimulated phosphodiesterase (PDE II). Evidence for cyclic AMP-specific hydrolysis

Chronic treatment of rats with LiCl is known to induce a decrease in cAMP, while this decrease has also been found to occur together with both a simultaneous increase in total cortical phosphodiesterase (PDE; EC 3.1.4.17) activity and a concomitant increase in cGMP. These studies have implicated an involvement of PDE in lithium (Li⁺) action and it has been suggested that cGMP and the cGMP-stimulated PDE may be instrumental in the observed effects of Li⁺ on cAMP. In this study, three isozymes of PDE were isolated and identified from rat cortex and their activity determined, together with simultaneous measurement of cAMP and cGMP, after chronic treatment with oral LiCl (0.35% m/m). Li⁺ treatment exerted profound effects on cyclic nucleotides in the cortex, inducing significant suppression of cAMP while increasing cGMP levels. However, the ion only induced a slight but insignificant increase in the activities of the three PDE isozymes. To confirm these observations, methylparaben (MPB), a drug demonstrating both an ability to induce a selective stimulation of cAMP-specific PDE and also to lower intracellular levels of cGMP, was co-administration orally (0.4% m/m) with Li⁺ over the same period. This combination emphasized certain actions of Li⁺ not noted with Li⁺ alone. MPB inhibited the Li⁺-induced increase in cGMP, yet did not prevent the ion from decreasing cAMP. However, the combination of Li⁺ and MPB engendered a synergistic 100% increase in the activity of the membrane-bound, cAMP-specific PDE, PDE IV. This combination also produced a significant suppression of cAMP, while no reduction in cGMP was observed. The data is indicative that Li⁺-induced suppression of cAMP does not appear to be related to an effect on the cGMP-dependent PDE II, and that the increases in cGMP and PDE induced by Li⁺ observed previously and in the present study are two unrelated events. Instead, the synergistic response of Li⁺ plus MPB on PDE IV, and the associated reduction of cAMP, indicate that Li⁺ may promote selective cAMP hydrolysis via an effect on membrane-bound forms of PDE. This effect of Li⁺ on PDE IV, as well as the reciprocal effects on cyclic nucleotide balance, may have important implications in explaining the antipsychotic actions of the ion.     

Functional identification of sll1383 from<Emphasis Type="Italic"> Synechocystis</Emphasis> sp PCC 6803 as L-<Emphasis Type="Italic">myo</Emphasis>-inositol 1-phosphate phosphatase (EC 3.1.3.25): molecular cloning,expression and characterization

The genome sequence of the cyanobacterium Synechocystis sp. PCC6803 revealed four Open reading frame (ORF) encoding putative inositol monophosphatase or inositol monophosphatase-like proteins. One of the ORFs, sll1383, is ∼870 base pair long and has been assigned as a probable myo-inositol 1 (or 4) monophosphatase (IMPase; EC 3.1.3.25). IMPase is the second enzyme in the inositol biosynthesis pathway and catalyses the conversion of L-myo-inositol 1-phosphate to free myo-inositol. The present work describes the functional assignment of ORF sll1383 as myo-inositol 1-phosphate phosphatase (IMPase) through molecular cloning, bacterial overexpression, purification and biochemical characterization of the gene product. Affinity (K _m) of the recombinant protein for the substrate DL-myo-inositol 1-phosphate was found to be much higher (0.0034 ± 0.0003 mM) compared to IMPase(s) from other sources but in comparison V _max (∼0.033 μmol Pi/min/mg protein) was low. Li⁺ was found to be an inhibitor (IC₅₀ 6.0 mM) of this enzyme, other monovalent metal ions (e.g. Na⁺, K⁺ NH₄⁺) having no significant effect on the enzyme activity. Like other IMPase(s), the activity of this enzyme was found to be totally Mg²⁺ dependent, which can be substituted partially by Mn²⁺. However, unlike other IMPase(s), the enzyme is optimally active at ∼42°C. To the best of our knowledge, sll1383 encoded IMPase has the highest substrate affinity and specificity amongst the known examples from other prokaryotic sources. A possible application of this recombinant protein in the enzymatic coupled assay of L-myo-inositol 1-phosphate synthase (MIPS) is discussed.     

