Unruh effect as a result of quantization of spacetime

A way to encode acceleration directly into fields has recently being proposed, thus establishing a new kind of fields, the accelerated fields. The definition of accelerated fields points to the quantization of space and time, analogously to the way quantities like energy and momentum are quantized in usual quantum field theories. Unruh effect has been studied in connection with quantum field theory in curved spacetime and it is described by recruiting a uniformly accelerated observer. In this work, as a first attempt to demonstrate the utility of accelerated fields, we present an alternative way to derive Unruh effect. We show, by studying quantum field theory on quantum spacetime, that Unruh effect can be obtained without changing the reference frame. Thus, in the framework of accelerated fields, the observational confirmation of Unruh effect could be assigned to the existence of quantum properties of spacetime.Comment: Comments are welcom

Spin and localization of relativistic fermions and uncertainty relations

We discuss relations between several relativistic spin observables and derive a Lorentz-invariant characteristic of a reduced spin density matrix.A relativistic position operator that satisfies all the properties of its nonrelativistic analog does not exist. Instead we propose two causality-preserving positive operator-valued measures (POVMs) that are based on projections onto one-particle and antiparticle spaces, and on the normalized energy density. They predict identical expectation values for position. The variances differ by less than a quarter of the squared de Broglie wavelength and coincide in the nonrelativistic limit. Since the resulting statistical moment operators are not canonical conjugates of momentum, the Heisenberg uncertainty relations need not hold. Indeed, the energy density POVM leads to a lower uncertainty. We reformulate the standard equations of the spin dynamics by explicitly considering the charge-independent acceleration, allowing a consistent treatment of backreaction and inclusion of a weak gravitational field.Comment: Final version. The presentation is streamlined. Thanks to the referees it can now be also used as a brief revie

Differential alphav integrin-mediated Ras-ERK signaling during two pathways of angiogenesis.

Antagonists of alphavbeta3 and alphavbeta5 disrupt angiogenesis in response to bFGF and VEGF, respectively. Here, we show that these alphav integrins differentially contribute to sustained Ras-extracellular signal-related kinase (Ras-ERK) signaling in blood vessels, a requirement for endothelial cell survival and angiogenesis. Inhibition of FAK or alphavbeta5 disrupted VEGF-mediated Ras and c-Raf activity on the chick chorioallantoic membrane, whereas blockade of FAK or integrin alphavbeta3 had no effect on bFGF-mediated Ras activity, but did suppress c-Raf activation. Furthermore, retroviral delivery of active Ras or c-Raf promoted ERK activity and angiogenesis, which anti-alphavbeta5 blocked upstream of Ras, whereas anti-alphavbeta3 blocked downstream of Ras, but upstream of c-Raf. The activation of c-Raf by bFGF/alphavbeta3 not only depended on FAK, but also required p21-activated kinase-dependent phosphorylation of serine 338 on c-Raf, whereas VEGF-mediated c-Raf phosphorylation/activation depended on Src, but not Pak. Thus, integrins alphavbeta3 and alphavbeta5 differentially regulate the Ras-ERK pathway, accounting for distinct vascular responses during two pathways of angiogenesis

Spatial restriction of alpha4 integrin phosphorylation regulates lamellipodial stability and alpha4beta1-dependent cell migration.

Integrins coordinate spatial signaling events essential for cell polarity and directed migration. Such signals from alpha4 integrins regulate cell migration in development and in leukocyte trafficking. Here, we report that efficient alpha4-mediated migration requires spatial control of alpha4 phosphorylation by protein kinase A, and hence localized inhibition of binding of the signaling adaptor, paxillin, to the integrin. In migrating cells, phosphorylated alpha4 accumulated along the leading edge. Blocking alpha4 phosphorylation by mutagenesis or by inhibition of protein kinase A drastically reduced alpha4-dependent migration and lamellipodial stability. alpha4 phosphorylation blocks paxillin binding in vitro; we now find that paxillin and phospho-alpha4 were in distinct clusters at the leading edge of migrating cells, whereas unphosphorylated alpha4 and paxillin colocalized along the lateral edges of those cells. Furthermore, enforced paxillin association with alpha4 inhibits migration and reduced lamellipodial stability. These results show that topographically specific integrin phosphorylation can control cell migration and polarization by spatial segregation of adaptor protein binding

PTP4A1 promotes TGFβ signaling and fibrosis in systemic sclerosis.

Systemic sclerosis (SSc) is an autoimmune disease characterized by fibrosis of skin and internal organs. Protein tyrosine phosphatases have received little attention in the study of SSc or fibrosis. Here, we show that the tyrosine phosphatase PTP4A1 is highly expressed in fibroblasts from patients with SSc. PTP4A1 and its close homolog PTP4A2 are critical promoters of TGFβ signaling in primary dermal fibroblasts and of bleomycin-induced fibrosis in vivo. PTP4A1 promotes TGFβ signaling in human fibroblasts through enhancement of ERK activity, which stimulates SMAD3 expression and nuclear translocation. Upstream from ERK, we show that PTP4A1 directly interacts with SRC and inhibits SRC basal activation independently of its phosphatase activity. Unexpectedly, PTP4A2 minimally interacts with SRC and does not promote the SRC-ERK-SMAD3 pathway. Thus, in addition to defining PTP4A1 as a molecule of interest for TGFβ-dependent fibrosis, our study provides information regarding the functional specificity of different members of the PTP4A subclass of phosphatases