239 research outputs found
Private (Transnational) Power without Authority. Online fascist propaganda and political participation in CasaPound v. Facebook
Emission lines of Fe XI in the 257--407 A wavelength region observed in solar spectra from EIS/Hinode and SERTS
Theoretical emission-line ratios involving Fe XI transitions in the 257-407 A
wavelength range are derived using fully relativistic calculations of radiative
rates and electron impact excitation cross sections. These are subsequently
compared with both long wavelength channel Extreme-Ultraviolet Imaging
Spectrometer (EIS) spectra from the Hinode satellite (covering 245-291 A), and
first-order observations (235-449 A) obtained by the Solar Extreme-ultraviolet
Research Telescope and Spectrograph (SERTS). The 266.39, 266.60 and 276.36 A
lines of Fe XI are detected in two EIS spectra, confirming earlier
identifications of these features, and 276.36 A is found to provide an electron
density diagnostic when ratioed against the 257.55 A transition. Agreement
between theory and observation is found to be generally good for the SERTS data
sets, with discrepancies normally being due to known line blends, while the
257.55 A feature is detected for the first time in SERTS spectra. The most
useful Fe XI electron density diagnostic is found to be the 308.54/352.67
intensity ratio, which varies by a factor of 8.4 between N_e = 10^8 and 10^11
cm^-3, while showing little temperature sensitivity. However, the 349.04/352.67
ratio potentially provides a superior diagnostic, as it involves lines which
are closer in wavelength, and varies by a factor of 14.7 between N_e = 10^8 and
10^11 cm^-3. Unfortunately, the 349.04 A line is relatively weak, and also
blended with the second-order Fe X 174.52 A feature, unless the first-order
instrument response is enhanced.Comment: 9 pages, 5 figures, 13 tables; MNRAS in pres
EUV Spectra of the Full Solar Disk: Analysis and Results of the Cosmic Hot Interstellar Plasma Spectrometer (CHIPS)
We analyze EUV spectra of the full solar disk from the Cosmic Hot
Interstellar Plasma Spectrometer (CHIPS) spanning a period of two years. The
observations were obtained via a fortuitous off-axis light path in the 140 --
270 Angstrom passband. The general appearance of the spectra remained
relatively stable over the two-year time period, but did show significant
variations of up to 25% between two sets of Fe lines that show peak emission at
1 MK and 2 MK. The variations occur at a measured period of 27.2 days and are
caused by regions of hotter and cooler plasma rotating into, and out of, the
field of view. The CHIANTI spectral code is employed to determine plasma
temperatures, densities, and emission measures. A set of five isothermal
plasmas fit the full disk spectra well. A 1 -- 2 MK plasma of Fe contributes
85% of the total emission in the CHIPS passband. The standard Differential
Emission Measures (DEMs) supplied with the CHIANTI package do not fit the CHIPS
spectra well as they over-predict emission at temperatures below log(T) = 6.0
and above log(T) = 6.3. The results are important for cross-calibrating TIMED,
SORCE, SOHO/EIT, and CDS/GIS, as well as the recently launched Solar Dynamics
Observatory.Comment: 27 Pages, 13 Figure
Overexpression of catalase diminishes oxidative cysteine modifications of cardiac proteins
Reactive protein cysteine thiolates are instrumental in redox regulation. Oxidants, such as hydrogen peroxide (H2O2), react with thiolates to form oxidative post-translational modifications, enabling physiological redox signaling. Cardiac disease and aging are associated with oxidative stress which can impair redox signaling by altering essential cysteine thiolates. We previously found that cardiac-specific overexpression of catalase (Cat), an enzyme that detoxifies excess H2O2, protected from oxidative stress and delayed cardiac aging in mice. Using redox proteomics and systems biology, we sought to identify the cysteines that could play a key role in cardiac disease and aging. With a 'Tandem Mass Tag' (TMT) labeling strategy and mass spectrometry, we investigated differential reversible cysteine oxidation in the cardiac proteome of wild type and Cat transgenic (Tg) mice. Reversible cysteine oxidation was measured as thiol occupancy, the ratio of total available versus reversibly oxidized cysteine thiols. Catalase overexpression globally decreased thiol occupancy by ≥1.3 fold in 82 proteins, including numerous mitochondrial and contractile proteins. Systems biology analysis assigned the majority of proteins with differentially modified thiols in Cat Tg mice to pathways of aging and cardiac disease, including cellular stress response, proteostasis, and apoptosis. In addition, Cat Tg mice exhibited diminished protein glutathione adducts and decreased H2O2 production from mitochondrial complex I and II, suggesting improved function of cardiac mitochondria. In conclusion, our data suggest that catalase may alleviate cardiac disease and aging by moderating global protein cysteine thiol oxidation.Chunxiang Yao, Jessica B. Behring, Di Shao, Aaron L. Sverdlov, Stephen A. Whelan, Aly Elezaby, Xiaoyan Yin, Deborah A. Siwik, Francesca Seta, Catherine E. Costello, Richard A. Cohen, Reiko Matsui, Wilson S. Colucci, Mark E. McComb, Markus M. Bachschmi
