Proposal of a Wireless Power Transfer Technique for Low-Power Multireceiver Applications

In this paper, we proposed and verified the feasibility of a unique wireless power transfer structure called a rail transformer to drive multiple low-power devices such as electronic shelf label (ESL) devices. The rail transformer is composed of a rectangular, circular-shaped transmitting yoke and two transmitting coils to provide wireless power. Multiple receiving yokes coupled with receiving coils are installed across the elongated edge of the transmitting yoke. It can be driven by low-frequency ac power at 50/60 Hz. In our prototype, the transmitting yoke is 900 mm long and 15 mm wide. We obtained the minimal induced wireless power, and the voltage was similar to 61 mW and 3.5 V, which is sufficient to drive a typical ESL device. By designing a nonuniform gap thickness between the transmitting and the receiving yokes at the specific locations, we improved the uniformity of the induced power for multiple ESL devices.ArticleIEEE TRANSACTIONS ON MAGNETICS. 51(11):8402904 (2015)journal articl

Verification of logic circuits using Mizar and its application to an adder circuit on a radix-2k2^kSD number (Topics in Information Sciences and Applied Functional Analysis)

ファイル差し替え（2021/08/20

Proposal of a Wireless Power Transfer Technique for Low-Power Multireceiver Applications

In this paper, we proposed and verified the feasibility of a unique wireless power transfer structure called a rail transformer to drive multiple low-power devices such as electronic shelf label (ESL) devices. The rail transformer is composed of a rectangular, circular-shaped transmitting yoke and two transmitting coils to provide wireless power. Multiple receiving yokes coupled with receiving coils are installed across the elongated edge of the transmitting yoke. It can be driven by low-frequency ac power at 50/60 Hz. In our prototype, the transmitting yoke is 900 mm long and 15 mm wide. We obtained the minimal induced wireless power, and the voltage was similar to 61 mW and 3.5 V, which is sufficient to drive a typical ESL device. By designing a nonuniform gap thickness between the transmitting and the receiving yokes at the specific locations, we improved the uniformity of the induced power for multiple ESL devices.ArticleIEEE TRANSACTIONS ON MAGNETICS. 51(11):8402904 (2015)journal articl

Tomosyn Negatively Regulates Arginine Vasopressin Secretion in Embryonic Stem Cell-Derived Neurons.

Arginine vasopressin (AVP) is secreted via exocytosis; however, the precise molecular mechanism underlying the exocytosis of AVP remains to be elucidated. To better understand the mechanisms of AVP secretion, in our study we have identified proteins that bind with a 25 kDa synaptosomal-associated protein (SNAP25). SNAP25 plays a crucial role in exocytosis, in the posterior pituitary. Embryonic stem (ES) cell-derived AVP neurons were established to investigate the functions of the identified proteins. Using glutathione S-transferase (GST)-pulldown assays and proteomic analyses, we identified tomosyn-1 (syntaxin-binding protein 5) as a SNAP25-binding protein in the posterior pituitary. Coimmunoprecipitation assays indicated that tomosyn formed N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes with SNAP25 and syntaxin1. Immunohistochemistry showed that tomosyn localized to the posterior pituitary. Mouse ES cells self-differentiated into AVP neurons (mES-AVP) that expressed tomosyn and two transmembrane SNARE proteins, including SNAP25 and syntaxin1. KCl increased AVP secretion in mES-AVP, and overexpression of tomosyn-1 reduced KCl-stimulated AVP secretion. Downregulation of tomosyn-1 with siRNA increased KCl-stimulated AVP secretion. These results suggested that tomosyn-1 negatively regulated AVP secretion in mES-AVP and further suggest the possibility of using mES-AVP culture systems to evaluate the role of synaptic proteins from AVP neurons

List of primary antibodies.

<p>List of primary antibodies.</p

Tomosyn is a SNAP25 binding protein in the posterior pituitary.

<p>(a) <i>In vitro</i> binding assay. Rat posterior pituitary lysates was incubated with GST-SNAP25 and glutathione (GSH) Sepharose. Eluted proteins bound to the beads were separated on SDS-PAGE followed by silver staining of proteins. The arrow indicates the band of interest. (b) Western blotting of pull-down samples. The arrowhead indicates the location of the immune reactive band reacting with anti-tomosyn antibody (Santa Cruz Biotechnology #sc-136105). Lane 1 = GST-SNAP25 with rat posterior pituitary lysates; lane 2 = GST-SNAP25 without rat posterior pituitary lysates (for both a, and b); Marker = molecular weight markers.</p

Tomosyn-1 negatively regulates secretion of AVP vesicles.

