Consensus under Misaligned Orientations

This paper presents a consensus algorithm under misaligned orientations, which is defined as (i) misalignment to global coordinate frame of local coordinate frames, (ii) biases in control direction or sensing direction, or (iii) misaligned virtual global coordinate frames. After providing a mathematical formulation, we provide some sufficient conditions for consensus or for divergence. Besides the stability analysis, we also conduct some analysis for convergence characteristics in terms of locations of eigenvalues. Through a number of numerical simulations, we would attempt to understand the behaviors of misaligned consensus dynamics.Comment: 23 pages, 9 figure

New Morphologies and Phase Transitions of Rod–Coil Dendritic–Linear Block Copolymers Depending on Dendron Generation and Preparation Procedure

Amphiphilic rod–coil dendritic–linear block copolymers PEG­(G_<i>m</i>)-<i>b</i>-PMPCS (where <i>m</i> is the number of dendron generation, and <i>m</i> = 1, 2, 3) composed of a semirigid Percec-type dendron with hydrophilic poly­(ethylene glycol) (PEG) tails and a rod-like mesogen-jacketed liquid crystalline polymer, poly­{2,5-bis­[(4′-methoxy-phenyl)­oxycarbonyl]­styrene} (PMPCS), were successfully prepared. The self-assembled structures undergo a transition from vesicles through large compound vesicles (LCVs) to short cylindrical micelles with increasing dendron generation. PEG­(G₂)-<i>b</i>-PMPCS forms stable LCVs with porous surfaces of a narrow size distribution in a mixed solvent of tetrahydrofuran and water. The formation mechanism of the supramolecular structure with nano- and microsized scales is studied through changing the rate of water addition. It is composed of two steps: morphological transformation and vesicles fusion or differentiation. Vesicles are precursors for LCVs regardless of what the initial morphology is. However, the final LCV structures are different. Slow addition of water produces spherical LCVs, while those formed during fast water addition are irregular (like deformed spherical) LCVs

Src/β-arrestin2 signal complex was required for mechanical stretch-mediated AT1-R signaling.

<p>(<b>A</b>) Western blotting analyses of time-dependent Src phosphorylation after treatment with β-arrestin1/2 siRNA or scrambled siRNA. (<b>B</b>) Coimmunoprecipitation analyses of Src and AT1-R in lysates of stretched cardiomyocytes in a time-dependent manner. (<b>C</b>) HA-tagged Src and FLAG-tagged β-arrestin2 (or dominant negative β-arrestin2-V54D) were transient transfected into HEK-293-AT1 cells, whole cell extracts were immunoprecipitated with anti-FLAG monoclonal antibody, and the proteins in the immunoprecipitates and in the total lysates were probed by Western blotting using an anti-HA antibody. (<b>D</b>) The intercellular location of Src kinase in GFP-tagged β-arrestin2 WT and dominant negative GFP-tagged β-arrestin2-V54D transfected HEK-293-AT1 cells was visualized by immunofluorescence after stretching cells for 10 min. (<b>E</b>) The effect of β-arrestin2 WT or β-arrestin2-V54D transfection on mechanical stretch-induced ERK1/2 phosphorylation. (<b>F</b>) The effect of SU6656 (5 mmol/L) on ERK1/2 phosphorylation in cardiomyocytes stimulated by mechanical stretch or AngII (10⁻⁷ mol/L). * <i>P</i><0.05 vs. both AngII and SU6656 treated groups; # <i>P</i><0.05 vs. stretched groups (n = 3 separated experiments).</p

The effects of different ARBs on the cardiac function and Src expression in AGT KO mice.