Lithium induces dorsal-type migration of mesodermal cells in the entire marginal zone of urodele amphibian embryos

Summary The effect of lithium (Li⁺) on gastrulation movements was investigated during the development of the urodele amphibianPleurodeles waltl. Attention was focused on mesodermal cell migration. Under conditions of Li⁺ treatment providing a maximal enhancement of dorsoanterior structures, it was found that the dorsoventral polarity of gastrulation was abolished. In particular, vital staining and scanning electron microscopy observations on embryo fractures showed that mesodermal cells migrated radially after Li⁺ treatment, which led to the formation of rounded embryos. Epiboly movements thus were accelerated. Nevertheless, contrasting with the precocious disappearance of the early-formed yolk plug, archenteron invagination was constantly retarded and commenced with a delay of several hours as compared to control gastrulae. Cell-lineage analysis of the progenies from ventral or dorsal equatorial blastomeres of 32-cell-stage embryos provided evidence that both dorsal and ventral mesoderm contributed to notochordal tissue after Li⁺ treatment. Dorsalization of the entire marginal zone was confirmed by the ability of the entire mesoderm rudiment to behave as a dorsal organiser after Li⁺ treatment. Comparison of the migratory behaviour of isolated animal hemispheres from Li⁺-treated or control embryos cultured on fibronectin-coated substrate indicated that all marginal cells acquired the autonomous capacity for migration of dorsal marginal cells under the action of lithium.     

Regional and Subcellular Localization of Li+ and Other Cations in the Rat Brain Following Long-Term Lithium Administration

Abstract: Rats were given LiCl in their diet (40 mmol/kg dry weight) for at least 3 months to elucidate the regional and subcellular localization of Li⁺ in the brain as well as the effect of chronic lithium administration on the distribution of other cations. At steady-state the mean concentrations of Li⁺ were 0.66 mmol/kg wet weight in the whole brain and 0.52 mM in plasma. The tissue/plasma concentration ratio exceeded unity in all anatomical regions. No region showed excessive accumulation of Li⁺. Whole brain or regional contents of Na⁺ or K⁺ were unaffected by lithium treatment. Subcellular Li⁺ localization was demonstrated in nuclear, crude mitochondrial, and microsomal fractions of whole brain homogenate. Subfractionation of the crude mitochondrial fraction revealed energy-independent intrasynaptosomal and intramitochondrial Li⁺ and K⁺ localization at 0–4°C. Li⁺ administered in vivo disappeared within 10 min from synaptosomes incubated at 37°C. Li⁺ added in vitro at 1 mM attained a synaptosomal steady-state concentration within 30 min at 37°C. In control rats, synaptosomal concentrations and synaptosomal/medium concentration gradients of cations paralleled their respective in vivo concentrations and gradients. Lithium treatment caused synaptosomal depletion of K⁺ and Mg²⁺ and hence probably partial membrane depolarization. Addition of 1 mM Li⁺ in vitro also caused synaptosomal Mg²⁺ depletion. The results indicate that Li⁺ is “accumulated” in brain sediments and synaptosomes following its long-term treatment. The estimated intracellular and intrasynaptosomal Li⁺ concentrations are lower than predicted by passive distribution according to the Nernst equation, evidencing active extrusion of Li⁺.     

