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Lithium-sulfur (Li-S) batteries are promising candidates for next generation electrical energy storage devices due to their high specific energy. Despite intense research, there are still a number of technical challenges in developing a high performance Li-S battery. To elucidate the issues, an all solid-state Li-S battery was fabricated using Li 3 PS 4 solid electrolyte. Most of the theoretical capacity of sulfur, 1600 mAhg −1 was attained in the initial discharge-charge cycles with a high coulombic efficiency approaching 99%. To verify the benefit of the solid state electrolyte, galvanostatic stripping-deposition tests were also carried out on a symmetrical Li/Li cell and compared with those of a liquid electrolyte (1 M-lithium bis(trifluoromethane sulfonyl) imide (LiTFSI) in a mixture of 1,3-dioxolane (DOL)-diethoxyethane (DEE)). The kinetics and thermodynamics of the solid-state cell are discussed from the viewpoint of the charge transfer processes. This study demonstrates both the merits and drawbacks of using the solid sulfide electrolyte in a Li-S battery and facilitates the further improvement of this important high energy storage device. Lithium-sulfur (Li-S) batteries are attracting growing interest owing to their high specific energy above 3000 Whkg −1 (active material). However, before this technology can be used in practice, there are some significant challenges to overcome, including red-ox shuttle of polysulfides as well as poor lithium cycle performance.The polysulfide redox shuttle originates from the dissolution of the cathode material into the organic electrolyte. So far, various approaches have been suggested to solve the red-ox shuttle issue. LiNO 3 is a well-known additive for optimizing the solid electrolyte interphase (SEI) on lithium metal electrode, such as to block the deposition of polysulfides.1,2 An ionommer (e.g., Nafion) has also been proposed for preventing the polysulfide migration 3 and a buffer solution containing polysulfides can facilitate a good cycle ability as well. 4 The poor lithium cycle performance is due to the consumption of lithium metal during the charge-discharge process. It is well known that the lithium cycling response is primarily determined by the type of electrolyte to which it is in contact. 5,6 In the development of lithiummetal secondary batteries the Figure of Merit (FOM) is the parameter used to evaluate the lithium cycling ability. 5,6 Although lithium metal has a high specific capacity of 3862 mAhg −1 , its effective degree of utilization (i.e., the lithium loss relative to the amount of total input lithium metal) has to be taken into account. Generally, a valid parameter to determine the cycle ability of the lithium anode is the efficiency. For instance, it is difficult to achieve an efficiency higher than 99% for lithium cycling in a typical liquid electrolyte cell due to losses during its dissolution-deposition reaction. Therefore, the improvement of the FOM of a liquid electrolyte Li-S battery has been a major challenge to enhance the charge-disc...

ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-like (ADAMTSL) proteins, a subgroup of the ADAMTS superfamily, share several domains with ADAMTS proteinases, including thrombospondin type I repeats, a cysteine-rich domain, and an ADAMTS spacer, but lack a catalytic domain. We identified two new members of ADAMTSL proteins, ADAMTSL-6␣ and -6␤, that differ in their N-terminal amino acid sequences but have common C-terminal regions. When transfected into MG63 osteosarcoma cells, both isoforms were secreted and deposited into pericellular matrices, although ADAMTSL-6␣, in contrast to -6␤, was barely detectable in the conditioned medium. Immunolabeling at the light and electron microscopic levels showed their close association with fibrillin-1-rich microfibrils in elastic connective tissues. Surface plasmon resonance analyses demonstrated that ADAMTSL-6␤ binds to the N-terminal half of fibrillin-1 with a dissociation constant of ϳ80 nM. When MG63 cells were transfected or exogenously supplemented with ADAMTSL-6, fibrillin-1 matrix assembly was promoted in the early but not the late stage of the assembly process. Furthermore, ADAMTSL-6 transgenic mice exhibited excessive fibrillin-1 fibril formation in tissues where ADAMTSL-6 was overexpressed. All together, these results indicated that ADAMTSL-6 is a novel microfibril-associated protein that binds directly to fibrillin-1 and promotes fibrillin-1 matrix assembly.

Extracellular matrix (ECM), which provides critical scaffolds for all adhesive cells, regulates proliferation, differentiation, and apoptosis. Different cell types employ customized ECMs, which are thought to play important roles in the generation of so-called niches that contribute to cell-specific functions. The molecular entities of these customized ECMs, however, have not been elucidated. Here, we describe a strategy for transcriptome-wide identification of ECM proteins based on computational screening of >60,000 full-length mouse cDNAs for secreted proteins, followed by in vitro functional assays. These assays screened the candidate proteins for ECM-assembling activities, interactions with other ECM molecules, modifications with glycosaminoglycans, and cell-adhesive activities, and were then complemented with immunohistochemical analysis. We identified 16 ECM proteins, of which seven were localized in basement membrane (BM) zones. The identification of these previously unknown BM proteins allowed us to construct a body map of BM proteins, which represents the comprehensive immunohistochemistry-based expression profiles of the tissue-specific customization of BMs. basement membrane ͉ body map ͉ niche ͉ cell adhesion ͉ glycosaminoglycan

In order to provide a uniform and desirable dose distribution over a large radiation field, spot beam scanning is one of the most useful methods. A new spot beam scanning system was constructed for a 70 MeV proton beam. The lateral dose distribution was uniform with +/- 2.5% for an 18 cm square field. It was possible to control the dose at each point in the radiation field by this spot scanning method. This system has been confirmed to be satisfactory for delivering a proton beam in the desired field shape and dose level.

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We screened more than 60000 RIKEN mouse cDNAs for novel ECM (extracellular matrix) proteins by extensive computational screening followed by recombinant expression and immunohistochemical characterization. We identified two novel olfactomedin-family proteins characterized by the presence of tandem CXCXCX9C motifs in the N-terminal region, a coiled-coil domain and an olfactomedin domain in the C-terminal region. These proteins, named photomedin-1 and photomedin-2, were secreted as disulphide-bonded dimers (photomedin-1) or oligomers/multimers (photomedin-2) with O-linked carbohydrate chains, although photomedin-1 was proteolytically processed in the middle of the molecule after secretion. In the retina, photomedin-1 was selectively expressed in the outer segment of photoreceptor cells and photomedin-2 was expressed in all retinal neurons. Among a panel of ECM components, including glycosaminoglycans, photomedins preferentially bound to chondroitin sulphate-E and heparin. These results, together, indicate that photomedins are novel olfactomedin-domain-containing extracellular proteins capable of binding to proteoglycans containing these glycosaminoglycan chains.