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Articles by M. Ito
Total Records ( 12 ) for M. Ito
  N Yamada , S Ota , Ying Liu , C. M Chang , S Thaker , M Nakamura and M. Ito

Risk factors for pulmonary embolism (PE) have been identified among populations in Western countries but have not been well characterized in Japan. A hospital-based case-control design employed cases with PE, which diagnosed by standard imaging techniques; controls were individuals drawn by systematic random sampling from the hospital admission register. A total of 100 (38 males and 62 females) and 199 controls were identified. Patients with PE were younger (56.5 vs 60.9 years) and more likely to be female. The odds ratio ([OR] adjusted for other factors) and 95% confidence interval (CI) for risk of PE was elevated for the following: female gender, prolonged immobilization, history of prior venous thromboembolism (VTE), lower extremity varicose veins, body mass index (BMI) ≥ 25 kg/m 2, extremity paralysis, and gout/hyperuricemia. Inherited thrombophilia was found in 14 patients with PE (14%). Risk factors for PE in Japan are comparable in magnitude to those in Western countries; only one third of PE cases had received VTE prophylaxis.

  A. Nishimura , Y. Hayashi , K. Tanaka , M. Hirota , S. Kato , M. Ito , K. Araki and E.J. Hu
  In this study, the environmental load of photovoltaic power generation system (PV) during its life cycle and energy payback time (EPT) are evaluated by LCA scheme. Two hypothetical case studies in Toyohashi, Japan and Gobi dessert in China have been carried out to investigate the influence of installation location and PV type on environmental load and EPT. The environmental load and EPT of a high-concentration photovoltaic power generation system (hcpV) and a multi-crystalline silicon photovoltaic power generation system (mc-Si PV) are studied. The study shows for a PV of 100 MW size, the total impacts of the hcpV installed in Toyohashi is larger than that of the hcpV installed in Gobi desert by 5% without consideration of recycling stage. The EPT of the hcpV assumed to be installed in Gobi desert is shorter than EPT of the hcpV assumed to be installed in Toyohashi by 0.64 year. From these results, the superiority to install PV in Gobi desert is certificated. Comparing with hcpV and mc-Si PV, the ratio of the total impacts of mc-Si PV to that of hcpV is 0.34 without consideration of recycling stage. The EPT of hcpV is longer than EPT of mc-Si PV by 0.27 year. The amount of global solar radiation contributing to the amount of power generation of mc-Si PV is larger than the amount of direct solar radiation contributing to the amount of power generation of hcpV by about 188 kW h/(m2 year) in Gobi desert. Consequently, it appears that using mc-Si PV in Gobi desert is the best option.
  K Zama , Y Hayashi , S Ito , Y Hirabayashi , T Inoue , K Ohno , N Okino and M. Ito

We report here a method of simultaneously quantifying glucosylceramide (GlcCer) and galactosylceramide (GalCer) by normal-phase HPLC using O-phtalaldehyde derivatives. Treatment with sphingolipid ceramide N-deacylase which converts the cerebrosides in the sample to their lyso-forms was followed by the quantitative labeling of free NH2 groups of the lyso-cerebrosides with O-phtalaldehyde. Using this method, 14.1 pmol of GlcCer and 10.4 pmol of GalCer, and 108.1 pmol of GlcCer and 191.1 pmol of GalCer were detected in zebrafish embryos and RPMI 1864 cells, respectively, while 22.2 pmol of GlcCer but no GalCer was detected in CHOP cells using cell lysate containing 100 µg of protein. Linearity for the determination of each cerebroside was observed from 50 to 400 µg of protein under the conditions used, which corresponds to approximately 103 to 105 RPMI cells and 5 to 80 zebrafish embryos. The present method clearly revealed that the treatment of RPMI cells with a GlcCer synthase inhibitor P4 resulted in a marked decrease in GlcCer but not GalCer, concomitantly with a significant decrease in the GlcCer synthase activity. On the other hand, GlcCer but not GalCer increased 2-fold when an acid glucocerebrosidase inhibitor CBE was injected into zebrafish embryos. Interestingly, the treatment of CHOP cells with ciclosporin A increased GlcCer possibly due to the inhibition of LacCer synthase. A significant increase in levels of GlcCer in fibroblasts from patients with Gaucher disease was clearly shown by the method. The proposed method is useful for the determination of GlcCer and GalCer levels in various biological samples.

