Novel features of the energy momentum tensor of a Casimir apparatus in a weak gravitational field

The influence of the gravity acceleration on the regularized energy-momentum tensor of the quantized electromagnetic field between two plane parallel conducting plates is derived. A perturbative expansion, to first order in the constant acceleration parameter, of the Green functions involved and of the energy-momentum tensor is derived by means of the covariant geodesic point splitting procedure. The energy-momentum tensor is covariantly conserved and satisfies the expected relation between gauge-breaking and ghost parts.Comment: 8 pages, based on a talk given by Luigi Rosa at the QFEXT07 Conference, Leipzig. Equation (13) and the formulae for rho and energy E stored in the Casimir device have been amended, jointly with related discussio

Energy-momentum tensor for a scalar Casimir apparatus in a weak gravitational field: Neumann conditions

We consider a Casimir apparatus consisting of two perfectly conducting parallel plates, subject to the weak gravitational field of the Earth. The aim of this paper is the calculation of the energy-momentum tensor of this system for a free, real massless scalar field satisfying Neumann boundary conditions on the plates. The small gravity acceleration (here considered as not varying between the two plates) allows us to perform all calculations to first order in this parameter. Some interesting results are found: a correction, depending on the gravity acceleration, to the well-known Casimir energy and pressure on the plates. Moreover, this scheme predicts a tiny force in the upwards direction acting on the apparatus. These results are supported by two consistency checks: the covariant conservation of the energy-momentum tensor and the vanishing of its regularized trace, when the scalar field is conformally coupled to gravity.Comment: 5 pages in double-column format, Revtex4. The final version is shorter, and the presentation has been improve

Restoration of CFTR function in patients with cystic fibrosis carrying the F508del-CFTR mutation

<div><p>Restoration of BECN1/Beclin 1-dependent autophagy and depletion of SQSTM1/p62 by genetic manipulation or autophagy-stimulatory proteostasis regulators, such as cystamine, have positive effects on mouse models of human cystic fibrosis (CF). These measures rescue the functional expression of the most frequent pathogenic CFTR mutant, F508del, at the respiratory epithelial surface and reduce lung inflammation in <i>Cftr^F508del</i> homozygous mice. Cysteamine, the reduced form of cystamine, is an FDA-approved drug. Here, we report that oral treatment with cysteamine greatly reduces the mortality rate and improves the phenotype of newborn mice bearing the <i>F508del-CFTR</i> mutation. Cysteamine was also able to increase the plasma membrane expression of the F508del-CFTR protein in nasal epithelial cells from <i>F508del</i> homozygous CF patients, and these effects persisted for 24 h after cysteamine withdrawal. Importantly, this cysteamine effect after washout was further sustained by the sequential administration of epigallocatechin gallate (EGCG), a green tea flavonoid, both <i>in vivo</i>, in mice, and <i>in vitro</i>, in primary epithelial cells from CF patients. In a pilot clinical trial involving 10 <i>F508del-CFTR</i> homozygous CF patients, the combination of cysteamine and EGCG restored BECN1, reduced SQSTM1 levels and improved CFTR function from nasal epithelial cells <i>in vivo</i>, correlating with a decrease of chloride concentrations in sweat, as well as with a reduction of the abundance of <i>TNF/TNF-alpha (tumor necrosis factor)</i> and <i>CXCL8</i> (<i>chemokine [C-X-C motif] ligand 8</i>) transcripts in nasal brushing and TNF and CXCL8 protein levels in the sputum. Altogether, these results suggest that optimal schedules of cysteamine plus EGCG might be used for the treatment of CF caused by the <i>F508del-CFTR</i> mutation.</p></div

SO(10) GUT Models and Cosmology

$SO(10)$ grand unified models have an intermediate symmetry group in between $SO(10)$ and $SU(3)_{C} \otimes SU(2)_{L} \otimes U(1)_{Y}$. Hence they lead to a prediction for proton lifetime in agreement with the experimental lower limit. This paper reviews the recent work on the tree-level potential and the one-loop effective potential for such models, with application to inflationary cosmology. The open problems are the use of the most general form of tree-level potential for $SO(10)$ models in the reheating stage of the early universe, and the analysis of non-local effects in the semiclassical field equations for such models in Friedmann-Robertson-Walker backgrounds.Comment: 7 pages, Latex, talk prepared for the Second International Sakharov Conference on Physics, Moscow (May 1996

Push on a Casimir apparatus in a weak gravitational field

The influence of the gravity acceleration on the regularized energy-momentum tensor of the quantized electromagnetic field between two plane parallel conducting plates is derived. We use Fermi coordinates and work to first order in the constant acceleration parameter. A new simple formula for the trace anomaly is found to first order in the constant acceleration, and a more systematic derivation is therefore obtained of the theoretical prediction according to which the Casimir device in a weak gravitational field will experience a tiny push in the upwards direction.Comment: 14 pages, Plain Tex. Talk given at the 17th SIGRAV Conference on General Relativity and Gravitational Physics, Torino, September 200

Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins

Significant advances in the understanding of the molecular determinants of fibrillogenesis can be expected from comparative studies of the aggregation propensities of proteins with highly homologous structures but different folding pathways. Here, we fully characterize, by means of stopped-flow, T-jump, CD and DSC experiments, the unfolding mechanisms of three highly homologous proteins, zinc binding Ros87 and Ml153-149 and zinc-lacking Ml452-151. The results indicate that the three proteins significantly differ in terms of stability and (un)folding mechanisms. Particularly, Ros87 and Ml153-149 appear to be much more stable to guanidine denaturation and are characterized by folding mechanisms including the presence of an intermediate. On the other hand, metal lacking Ml452-151 folds according to a classic two-state model. Successively, we have monitored the capabilities of Ros87, Ml452-151 and Ml153-149 to form amyloid fibrils under native conditions. Particularly, we show, by CD, fluorescence, DLS, TEM and SEM experiments, that after 168 hours, amyloid formation of Ros87 has started, while Ml153-149 has formed only amorphous aggregates and Ml452-151 is still monomeric in solution. This study shows how metal binding can influence protein folding pathways and thereby control conformational accessibility to aggregation-prone states, which in turn changes aggregation kinetics, shedding light on the role of metal ions in the development of protein deposition diseases