Unraveling the role of internal-external metal substitution in Zn3[Co(CN6)]2 for the styrene oxide-CO2 cycloaddition reaction.

We investigated the influence of the structural and textural properties along with the chemical environment of pure Zn3[Co(CN)6]2 in comparison with the modified phases on the catalytic performance in the cycloaddition reaction between styrene oxide and CO2. We relate these to the proposed reaction pathways and mechanisms. The natural cubic phase (ZnCoCn) was dehydrated to obtain the rhombohedral phase (ZnCoRn), while the stabilized cubic phase (ZnCoCs) was synthesized by substituting external zinc atoms with cadmium atoms. The rhombohedral stabilized phase (ZnCoRs) was achieved by the internal cobalt change with iron. All the materials were extensively characterized using X-ray diffraction (XRD), thermogravimetric analysis (TGA), differential scanning calorimetry (DSC), X-ray photoelectron spectroscopy (XPS), and N2 adsorption. The catalytic behavior of the four phases was tested. The crystalline structure of each phase was obtained, and by XPS, it was demonstrated that the chemical environments of all elements conforming to the rhombohedral stabilized phase are different from those of all other materials owing to the exchange of internal metals. The bulk textural properties were similar; only the ZnCoRs presented more micropore area but did not exceed the total surface area of the other materials. The product distribution and yield at reaction times of 2 h and 6 h were closer to those of the cubic phases. The natural rhombohedral phase exhibits the best performance. The tetrabutylammonium bromide (TBAB) and rhombohedral stabilized phase work together to yield a bigger copolymer quantity at the expense of the styrene carbonate (StCO3) production. From the proposed mechanism, the TBAB cation (TBA+) has a "protection" function that drives the closing of the StCO3 ring; however, the charge distribution anisotropy in the four nitrogen atoms generated by Co replacement in ZnCoRs could hold TBA+ as the reaction time progressed, causing an unavailability that triggered the copolymerization propagation step.

Cholesterol depletion uncouples ß-dystroglycans from discrete sarcolemmal domains, reducing the mechanical activity of skeletal muscle.

BACKGROUND/AIMS: ß-Dystroglycan (ß-DG) is a transmembrane glycoprotein that links the intracellular cytoskeleton to the extracellular matrix and is crucial for the molecular pathway of lateral force transmission in muscle. We aimed to investigate the effect of decreasing sarcolemmal cholesterol on the distribution of ß-DG, its interaction with dystrophin and the impact on the contraction efficiency of muscle. METHODS: Isolated rat extensor digitorum longus muscles were incubated with methyl ß-cyclodextrin (MßCD) to deplete cholesterol and with MßCD-cholesterol to restore cholesterol. Electric stimulation protocols were used to determine muscle force and fatigue. Detergent-resistant membranes (lipid rafts) were separated from isolated skeletal muscle sarcolemma. The distribution and interactions of ß-DG, caveolin-3 and dystrophin were determined by an immunoreactivity analysis. RESULTS: Cholesterol depletion in muscle results in a weakened force of contraction, which recovers after cholesterol restoration. The rate of fatigue is unaffected, but fatigue recovery is dependent upon cholesterol restoration. MßCD modifies the structures of lipid rafts obtained from MßCD-treated muscles by, displacing the membrane proteins ß-DG and caveolin-3 f from the lipid raft, thus reducing the interaction of ß-DG with dystrophin. CONCLUSION: Cholesterol depletion weakens the muscle contractile force by disturbing the sarcolemmal distribution of ß-dystroglycan and its interaction with dystrophin, two key proteins in the alignment of lateral force transmission pathway.

Altered calcium pump and secondary deficiency of gamma-sarcoglycan and microspan in sarcoplasmic reticulum membranes isolated from delta-sarcoglycan knockout mice.

Sarcoglycans (SGs) and sarcospan (SSPN) are transmembrane proteins of the dystrophin-glycoprotein complex. Mutations in the genes encoding SGs cause many inherited forms of muscular dystrophy. In this study, using purified membranes of wild-type (WT) and delta-SG knockout (KO) mice, we found the specific localization of the SG-SSPN isoforms in transverse tubules (TT) and sarcoplasmic reticulum (SR) membranes. Immunoblotting revealed that the absence of delta-SG isoforms in TT and SR results in a secondary deficiency of gamma-SG and microSPN. Our results showed augmented ATP hydrolytic activity, ATP-dependent calcium uptake and passive calcium efflux, probably through SERCA1 in KO compared to WT mice. Furthermore, we found a conformational change in SERCA1 isolated from KO muscle as demonstrated by calorimetric analysis. Following these alterations with mechanical properties, we found an increase in force in KO muscle with the same rate of fatigue but with a decreased fatigue recovery compared to WT. Together our observations suggest, for the first time, that the delta-SG isoforms may stabilize the expression of gamma-SG and microSPN in the TT and SR membranes and that this possible complex may play a role in the maintenance of a stable level of resting cytosolic calcium concentration in skeletal muscle.