<p>(a–k) The effects of overexpression or siRNA treatments on tomosyn-1 expression. Dispersed SFEBq/gfCDM cultured cells were transfected with empty vector (vector) or tomosyn-1 vector (Tomosyn-1), scrambled siRNA (siScr) or Tomosyn-1 siRNA (siTomosyn-1 #1 or #2), or not treated (NT). (a, f, g) After 48 h, the expression levels of tomosyn were analysed by western blotting using anti-tomosyn antibody (Tomosyn, marked with arrowheads at the right). The levels of β-actin in the same samples were determined as a control for protein loading (bottom panels of a, f, g). (b–e) Representative immunostaining for tomosyn (green), copeptin (red), and DAPI (blue) at 48 h after overexpression of tomosyn-1 in dispersed SFEBq/gfCDM cultured cells. The merged image is shown in (e). (h–k) Representative immunostaining for tomosyn (green), copeptin (red), and DAPI (blue) at 48 h after knockdown of tomosyn-1 with siRNA in dispersed SFEBq/gfCDM cultured cells. The merged image is shown in (k). (l) AVP concentration in the media of artificial cerebrospinal fluid cultured cells (aCSF) (non-treated, NT; n = 13), KCl treatment (KCl; n = 13), empty vector with KCl (Vector + KCl; n = 12), and tomosyn-1 vector with KCl (Tomosyn-1 + KCl; n = 12). (m) AVP concentration from scrambled siRNA with KCl (siScr + KCl; n = 13), and siTomosyn-1 with KCl (siTomosyn-1 #1 + KCl group; n = 13, siTomosyn-1 #2 + KCl group; n = 12). Final KCl concentration was 100 mM. Values are expressed as the mean ± SEM. **P < 0.01.</p

Tomosyn is expressed in the rat hypothalamo-posterior pituitary axis.

<p>(a) Presence of tomosyn in the rat anterior and posterior pituitary as indicated by western blotting. Pituitary lysates were separated on SDS-PAGE followed by western blotting using anti-tomosyn, anti-SNAP25, anti-syntaxin 1A, anti-syntaxin 1B, anti-AVP, and anti-β-actin antibodies (as a loading control). (b) Subcellular fractionation of rat posterior pituitary samples. Fraction 1 (cytosolic proteins, F1) and Fraction 2 (membranes and membrane organelles, F2) were subjected to SDS-PAGE followed by western blotting using anti-tomosyn antibody. Five μg of proteins was loaded onto each lane. The subcellular fractionation was confirmed by western blotting with anti-Akt (cytosolic marker) and anti-N-cadherin (membrane fraction marker) antibodies. Tomosyn was present in both fractions. (c) Expression levels of tomosyn-1 mRNA in rat cortex and hypothalamus are similar. The amount of mRNA was determined using quantitative RT-PCR. The values are normalized to β-actin mRNA and are expressed as the mean ± SEM.</p

Arginine vasopressin (AVP)-secreting neurons from mouse embryonic stem cells express tomosyn.

<p>(a) Flow chart showing the method for culturing modified embryonic stem (ES) cells differentiating in serum-free medium (SFEBq)/growth factor-free chemically defined medium (gfCDM). DFNB = DMEM/F12 supplemented with 7 g/L glucose, N2 and B27. (b–e) Immunostaining with copeptin (red), NeuN (green), and DAPI (blue) in dispersed SFEBq/gfCDM cultured cells. A merged image is shown in the right panel. White scale bars indicate 20 μm. (f–k) Immunolocalization of proteins in dispersed SFEBq/gfCDM cultured cells, immunostaining with anti-tomosyn (green), anti-copeptin (red), or anti-SNAP25 (red) antibodies as analysed with confocal microscopy. Merged images are shown in the right panels. White scale bars indicate 25 μm. (l) AVP levels with or without 100 mM KCl stimulation in SFEBq/gfCDM cultured cells (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0164544#sec010" target="_blank">Methods</a> section). AVP concentrations in the media of artificial cerebrospinal fluid cultured cells (aCSF) (non-treated, NT; n = 8), or 100 mM KCl treatment (KCl; n = 8) are shown. Values are expressed as the mean ± SEM. **P < 0.01 versus NT (non-treated artificial spinal fluid). (m) Tomosyn-1 mRNA expressions in dispersed SFEBq/gfCDM cultured cells. The amount of mRNA was determined using quantitative RT-PCR. The values are normalized to β-actin mRNA and are expressed as the mean ± SEM.</p

Medical radiation exposure during gastrointestinal enteral metallic stent placement: Post hoc analysis of the REX‐GI study

Abstract Background and Aim Recently, the use of various endoscopic procedures performed under X‐ray fluoroscopy guidance has increased. With the popularization of such procedures, diagnostic reference levels (DRLs) have been widely accepted as the global standard for various procedures with ionizing radiation. The Radiation Exposure from Gastrointestinal Fluoroscopic Procedures (REX‐GI) study aimed to prospectively collect actual radiation exposure (RE) data and establish DRLs in gastrointestinal endoscopy units. In this post hoc analysis of the REX‐GI study, we established DRLs for each disease site by analyzing cases of gastrointestinal enteral metallic stent placement. Methods The REX‐GI study was a multicenter, prospective observational study conducted to collect actual RE data during gastrointestinal enteral metallic stent placement. To establish DRL values for three disease sites, namely the esophagus, gastroduodenum, and colon, we examined fluoroscopy time (FT; min), number of X‐ray images, air kerma at the patient entrance reference point (Ka,r; mGy), and the air kerma–area product (PKA; Gy cm2) during enteral metallic stent placement. Results Five‐hundred and twenty‐three stenting procedures were performed. The DRL values of FT (min) and the number of X‐ray images for the esophagus/gastroduodenum/colon were 9/16/18 min and 9/15/11 min, respectively. Furthermore, the DRL values of Ka,r and PKA for each disease site were 43.3/120/124 mGy and 10.3/36.6/48.4 Gy cm2, respectively. Among the procedures, esophageal stents were significantly associated with the lowest values (P < 0.001). Conclusion The characteristics of RE vary according to disease site among gastrointestinal enteral metallic stent placements. Thus, it is desirable to set DRL values based on the disease site