Lithium-selective permeation through lipid bilayer membranes mediated by a di-imide ionophore with nonsymmetrical imide substituents (ETH1810)

Summary The neutral, noncyclic Li^–-selective ionophore ETH1810, which is a di-imide, differs structurally from previous similar ionophores by removal of the intramolecular symmetry of the N-imide substituents. Properties of this ionophore, as a potential carrier of lithium, were probed through studies of ionophore-induced changes in electrical properties of lipid bilayer membranes. ETH1810 was found capable of transporting lithium and other monovalent cations, across lipid bilayer membranes, forming 21 ionophore: ion membrane-permeating species. It was found to be 10-fold more potent than ETH1644, which was the previous best ionophore of this type. The selectivity sequence among alkali cations was found to be: Li⁺(1)>Na⁺ (0,009)>K⁺ (0.004)>Cs⁺(0.0035). Among the physiological alkali cations, it constitutes a 40 (vs. Na⁺) to 160% (vs. K⁺) improvement over ETH1644. ETH1810 was also found to be capable of acting as a carrier of biogenic amines and related molecules, with the following selectivity sequence: tryptamine (20)>phenylethylamine (7.8)>tyramine (4.3)>serotonin (2.5)>Li⁺ (1)>NH ₄ ⁺ (0.013)>dopamine (0.012). It was found that protons, at physiological concentrations, do not interfere with the lithium transport mediated by ETH1810. The relationship between the improvements in ionic selectivity and potencyvs. the differences in structural features is discussed.     

Toward a Four‐Electron Redox Quinone Polymer for High Capacity Lithium Ion Storage

Despite recent advances, current polymeric organic cathode materials have failed to incorporate a high degree of lithium storage in a small molecular framework, resulting in low capacities relative to monomers. This report discloses the development of a lithium salt polymer of dihydroxyanthraquinone (LiDHAQS) capable of storing four Li⁺ per monomer. The combination of storing four Li⁺ per monomer and a low molecular weight monomer results in a capacity of 330 mA h g^?1, a record for this class of material. The additional redox events responsible for added Li⁺ storage occur between 3.0 and 3.6 V versus Li/Li⁺ resulting in an average discharge potential of 2.5 V versus Li/Li⁺. These metrics combined yield a high energy density of 825 W h kg^?1 which is a 55% improvement over commercial lithium cobalt oxide. The high performance of LiDHAQS makes it a promising material for next generation Li⁺ cathodes.     

Polysulfide‐Shuttle Control in Lithium‐Sulfur Batteries with a Chemically/Electrochemically Compatible NaSICON‐Type Solid Electrolyte

A NaSICON‐type Li⁺‐ion conductive membrane with a formula of Li_{1+ x} Y _x Zr_{2? x} (PO₄)₃ (LYZP) (x = 0–0.15) has been explored as a solid‐electrolyte/separator to suppress polysulfide‐crossover in lithium‐sulfur (Li‐S) batteries. The LYZP membrane with a reasonable Li⁺‐ion conductivity shows both favorable chemical compatibility with the lithium polysulfide species and exhibits good electrochemical stability under the operating conditions of the Li‐S batteries. Through an integration of the LYZP solid electrolyte with the liquid electrolyte, the hybrid Li‐S batteries show greatly enhanced cyclability in contrast to the conventional Li‐S batteries with the porous polymer (e.g., Celgard) separator. At a rate of C/5, the hybrid Li ||LYZP|| Li₂S₆ batteries developed in this study (with a Li‐metal anode, a liquid/LYZP hybrid electrolyte, and a dissolved lithium polysulfide cathode) delivers an initial discharge capacity of ≈1000 mA h g^?1 (based on the active sulfur material) and retains ≈90% of the initial capacity after 150 cycles with a low capacity fade‐rate of <0.07% per cycle.     

