Effects of High-Volume Versus High-Load Resistance Training on Skeletal Muscle Growth and Molecular Adaptations

We evaluated the effects of higher-load (HL) versus (lower-load) higher-volume (HV) resistance training on skeletal muscle hypertrophy, strength, and muscle-level molecular adaptations. Trained men (n = 15, age: 23 ± 3 years; training experience: 7 ± 3 years) performed unilateral lower-body training for 6 weeks (3× weekly), where single legs were randomly assigned to HV and HL paradigms. Vastus lateralis (VL) biopsies were obtained prior to study initiation (PRE) as well as 3 days (POST) and 10 days following the last training bout (POSTPR). Body composition and strength tests were performed at each testing session, and biochemical assays were performed on muscle tissue after study completion. Two-way within-subject repeated measures ANOVAs were performed on most dependent variables, and tracer data were compared using dependent samples t-tests. A significant interaction existed for VL muscle cross-sectional area (assessed via magnetic resonance imaging; interaction p = 0.046), where HV increased this metric from PRE to POST (+3.2%, p = 0.018) whereas HL training did not (−0.1%, p = 0.475). Additionally, HL increased leg extensor strength more so than HV training (interaction p = 0.032; HV \u3c HL at POST and POSTPR, p \u3c 0.025 for each). Six-week integrated non-myofibrillar protein synthesis (iNon-MyoPS) rates were also higher in the HV versus HL condition, while no difference between conditions existed for iMyoPS rates. No interactions existed for other strength, VL morphology variables, or the relative abundances of major muscle proteins. Compared to HL training, 6 weeks of HV training in previously trained men optimizes VL hypertrophy in lieu of enhanced iNon-MyoPS rates, and this warrants future research

Characterization of cytochrome bo(3) activity in a native-like surface-tethered membrane

We have developed a simple native-like surface-tethered membrane system to investigate the activity of cbo3 (cytochrome bo3), a terminal oxidase in Escherichia coli. The tethered membranes consist of E. coli inner-membrane extracts mixed with additional E. coli lipids containing various amounts of the cbo3 substrate UQ-10 (ubiquinol-10). Tethered membranes are formed by self-assembly from vesicles on to gold electrodes functionalized with cholesterol derivatives. cbo3 activity was monitored using CV (cyclic voltammetry) with electron transfer to cbo3 mediated by UQ-10. The apparent Km for oxygen with this system is 1.1±0.4 μM, in good agreement with values reported in the literature for whole-cell experiments and for purified cbo3. Increasing the concentration of lipophilic UQ-10 in the membrane leads to an increase in cbo3 activity. The activity of cbo3 with long-chain ubiquinones appears to be different from previous reports using short-chain substrate analogues such as UQ-1 in that typical Michaelis–Menten kinetics are not observed using UQ-10. This native-like membrane model thus provides new insights into the interaction of transmembrane enzymes with hydrophobic substrates which contrasts with studies using hydrophilic UQ analogues

Design of Drip Irrigation Lines

This report presents a simple way of estimating friction drop along the lateral line, pressure distribution along the drip line, and variation of emitter discharge along the lateral. Design charts are presented for determining pressure and length of the lateral lines and submains of a drip irrigation system

Identification of a Novel T-Cell Epitope in Soluble Egg Antigen of Schistosoma japonicum

Identification of T-cell epitopes harbored in soluble egg antigen (SEA) of Schistosoma japonicum and study of the immunological properties are essential for understanding the immunopathology and the control of schistosomiasis. As a follow-up to our previous work, the 66- to 80-kDa fragment from SEA was partially digested with protease, fractionated by reverse-phase high-pressure liquid chromatography, and found to be carrying a peptide which stimulated proliferation and gamma interferon (IFN-γ) production of Th1 clones specific to SEA. Sequence analysis showed that the peptide was composed of 12 amino acids lined up as DLAVELAYLGNL. A synthetic homologue induced proliferation and IFN-γ and interleukin-2 (IL-2) production, but not IL-4 or IL-6 production, by the Th1 clones as well as by the spleen cells from SEA-immunized mice, thus indicating that the peptide carries a Th1 epitope of SEA