High fat, high sucrose diet causes cardiac mitochondrial dysfunction due in part to oxidative post-translational modification of mitochondrial complex II
Abstract not availableAaron L. Sverdlov, Aly Elezaby, Jessica B. Behring, Markus M. Bachschmid, Ivan Luptak, Vivian H. Tu, Deborah A. Siwik, Edward J. Miller, Marc Liesa, Orian S. Shirihai, David R. Pimentel, Richard A. Cohen, Wilson S. Colucc
Mitochondrial reactive oxygen species mediate cardiac structural, functional, and mitochondrial consequences of diet-induced metabolic heart disease
Mitochondrial reactive oxygen species (ROS) are associated with metabolic heart disease (MHD). However, the mechanism by which ROS cause MHD is unknown. We tested the hypothesis that mitochondrial ROS are a key mediator of MHD.Mice fed a high-fat high-sucrose (HFHS) diet develop MHD with cardiac diastolic and mitochondrial dysfunction that is associated with oxidative posttranslational modifications of cardiac mitochondrial proteins. Transgenic mice that express catalase in mitochondria and wild-type mice were fed an HFHS or control diet for 4 months. Cardiac mitochondria from HFHS-fed wild-type mice had a 3-fold greater rate of H2O2 production (P=0.001 versus control diet fed), a 30% decrease in complex II substrate-driven oxygen consumption (P=0.006), 21% to 23% decreases in complex I and II substrate-driven ATP synthesis (P=0.01), and a 62% decrease in complex II activity (P=0.002). In transgenic mice that express catalase in mitochondria, all HFHS diet-induced mitochondrial abnormalities were ameliorated, as were left ventricular hypertrophy and diastolic dysfunction. In HFHS-fed wild-type mice complex II substrate-driven ATP synthesis and activity were restored ex vivo by dithiothreitol (5 mmol/L), suggesting a role for reversible cysteine oxidative posttranslational modifications. In vitro site-directed mutation of complex II subunit B Cys100 or Cys103 to redox-insensitive serines prevented complex II dysfunction induced by ROS or high glucose/high palmitate in the medium.Mitochondrial ROS are pathogenic in MHD and contribute to mitochondrial dysfunction, at least in part, by causing oxidative posttranslational modifications of complex I and II proteins including reversible oxidative posttranslational modifications of complex II subunit B Cys100 and Cys103.Aaron L. Sverdlov, Aly Elezaby, Fuzhong Qin, Jessica B. Behring, Ivan Luptak, Timothy D. Calamaras, Deborah A. Siwik, Edward J. Miller, Marc Liesa, Orian S. Shirihai, David R. Pimentel, Richard A. Cohen, Markus M. Bachschmid, Wilson S. Colucc
Relações contratuais e perfil dos cirurgiões-dentistas em centros de especialidades odontológicas de baixo e alto desempenho no Brasil
A Cellular Potts Model simulating cell migration on and in matrix environments
Cell migration on and through extracellular matrix plays a critical role in a wide variety of physiological and pathological phenomena, and in scaffold-based tissue engineering. Migration is regulated by a number of extracellular matrix- or cell-derived biophysical parameters, such as matrix fiber orientation, gap size, and elasticity, or cell deformation, proteolysis, and adhesion. We here present an extended Cellular Potts Model (CPM) able to qualitatively and quantitatively describe cell migratory phenotype on both two-dimensional substrates and within three-dimensional environments, in a close comparison with experimental evidence. As distinct features of our approach, the cells are represented by compartmentalized discrete objects, differentiated in the nucleus and in the cytosolic region, while the extracellular matrix is composed of a fibrous mesh and of a homogeneous fluid. Our model provides a strong correlation of the directionality of migration with the topological ECM distribution and, further, a biphasic dependence of migration on the matrix density, and in part adhesion, in both two-dimensional and three-dimensional settings. Moreover, we demonstrate that the directional component of cell movement is strongly correlated with the topological distribution of the ECM fibrous network. In the three-dimensional networks, we also investigate the effects of the matrix mechanical microstructure, observing that, at a given distribution of fibers, cell motility has a subtle bimodal relation with the elasticity of the scaffold. Finally, cell locomotion requires deformation of the cell's nucleus and/or cell-derived proteolysis of steric fibrillar obstacles within rather rigid matrices characterized by small pores, not, however, for sufficiently large pores. In conclusion, we here propose a mathematical modeling approach that serves to characterize cell migration as a biological phenomen in health, disease and tissue engineering applications. The research that led to the present paper was partially supported by a grant of the group GNFM of INdA
Subcutaneous immunoglobulin replacement therapy with Hizentra®, the first 20% SCIG preparation: a Practical approach
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