An Anion‐Tuned Solid Electrolyte Interphase with Fast Ion Transfer Kinetics for Stable Lithium Anodes

The spatial distribution and transport characteristics of lithium ions (Li⁺) in the electrochemical interface region of a lithium anode in a lithium ion battery directly determine Li⁺ deposition behavior. The regulation of the Li⁺ solvation sheath on the solid electrolyte interphase (SEI) by electrolyte chemistry is key but challenging. Here, 1 m lithium trifluoroacetate (LiTFA) is induced to the electrolyte to regulate the Li⁺ solvation sheath, which significantly suppresses Li dendrite formation and enables a high Coulombic efficiency of 98.8% over 500 cycles. With its strong coordination between the carbonyl groups (C?O) and Li⁺, TFA^? modulates the environment of the Li⁺ solvation sheath and facilitates fast desolvation kinetics. In addition, due to relatively smaller lowest unoccupied molecular orbital energy than solvents, TFA^? has a preferential reduction to produce a stable SEI with uniform distribution of LiF and Li₂O. Such stable SEI effectively reduces the energy barrier for Li⁺ diffusion, contributing to low nucleation overpotential, fast ion transfer kinetics, and uniform Li⁺ deposition with high cycling stability. This work provides an alternative insight into the design of interface chemistry in terms of regulating anions in the Li⁺ solvation sheath. It is anticipated that this anion‐tuned strategy will pave the way to construct stable SEIs for other battery systems.     

LITHIUM INHIBITS GROWTH IN A MURINE NEURAL PRECURSOR CELL LINE

The influence of lithium on cell growth and cell viability was studied in short-term cultures of a neural precursor cell line (NT) developed from a murine teratocarcinoma. At very low concentrations ranging from 0.1 m to 1 m Li₂CO₃(equivalent to therapeutic blood concentrations) there was no difference between untreated and treated cultures. 10 m lithium (Li⁺) was found to be toxic with 33% of cell death, while there was inhibition of growth without cell death at concentrations of 2.5 m and 5 m of Li⁺. In experiments where 2.5 m Li⁺was added at the time of seeding, there was growth arrest on day 1 followed by recovery on day 2. Flow cytometric analysis revealed that cells treated with Li⁺were blocked in S phase. At 5 m concentration of Li⁺, the recovery occurred on day 3 and the plating efficiency was significantly low. The ability to form colonies in soft agar was reduced at 2.5 m and 5 m concentrations of Li⁺to an equal extent. Thus, Li⁺has growth inhibitory as well as anchorage-independent growth reducing effects. The NT cell line therefore would be a good model system to study the mechanism of teratogenic effect of Li⁺.     

Lithium treatment of affective disorders: effects of lithium on the inositol phospholipid and cyclic AMP signalling pathways

The effects of lithium (Li⁺) on the adenylyl cyclase and inositol phospholipid receptor signalling pathways were compared directly in noradrenergic and carbachol stimulated rat brain cortical tissue slices. Li⁺ was a comparatively weak inhibitor of noradrenaline-stimulated cyclic AMP accumulation with an IC₅₀ of approx. 20 mM. By contrast, half-maximal effects of Li⁺ on inositol monophosphate (InsP) accumulation in [³H]inositol labelled tissue slices occurred at about 1 mM. A similar IC₅₀ for Li⁺ of about 1 mM was also obtained for noradrenaline-stimulated accumulation of CMP-phosphatidate (CMPPA), a sensitive indicator of intracellular inositol depletion, in tissue slices that had been prelabelled with [³H]cytidine. The effect of myo-inositol (inositol) depletion on the prolonged activity of phosphoinositidase C (PIC) was examined in carbachol-stimulated corticol slices using a novel mass assay fro InsP. Exposure to a maximal dose of carbachol for 30 min in the presence of 5 mM Li⁺ caused a 10-fold increase in the level of radioactivity associated with the InsP fraction, but only a 2-fold increase in InsP mass. During prolonged incubations in the presence of both carbachol and Li⁺ the accumulation of InsP mass was enhanced if 30 mM inositol was included in the medium. The results are comptable with the inositol depletion hypothesis of Li⁺ action but do not support the concept that adenylyl cyclase or guanine nucleotide dependent proteins represent therapeutically relevant targets of this drug.     

