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Sakaiminato, Japan

The present invention provides a food/drink or pharmaceutical composition for oral administration for improving an acidic urine, comprising fucoidan or a fucoidan-containing material as an active ingredient, characterized in that a urinal pH is persistently increased; use of fucoidan or a fucoidan-containing material for production of the food/drink or the pharmaceutical composition for oral administration; and a method for improving an acidic urine by persistently increasing a urinal pH of a patient, which comprises orally administering fucoidan or a fucoidan-containing material to a patient.


Patent
Tottori University and Marine Products Kimuraya Co. | Date: 2014-07-10

Disclosed is a therapy which is for preventing or treating cartilage damage and diseases associated with cartilage damage, such as arthritides and osteoarthritis, and utilizes a more effective and more safe medicinal agent. Specifically disclosed are a cartilage production promoter, a glucosaminoglycan and/or proteoglycan production promoter, and a prophylactic or therapeutic agent for diseases associated with cartilage damage, each of which comprises fucoidan as an active ingredient.


Morimoto M.,Tottori University | Takatori M.,Tottori University | Hayashi T.,Tottori University | Mori D.,Tottori University | And 8 more authors.
Carbohydrate Research | Year: 2014

Fucoidan and chondroitin sulfate, which are well known sulfated polysaccharides, were depolymerized under hydrothermal conditions (120-180 C, 5-60 min) as a method for the preparation of sulfated polysaccharides with controlled molecular weights. Fucoidan was easily depolymerized, and the change of the molecular weight values depended on the reaction temperature and time. The degree of sulfation and IR spectra of the depolymerized fucoidan did not change compared with those of untreated fucoidan at reaction temperatures below 140 C. However, fucoidan was partially degraded during depolymerization above 160 C. Nearly the same depolymerization was observed for chondroitin sulfate. These results indicate that hydrothermal treatment is applicable for the depolymerization of sulfated polysaccharides, and that low molecular weight products without desulfation and deformation of the initial glycan structures can be obtained under mild hydrothermal conditions.©2013 Elsevier Ltd. All rights reserved. Source


Sekiguchi T.,Kyushu University | Kamada Y.,Japan National Institute for Basic Biology | Furuno N.,Hiroshima University | Funakoshi M.,Okayama University | And 2 more authors.
Genes to Cells | Year: 2014

The yeast Ras-like GTPases Gtr1p and Gtr2p form a heterodimer, are implicated in the regulation of TOR complex 1 (TORC1) and play pivotal roles in cell growth. Gtr1p and Gtr2p bind Ego1p and Ego3p, which are tethered to the endosomal and vacuolar membranes where TORC1 functions are regulated through a relay of amino acid signaling interactions. The mechanisms by which Gtr1p and Gtr2p activate TORC1 remain obscure. We probed the interactions of the Gtr1p-Gtr2p complex with the Ego1p-Ego3p complex and TORC1 subunits. Mutations in the region (179-220 a.a.) following the nucleotide-binding region of Gtr1p and Gtr2p abrogated their mutual interaction and resulted in a loss in function, suggesting that complex formation between Gtr1p and Gtr2p was indispensable for TORC1 function. A modified yeast two-hybrid assay showed that Gtr1p-Gtr2p complex formation is important for its interaction with the Ego1p-Ego3p complex. GTP-bound Gtr1p interacted with the region containing the HEAT repeats of Kog1p and the C-terminal region of Tco89p. The GTP-bound Gtr2p suppressed a Kog1p mutation. Our findings indicate that the interactions of the Gtr1p-Gtr2p complex with the Ego1p-Ego3p complex and TORC1 components Kog1p and Tco89p play a role in TORC1 function. © 2014 by the Molecular Biology Society of Japan and Wiley Publishing Asia Pty Ltd. Source


Sa-Moura B.,Yale University | Sa-Moura B.,Abel Salazar Biomedical Sciences Institute | Funakoshi M.,Yale University | Funakoshi M.,Marine Products Kimuraya Co. | And 5 more authors.
Journal of Biological Chemistry | Year: 2013

Regulated protein degradation mediated by the ubiquitinproteasomesystem(UPS)iscriticaltoeukaryoticproteinhomeostasis. Often vital to degradation of protein substrates is their disassembly, unfolding, or extraction from membranes. These processes are catalyzed by the conserved AAA-ATPase Cdc48 (also known as p97). Here we characterize the Cuz1 protein (Cdc48-associated UBL/zinc finger protein-1), encoded by a previously uncharacterized arsenite-inducible gene in budding yeast. Cuz1, like its human ortholog ZFAND1, has both anAN1-type zinc finger (Zf-AN1) andadivergent ubiquitin-like domain (UBL). We show that Cuz1 modulates Cdc48 function in the UPS. The two proteins directly interact, and the Cuz1 UBL, but not Zf-AN1, is necessary for binding to the Cdc48 N-terminal domain. Cuz1 also associates, albeit more weakly, with the proteasome, and the UBL is dispensable for this interaction. Cuz1-proteasome interaction is strongly enhanced by exposure of cells to the environmental toxin arsenite, and in a proteasome mutant, loss of Cuz1 enhances arsenite sensitivity. Whereas loss of Cuz1 alone causes only minor UPS degradation defects, its combination with mutations in the Cdc48 Npl4-Ufd1 complex leadstomuch greater impairment. Cuz1 helpslimit the accumulation of ubiquitin conjugates on both the proteasome and Cdc48, suggestingapossible rolein the transfer of ubiquitylated substrates from Cdc48 to the proteasome or in their release from these complexes. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc Published in the U.SA. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Source

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