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Yamaguchi-shi, Japan

Yamaguchi Prefectural University is a public university in Yamaguchi, Yamaguchi, Japan. The predecessor of the school was founded in 1941, and it was chartered as a university in 1975. In 1996 it became coeducative. Wikipedia.


Matsui K.,Yamaguchi University | Takaki S.,Yamaguchi University | Shimada K.,Yamaguchi Prefectural University | Hajika M.,Japan National Agriculture and Food Research Organization
Bioscience, Biotechnology and Biochemistry | Year: 2011

Oxygenation of lipids during the processing soybeans affects the flavor properties of soy products. We prepared tofu under anaerobic conditions and then evaluated its sensory properties and the compositions of volatiles and oxidized lipids. Anaerobic processing resulted in tofu with less intense richness (kokumi) concomitant with reductions in the amounts of oxidized lipids and volatile compounds. Source


Yamazaki F.,Yamaguchi Prefectural University
Journal of Physiological Sciences | Year: 2015

To clarify the characteristics of the thermal control of skin blood flow (SkBF) in individuals with a cold constitution, we examined the cutaneous vasoconstrictor responses in the calf and dorsal foot during whole-body and local skin cooling in young women complaining of chilliness (C group) and young women not suffering from it (N group). During whole-body skin cooling, the vasoconstrictor sensitivity in the dorsal foot, but not in the calf, was greater in the C group than in the N group. The C group also showed greater vasoconstrictor responses in the dorsal foot, but not in the calf, during local skin cooling and the iontophoretic application of norepinephrine. These findings suggest that the C group possesses a specific SkBF controlling system that is characterized by higher adrenergic sensitivity for greater cutaneous vasoconstriction in the distal portion of the lower extremities during cold exposure. © 2015, The Physiological Society of Japan and Springer Japan. Source


Onda Y.,Japan National Institute of Agrobiological Science | Nagamine A.,Japan National Institute of Agrobiological Science | Sakurai M.,Japan National Institute of Agrobiological Science | Kumamaru T.,Kyushu University | And 2 more authors.
Plant Cell | Year: 2011

In the rice (Oryza sativa) endosperm, storage proteins are synthesized on the rough endoplasmic reticulum (ER), in which prolamins are sorted to protein bodies (PBs) called type-I PB (PB-I). Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3, an ortholog of human P5, contains a conserved structural disulfide in the redox-inactive thioredoxin-like (TRX) domain and was efficiently targeted to the surface of PB-I in a redox active site-dependent manner, whereas PDIL1;1, an ortholog of human PDI, was localized in the ER lumen. Complementation analyses using PDIL1;1 knockout esp2 mutant indicated that the a and a′ TRX domains of PDIL1;1 exhibited similar redox activities and that PDIL2;3 was unable to perform the PDIL1;1 functions. PDIL2;3 knockdown inhibited the accumulation of Cys-rich 10-kD prolamin (crP10) in the core of PB-I. Conversely, crP10 knockdown dispersed PDIL2;3 into the ER lumen. Glutathione S-transferase-PDIL2;3 formed a stable tetramer when it was expressed in Escherichia coli, and the recombinant PDIL2;3 tetramer facilitated a-globulin(C79F) mutant protein to form nonnative intermolecular disulfide bonds in vitro. These results indicate that PDIL2;3 and PDIL1;1 are not functionally redundant in sulfhydryl oxidations of structurally diverse storage proteins and play distinct roles in PB development. We discuss PDIL2;3-dependent and PDIL2;3-independent oxidation pathways that sustain disulfide bonds of crP10 in PB-I. © American Society of Plant Biologists. Source


Washida H.,Washington State University | Washida H.,Nara Institute of Science and Technology | Sugino A.,Washington State University | Sugino A.,Nara Institute of Science and Technology | And 9 more authors.
Plant Journal | Year: 2012

Studies focusing on the targeting of RNAs that encode rice storage proteins, prolamines and glutelins to specific sub-domains of the endoplasmic reticulum (ER), as well as mis-localization studies of other storage protein RNAs, indicate a close relationship between the ER site of RNA translation and the final site of protein deposition in the endomembrane system in developing rice endosperm. In addition to prolamine and glutelin, rice accumulates smaller amounts of α-globulins, which are deposited together with glutelin in the protein storage vacuole (PSV). In situ RT-PCR analysis revealed that α-globulin RNAs are not distributed to the cisternal ER as expected for a PSV-localized protein, but instead are targeted to the protein body-ER (PB-ER) by a regulated process requiring cis-sorting sequences. Sequence alignments with putative maize Î-zein cis-localization elements identified several candidate regulatory sequences that may be responsible for PB-ER targeting. Immunocytochemical analysis confirmed the presence of α-globulin on the periphery of the prolamine protein bodies and packaging in Golgi-associated dense vesicles, as well as deposition and storage within peripheral regions of the PSV. Mis-targeting of α-globulin RNAs to the cisternal ER dramatically alters the spatial arrangement of α-globulin and glutelin within the PSV, with the accompanying presence of numerous small α-globulin particles in the cytoplasm. These results indicate that α-globulin RNA targeting to the PB-ER sub-domain is essential for efficient transport of α-globulins to the PSV and its spatial arrangement in the PSV. Such RNA localization prevents potential deleterious protein-protein interactions, in addition to performing a role in protein targeting. © 2011 Blackwell Publishing Ltd. Source


Yamashita O.,Yamaguchi University | Yoshimura K.,Yamaguchi University | Yoshimura K.,Yamaguchi Prefectural University | Nagasawa A.,Yamaguchi University | And 4 more authors.
PLoS ONE | Year: 2013

Aims: Abdominal aortic aneurysms (AAAs) are characterized by chronic inflammation, which contributes to the pathological remodeling of the extracellular matrix. Although mechanical stress has been suggested to promote inflammation in AAA, the molecular mechanism remains uncertain. Periostin is a matricellular protein known to respond to mechanical strain. The aim of this study was to elucidate the role of periostin in mechanotransduction in the pathogenesis of AAA. Methods and Results: We found significant increases in periostin protein levels in the walls of human AAA specimens. Tissue localization of periostin was associated with inflammatory cell infiltration and destruction of elastic fibers. We examined whether mechanical strain could stimulate periostin expression in cultured rat vascular smooth muscle cells. Cells subjected to 20% uniaxial cyclic strains showed significant increases in periostin protein expression, focal adhesion kinase (FAK) activation, and secretions of monocyte chemoattractant protein-1 (MCP-1) and the active form of matrix metalloproteinase (MMP)-2. These changes were largely abolished by a periostin-neutralizing antibody and by the FAK inhibitor, PF573228. Interestingly, inhibition of either periostin or FAK caused suppression of the other, indicating a positive feedback loop. In human AAA tissues in ex vivo culture, MCP-1 secretion was dramatically suppressed by PF573228. Moreover, in vivo, periaortic application of recombinant periostin in mice led to FAK activation and MCP-1 upregulation in the aortic walls, which resulted in marked cellular infiltration. Conclusion: Our findings indicated that periostin plays an important role in mechanotransduction that maintains inflammation via FAK activation in AAA. © 2013 Yamashita et al. Source

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