Critical analysis of the manoeuvres proposed for the diagnosis of the tunnel carpal syndrome

Carpal tunnel syndrome (CTS) is the most common entrapment neuropathy. It is mainly due to the compression of median nerve at the wrist and it may be idiopathic or secondary to different rheumatic or non rheumatic diseases, including occupational activities. Since signs and symptoms of CTS are characteristic, a careful examination of the affected patient may be very satisfactory for the diagnosis, in particular by mean of some manoeuvres. In this review we described and commented the tests considered most useful in the diagnosis of CTS. We also analysed the diagnostic values of electromiography, the most important electrodiagnostic study for the CTS

Acknowledgement to reviewers of JSAN in 2016

The editors of JSAN would like to express their sincere gratitude to the following reviewers for assessing manuscripts in 2016.[...

A Soluble Form of the High Affinity IgE Receptor, Fc-Epsilon-RI, Circulates in Human Serum

Soluble IgE receptors are potential in vivo modulators of IgE-mediated immune responses and are thus important for our basic understanding of allergic responses. We here characterize a novel soluble version of the IgE-binding alpha-chain of Fc-epsilon-RI (sFcεRI), the high affinity receptor for IgE. sFcεRI immunoprecipitates as a protein of ∼40 kDa and contains an intact IgE-binding site. In human serum, sFcεRI is found as a soluble free IgE receptor as well as a complex with IgE. Using a newly established ELISA, we show that serum sFcεRI levels correlate with serum IgE in patients with elevated IgE. We also show that serum of individuals with normal IgE levels can be found to contain high levels of sFcεRI. After IgE-antigen-mediated crosslinking of surface FcεRI, we detect sFcεRI in the exosome-depleted, soluble fraction of cell culture supernatants. We further show that sFcεRI can block binding of IgE to FcεRI expressed at the cell surface. In summary, we here describe the alpha-chain of FcεRI as a circulating soluble IgE receptor isoform in human serum

The design of the instrument control unit and its role within the data processing system of the ESA PLATO Mission

PLATO1 is an M-class mission of the European Space Agency's Cosmic Vision program, whose launch is foreseen by 2026. PLAnetary Transits and Oscillations of stars aims to characterize exoplanets and exoplanetary systems by detecting planetary transits and conducting asteroseismology of their parent stars. PLATO is the next generation planetary transit space experiment, as it will fly after CoRoT, Kepler, TESS and CHEOPS; its objective is to characterize exoplanets and their host stars in the solar neighbors. While it is built on the heritage from previous missions, the major breakthrough to be achieved by PLATO will come from its strong focus on bright targets, typically with mvv<=8. The prime science goals characterizing and distinguishing PLATO from the previous missions are: the detection and characterization of exoplanetary systems of all kinds, including both the planets and their host stars, reaching down to small, terrestrial planets in the habitable zone; the identification of suitable targets for future, more detailed characterization, including a spectroscopic search for biomarkers in nearby habitable exoplanets (e.g. ARIEL Mission scientific case, E-ELT observations from Ground); a full characterization of the planet host stars, via asteroseismic analysis: this will provide the Community with the masses, radii and ages of the host stars, from which masses, radii and ages of the detected planets will be determined

Current progress in the understanding of IgE-FcεRI interaction

The last decade has seen a wealth of studies aimed at the characterization of the binding between IgE and its high-affinity receptor, FcεRI. IgE-FcεRI complex formation is a major molecular event in atopic allergy. IgE-FcεRI binding connects allergen recognition to cellular triggering, ultimately leading to disease manifestations. Consequently, pharmacological intervention at this site is of universal relevance for atopic allergy. Until recent years, the complexity of IgE-FcεRI binding, together with the difficulty in obtaining fully functional recombinant IgE and FcεRI derivatives, often led to confusion and difficulty in data interpretation. Major advances in the understanding of this intricate protein-protein interaction have now been accomplished. Most of the current knowledge on the IgE-FcεRI recognition mode derives from long-lasting efforts in the field of structural biology. Protein engineering, high-throughput screening, immunological and biochemical studies also made relevant contributions in this domain. The data accumulated to date predict that IgE and FcεRI use their modular architecture to approach each other in an asymmetric stepwise manner determining a 1:1 stoichiometry. This recognition appears to be enhanced by conformational changes occurring upon binding, leading to the well-known high-affinity. In conclusion, the vast amount of high-quality data available broadened our knowledge on the IgE-FcεRI system; however, the fine structural details of the recognition process are still largely hypothetical. More studies are necessary to provide the experimental comprehensive picture required to carefully design efficient drugs acting at the IgE-FcεRI interface. Copyright © 2003 S. Karger AG, Basel