Cloning of Arabidopsis thaliana phosphatidylinositol synthase and functional expression in the yeast pis mutant

It is believed that phosphatidylinositol (PI) metabolism plays a central role in signalling pathways in both animals and higher plants. PI is synthesized from CDP-diacylglycerol (CDP-DG) and myo-inositol by phosphatidylinositol synthase (PI synthase, EC 2.7.8.11). Here we report the identification of a plant cDNA (AtPIS1) encoding a 26 kDa PI synthase from Arabidopsis thaliana. The plant enzyme as deduced from its cDNA sequence shares 35–41% identical amino acids with PI synthases from Saccharomyces cerevisiae and mammals. AtPIS1 functionally complements a mutant of S. cerevisiae with a lesion in PI synthase, and recombinant AtPIS1 protein present in yeast membranes strongly depends on the two principal substrates, myo-inositol and CDP-DG, and requires Mg²⁺ ions for full activity.     

Light- and Clock-Controlled Leaflet Movements in Samanea saman*: A Physiological,Biophysical and Biochemical Analysis**

Leaflet movements in the legume Samanea saman are under joint control by light and a circadian oscillator. The movements are driven by massive fluxes of K⁺, Cl^?, and H⁺ through pulvinar motor cell membranes. Light and the oscillator affect leaflet movements by altering the activity of ion transport systems. Some effects of light on ion transport may be mediated by the phosphatidylinositol (PI) cycle, since brief irradiation of the pulvinus with white light accelerates PI turnover.     

Coordinating Anions “to the Rescue” of the Lithium Ion Mobility in Ternary Solid Polymer Electrolytes Plasticized With Ionic Liquids

Lithium salts with low coordinating anions such as bis(trifluoromethanesulfonyl)imide (TFSI) have been the state-of-the-art for polyethylene oxide (PEO)-based “dry” polymer electrolytes for 3 decades. Plasticizing PEO with TFSI-based ionic liquids (ILs) to form ternary solid polymer electrolytes (TSPEs) increases conductivity and Li⁺ diffusivity. However, the Li⁺ transport mechanism is unaffected compared to their “dry” counterparts and is essentially coupled to the dynamics of the polymer host matrix, which limits Li⁺ transport improvement. Thus, a paradigm shift is hereby suggested: the utilization of more coordinating anions such as trifluoromethanesulfonyl-N-cyanoamide (TFSAM), able to compete with PEO for Li⁺ solvation, to accelerate the Li⁺ transport and reach a higher Li⁺ transference number. The Li–TFSAM interaction in binary and ternary TFSAM-based electrolytes is probed by experimental methods and discussed in the context of recent computational results. In PEO-based TSPEs, TFSAM drastically accelerates the Li⁺ transport (increases Li⁺ transference number by a factor 6 and the Li⁺ conductivity by 2–3) and computer simulations reveal that lithium dynamics are effectively re-coupled from polymer to anion dynamics. Last, this concept of coordinating anions in TSPEs is successfully applied in LFP||Li metal cells leading to enhanced capacity retention (86% after 300 cycles) and an improved rate performance at 2C.     

Breakdown of phosphatidylinositol in soybean callus

We have investigated the breakdown of membrane-bound phosphatidylinositol (PI) in homogenates of soybean (Glycine max) callus. The breakdown of PI was stimulated by the detergent deoxycholate. At pH 7.0 and 1·gl^-1 of deoxycholate the loss of PI was rapid and extensive: more than 80% was broken down within 10 min. The breakdown of PI was also stimulated by millimolar concentrations of Ca²⁺. The products of breakdown of added PI (purified from soybean callus) in this system were identified from their chromatographic mobilities as 1,2-diacylglycerol, myo-inositol 1-phosphate and myo-inositol 1:2-cyclic monophosphate.Abbreviations DOC deoxycholate - EDTA ethylenedi-aminetetraacetic acid,-acetate - Pi Inorganic phosphate - PI phosphatidylinositol - PS phosphatidylserine - TLC thinlayer chromatography