  Y Ishibashi , Y Nagamatsu , S Meyer , A Imamura , H Ishida , M Kiso , N Okino , R Geyer and M. Ito

Although 6-gala series glycosphingolipids possessing R-Gal (/β) 1-6Galβ1-1'Cer have been found in some mollusks, pathogenic parasites, and fungi, their physiological functions and metabolic pathway are not fully understood. We described a novel method of detecting 6-gala series glyco- sphingolipids utilizing the specificity of endogalactosylceramidase (EGALC), which is capable of hydrolyzing 6-gala series glycosphingolipids to produce intact oligosaccharides and ceramides. EGALC catalyzes not only hydrolysis but also a transglycosylation reaction. In the latter reaction, EGALC transfers oligosaccharides from the glycosphingolipids to acceptors such as fluorescent 1-alkanols. Based on the transglycosylation reaction of EGALC, a specific, easy, fast, sensitive, and reproducible method of detecting 6-gala series glycosphingolipids was developed using NBD-pentanol as an acceptor. The fluorescent products, NBD-pentanol-conjugated 6-gala oligosaccharides, were separated and detected by TLC or HPLC with a fluorescent detector. Moreover, it was revealed that as well as glycosphingolipids, a glycoglycerolipid, digalactosyldiacylglycerol, was utilized by EGALC as a donor substrate. This method was successfully applied to detect 6-gala series glycosphingolipids in a fungus, Rhizopus oryzae, and a parasite, Taenia crassiceps. The method would be useful for studying glycosphingolipids and galactosyl glycerolipids which share the Gal (/β) 1-6Gal structure.

  X Xu , Y Horibata , M Inagaki , Y Hama , K Sakaguchi , H. M Goda and M. Ito

Endoglycoceramidase (EGCase; EC is a glycohydrolase that hydrolyzes the glycosidic linkage between the oligosaccharide and ceramide of various glycosphingolipids. We previously reported that hydra produced EGCase to digest glycosphingolipids of brine shrimp (Artemia salina), a type of aquatic crustacean used as a diet for the culture of hydra (Horibata Y, Sakaguchi K, Okino N, Iida H, Inagaki M, Fujisawa T, Hama Y, Ito M. 2004. J Biol Chem. 279:33379-33389). We report here that a major glycosphingolipid of brine shrimp is unique in structure and highly sensitive to EGCase. The glycosphingolipid was extracted from freshly hatched brine shrimp by Folch's partition, followed by mild alkaline hydrolysis and purification with a Sep-Pak plus silica cartridge. The structure of brine shrimp glycosphingolipid was determined by gas chromatography, gas chromatography-mass spectrometry, fast-atom bombardment mass spectrometry, and 1H-NMR spectrometry to be GlcNAc1-2Fuc1-3Manβ1-4Glcβ1-1'Cer. Two major molecular species of the glycosphingolipid were identified; the sugar and sphingoid base of each were the same but the major fatty acid was C22:0 and 2-hydroxy C22:0, respectively. This is the first report describing the glycosphingolipid that has an internal fucosyl residue substituted with 1-2 N-acetylglucosaminyl residue. This study also suggests the biological relevance of the glycosphingolipid as a dietary source of hydra which possesses EGCase as a digestion enzyme.

  M Kiyohara , K Sakaguchi , K Yamaguchi , T Araki and M. Ito

β-1,3-Xylanase from Vibrio sp. strain AX-4 (XYL4) is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules (CBMs) belonging to family 31 in the C-terminal region. To investigate the functions of these three modules, five deletion mutants lacking individual modules were constructed. The binding assay of these mutants showed that a repeating unit of the CBM was a non-catalytic β-1,3-xylan-binding module, while the catalytic module per se was not likely to contribute to the binding activity when insoluble β-1,3-xylan was used for the assay. The repeating CBMs were found to specifically bind to insoluble β-1,3-xylan, but not to β-1,4-xylan, Avicel, β-1,4-mannan, curdlan, chitin or soluble glycol-β-1,3-xylan. Both the enzyme and the binding activities for insoluble β-1,3-xylan but not soluble glycol-β-1,3-xylan were enhanced by NaCl in a concentration-dependent manner, indicating that the CBMs of XYL4 bound to β-1,3-xylan through hydrophobic interaction. This property of the CBMs was successfully applied to the purification of a recombinant XYL4 from the cell extracts of Escherichia coli transformed with the xyl4 gene and the detection of β-1,3-xylan-binding proteins including β-1,3-xylanase from the extract of a turban shell, Turbo cornutus.

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