Utsunomiya University

About: Utsunomiya University is a education organization based out in Utsunomiya, Japan. It is known for research contribution in the topics: Laser & Holography. The organization has 4139 authors who have published 6812 publications receiving 91975 citations. The organization is also known as: Utsunomiya daigaku.

Acceleration of Publish/Subscribe Messaging in ROS-compliant FPGA Component

Abstract: Intelligent robots demand complex information processing such as SLAM (Simultaneous Localization and Mapping) and DNN (Deep Neural Network). FPGA (Field Programmable Gate Array) is expected to accelerate these applications with high energy efficiency. Introducing FPGA into robots is difficult due to its high development costs. In order to introduce FPGA easily to a system on ROS (Robot Operating System) development platform, ROS-compliant FPGA Component has been proposed. However, large communication latency between ROS components is a severe problem. This research aims to reduce the latency by implementing Publish/Subscribe messaging of ROS as hardware. Based on result of network packets analysis in ROS system, we propose a method of implementing a Hardware ROS-compliant FPGA Component. It is done by separating registration part (XMLRPC) and data communication part (TCPROS) of Publish/Subscribe messaging. Evaluation result shows that the proposed Hardware ROS-compliant FPGA component can reduce delay time of Publish/Subscribe messaging even with small amount of hardware.

Purification and characterization of exo-type cellouronate lyase

Abstract: A bacterial strain, Brevundimonas sp. SH203, has an ability to degrade cellouronate, β-(1→4)-linked polyglucuronic acid sodium salt, which is artificially prepared from regenerated cellulose by TEMPO (2,2,6,6-tetramethylpiperidine-1-oxyl radical)-mediated oxidation. In a previous paper, an endo-type cellouronate lyase (CUL-I) has been isolated from the strain. In this paper, we purified another cellouronate lyase, CUL-II, from cell-free extracts of Brevundimonas sp. SH203. CUL-II was a monomeric protein with a molecular mass of 56 kDa by size exclusion chromatography and 62 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and most active at pH 7.5. CUL-II formed monomers in a small quantity from cellouronate without forming any intermediate oligomers, whereas it degraded C4′–C5′ unsaturated cellouronate dimer more easily. Thus, CUL-II behaves as an exo-type lyase in degradation of cellouronate. When CUL-I and CUL-II were simultaneously treated to cellouronate, it was degraded to monomers more efficiently than treatment with one enzyme alone, CUL-I or CUL-II. Hence, cellouronate is synergistically degraded to monomers by Brevundimonas sp. SH203 by endo- and exo-type lyases, CUL-I and CUL-II, respectively.

Differential dose response of mTOR signaling to oral administration of leucine in skeletal muscle and liver of rats.

Abstract: Phosphorylation of eukaryotic initiation factor 4E-binding protein 1 (4E-BP1) and 70-kDa ribosomal protein S6 kinase (S6K1) in the rat liver increased in proportion to the amount of leucine administered, ranging from 0.169 to 1.35 g/kg of body weight. In the skeletal muscle, phosphorylation of these factors reached a plateau at 0.675 g/kg of body weight. The sensitivity of mammalian target of rapamycin (mTOR) signaling to leucine in the skeletal muscle appeared to be higher than that in the liver.