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Search: authors:"Yoshiaki Miura"

5 papers found.
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Changes in N-glycans of IgG4 and its relationship with the existence of hypocomplementemia and individual organ involvement in patients with IgG4-related disease

Watanabe. Funding acquisition: Hiroshi Watanabe. Investigation: Naoki Konno, Mitsuru Sugimoto, Yoshiaki Miura, Taichi Aihara, Hiroshi Watanabe. Methodology: Naoki Konno, Mitsuru Sugimoto, Tadayuki Takagi ... Kobayashi, Kiyoshi Migita, Atsushi Komatsuda, Hiromasa Ohira, Hiroshi Watanabe. Software: Yoshiaki Miura, Taichi Aihara. Supervision: Kiyoshi Migita, Hiromasa Ohira, Hiroshi Watanabe. Validation: Hiroko

α-N-Acetylgalactosamine-capping of chondroitin sulfate core region oligosaccharides primed on xylosides

We previously reported that cultured mammalian cells incubated with 4-methylumbelliferyl (MU) or p-nitrophenyl (pNP) β-xyloside synthesize an α-GalNAc-terminated pentasaccharide resembling the glycosaminoglycan-core protein linkage region. Here we show that human melanoma M21 cells and human neuroblastoma cells incubated with Xylβ-MU/pNP also make an α-GalNAc-terminated...

Characterization of mammalian UDP-GalNAc:glucuronide α1-4-N-acetylgalactosaminyltransferase

We previously reported that cultured cells incubated with β-xylosides synthesized α-GalNAc-capped GAG-related xylosides, GalNAcαGlcAβGalβGalβXylβ-R and GalNAcαGlcA-βGalNAcβGlcAβGalβGalβXylβ-R, where R is 4-methylumbelliferyl or p-nitrophenyl (Manzi et al., 1995; Miura and Freeze, 1998). In this study, we characterized an α-N-acetylgalactosaminyltransferase (α-GalNAc-T) that...

Requirement for a different hydrophobic moiety and reliable chromogenic substrate for Endo-type glycosylceramidases

A series of synthetic lactosides with aglycones that differed in length and structure were used to determine the substrate specificity of Endo-type glycosylceramidases. Endoglycoceramidases (EGCase) from bacteria preferred lactosides with an acylamide structure over simple n-alkyl lactosides. While ceramide glycanase (CGase) from leech did not show preference. N-acyl-aminobutyl...

COG8 deficiency causes new congenital disorder of glycosylation type IIh

We describe a new Type II congenital disorder of glycosylation (CDG-II) caused by mutations in the conserved oligomeric Golgi (COG) complex gene, COG8. The patient has severe psychomotor retardation, seizures, failure to thrive and intolerance to wheat and dairy products. Analysis of serum transferrin and total serum N-glycans showed normal addition of one sialic acid, but severe...