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Hermitian Dirac Hamiltonian in time dependent gravitational field
It is shown by a straightforward argument that the Hamiltonian generating the
time evolution of the Dirac wave function in relativistic quantum mechanics is
not hermitian with respect to the covariantly defined inner product whenever
the background metric is time dependent. An alternative, hermitian, Hamiltonian
is found and is shown to be directly related to the canonical field Hamiltonian
used in quantum field theory.Comment: 9 pages, final version, to appear in Class. Quant. Gra
Canonical and gravitational stress-energy tensors
It is dealt with the question, under which circumstances the canonical
Noether stress-energy tensor is equivalent to the gravitational (Hilbert)
tensor for general matter fields under the influence of gravity. In the
framework of general relativity, the full equivalence is established for matter
fields that do not couple to the metric derivatives. Spinor fields are included
into our analysis by reformulating general relativity in terms of tetrad
fields, and the case of Poincare gauge theory, with an additional, independent
Lorentz connection, is also investigated. Special attention is given to the
flat limit, focusing on the expressions for the matter field energy
(Hamiltonian). The Dirac-Maxwell system is investigated in detail, with special
care given to the separation of free (kinetic) and interaction (or potential)
energy. Moreover, the stress-energy tensor of the gravitational field itself is
briefly discussed.Comment: final version, to appear in Int. J. Mod. Phys.
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Online fabrication and characterization of capsule populations with a flow-focusing microfluidic system
This paper was presented at the 3rd Micro and Nano Flows Conference (MNF2011), which was held at the Makedonia Palace Hotel, Thessaloniki in Greece. The conference was organised by Brunel University and supported by the Italian Union of Thermofluiddynamics, Aristotle University of Thessaloniki, University of Thessaly, IPEM, the Process Intensification Network, the Institution of Mechanical Engineers, the Heat Transfer Society, HEXAG - the Heat Exchange Action Group, and the Energy Institute.We have designed a microfluidic system that combines a double flow-focusing setup for calibrated capsule fabrication with a microchannel for the characterization of their mechanical properties. The double flow-focusing system consists of a first Y junction to create the microdroplets and of a second Y junction to introduce the cross-linking agent allowing the membrane formation. The human serum albumin (HSA) aqueous solution for the dispersed solution, hydrophobic phase for the continuous solution and cross-linking agent solution are introduced by means of syringe pumps. A wavy channel after the second junction allows to control the reticulation time. A cylindrical microchannel then enables to deform and characterize the capsules formed. The mechanical properties of the capsule membrane are obtained by inverse analysis (Chu et al. 2011). The results show that the drop size increases with the flow rate ratio between the central and lateral channels and does not change much regardless of the flow rate of the reticulation phase. The mean shear modulus of the capsules fabricated after 23 s of reticulation is of the order of the surface tension of HSA solution with Dragoxat indicating that the reticulation time is too short to form an elastic membrane around the droplet. When the reticulation time is increased to 60 s, the membrane shear modulus is multiplied by a factor of 3 confirming that a solid membrane has formed around the drop
Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1: a nuclear target protein of PARP-1
<p>Abstract</p> <p>Background</p> <p>Poly(ADP-ribose) polymerase-1 (PARP-1) is a nuclear enzyme that plays critical functions in many biological processes, including DNA repair and gene transcription. The main function of PARP-1 is to catalyze the transfer of ADP-ribose units from nicotinamide adenine dinucleotide (NAD<sup>+</sup>) to a large array of acceptor proteins, which comprises histones, transcription factors, as well as PARP-1 itself. We have previously demonstrated that transcription of the PARP-1 gene essentially rely on the opposite regulatory actions of two distinct transcription factors, Sp1 and NFI. In the present study, we examined whether suppression of PARP-1 expression in embryonic fibroblasts derived from PARP-1 knockout mice (PARP-1<sup>-/-</sup>) might alter the expression and/or DNA binding properties of Sp1 and NFI. We also explored the possibility that Sp1 or NFI (or both) may represent target proteins of PARP-1 activity.</p> <p>Results</p> <p>Expression of both Sp1 and NFI was found to be considerably reduced in PARP-1<sup>-/- </sup>cells. Co-immunoprecipitation assays revealed that PARP-1 physically interacts with Sp1 in a DNA-independent manner, but neither with Sp3 nor NFI, in PARP-1<sup>+/+ </sup>cells. In addition, <it>in vitro </it>PARP assays indicated that PARP-1 could catalyze the addition of polymer of ADP-ribose to Sp1, which also translated into a reduction of Sp1 binding to its consensus DNA target site. Transfection of the PARP-1 promoter into both PARP-1<sup>+/+ </sup>and PARP-1<sup>-/- </sup>cells revealed that the lack of PARP-1 expression in PARP-1<sup>-/- </sup>cells also results in a strong increase in PARP-1 promoter activity. This influence of PARP-1 was found to rely on the presence of the Sp1 sites present on the basal PARP-1 promoter as their mutation entirely abolished the increased promoter activity observed in PARP-1<sup>-/- </sup>cells. Subjecting PARP-1<sup>+/+ </sup>cells to an oxidative challenge with hydrogen peroxide to increase PARP-1 activity translated into a dramatic reduction in the DNA binding properties of Sp1. However, its suppression by the inhibitor PJ34 improved DNA binding of Sp1 and led to a dramatic increase in PARP-1 promoter function.</p> <p>Conclusion</p> <p>Our results therefore recognized Sp1 as a target protein of PARP-1 activity, the addition of polymer of ADP-ribose to this transcription factor restricting its positive regulatory influence on gene transcription.</p
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