<p>AGT KO mice were induced by AngII or TAC for 2 weeks with or without the pretreatment of valsartan or candesartan. (<b>A</b>) Representative M-mode tracings of AGT KO hearts stimulated by AngII (10⁻⁵ mol/L, top line) or by TAC for 2 weeks (bottom line). (<b>B</b>) Representative recording of LVAWd, LVPWd and LVEF in AGT KO mice from each group. (<b>C</b>) The expression of Src in myocardium of AGT KO mice from each group was determined. Data were presented as mean ± s.e.m. from five to eight mice. * <i>P</i><0.05 vs. AngII-treated AGT KO mice; # <i>P</i><0.05 vs. TAC-treated AGT KO mice.</p

In vivo analyses of the cardiac function by echocardiography and hemodynamic measurements.

<p>Both AGT KO mice and the C57BL/6 WT littermates were pretreated with or without Src kinase inhibitor (SU6656), followed by TAC for 2 weeks. (<b>A</b>) Quantifications of LVAWd, LVPWd, LVEF and LVESP by representative M-mode tracing and hemodynamic recording from five mice. (<b>B</b>) Quantifications of cardiac immediate-early response genes in C57BL/6 mice and AGT KO mice with or without pretreatment of SU6656 (n = 5 separated experiments). * <i>P</i><0.05 vs. saline-treated TAC-operated AGT KO mice.</p

Mechanical stretch preferentially activated a heterotrimeric G protein-independent AT1 signaling pathway.

<p>(<b>A</b>) In vitro cultured cardiomyocytes were seeded on 24 well plates (1.5×10⁵ cells) and labeled by myo-[³H] inositol (1.0 µCi/mL) at 37°C for 24 h. Inositol phosphates (IPx) release was determined at the different indicated time points triggered by AngII (10⁻⁷ mol/L) or stretch respectively, and including the treatment of candesartan. (<b>B</b>) The effect of GF109203X on ERK1/2 phosphorylation stimulated by stretch or AngII (10⁻⁷ mol/L). (<b>C</b>) The endogenous mRNA and protein levels of β-arrestin1 and β-arrestin2 in cardiomyocytes were determined before and after stretch for 10 min. (<b>D</b>) Time-dependent ERK1/2 phosphorylation was determined after treatment with β-arrestin1/2 siRNA or scrambled siRNA. (<b>E</b>) Mechanical stretch-induced expression of phosphorylated ERK1/2 was determined in a single plasmid (β-arrestin1 or β-arrestin2) transfected HEK-293-AT1 cells after knock-down of endogenous β-arrestin1/2. * <i>P</i><0.05 vs. AngII-induced group (n = 3 separated experiments).</p

Additional file 4: Figure S2. of Identification of QTL with large effect on seed weight in a selective population of soybean with genome-wide association and fixation index analyses

Extent of linkage disequilibrium (LD) in euchromatic (black) and heterochromatic (gray) regions of the 20 soybean chromosomes. (PDF 219 kb

Schema for the mechanism of cardiac hypertrophy via AT1-R-dependent signaling pathway induced by AngII or mediated by mechanical stretch, respectively.

<p>Schema for the mechanism of cardiac hypertrophy via AT1-R-dependent signaling pathway induced by AngII or mediated by mechanical stretch, respectively.</p

Mechanical stretch induced ERK1/2 signaling via activation of AT1-R, but not affected by G protein inhibition.

<p>(<b>A</b>) In vitro cultured cardiomyocytes were transfected with or without RGS4 plasmid, and then stimulated by stretch or AngII (10⁻⁷ mol/L) for 10 min, total proteins were collected and the expressions of phosphorylated ERK1/2 and total ERK1/2 were determined by Western blotting. (<b>B</b>) HA-tagged ERK2 was co-transfected with RGS4 plasmid into HEK-293 AT1 expressed cells for 24 h, ERK2 activity (indicated by MBP expression) was detected in cells induced by stretch or AngII, respectively. (<b>C</b>) Cardiomyocytes were pretreated with candesartan (10⁻⁶ mol/L) and then induced by stretch or AngII for 10 min, the expressions of phosphorylated ERK1/2 and total ERK1/2 were determined. * <i>P</i><0.05 vs. stretch-induced group (n = 3 separated experiments).</p