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3 results on '"Erina Ohno"'

1. Development and Application of Multidimensional HPLC Mapping Method for O-linked Oligosaccharides

Author

Koichi Kato, Atsuhiro Yoshida, Hirokazu Yagi, Erina Ohno, and Sachiko Kondo

Subjects
O-glycans, HPLC map, glycosylation profiling, sulfated oligosaccharide, IgA, Microbiology, QR1-502
Abstract

Glycosylation improves the solubility and stability of proteins, contributes to the structural integrity of protein functional sites, and mediates biomolecular recognition events involved in cell-cell communications and viral infections. The first step toward understanding the molecular mechanisms underlying these carbohydrate functionalities is a detailed characterization of glycan structures. Recently developed glycomic approaches have enabled comprehensive analyses of N-glycosylation profiles in a quantitative manner. However, there are only a few reports describing detailed O-glycosylation profiles primarily because of the lack of a widespread standard method to identify O-glycan structures. Here, we developed an HPLC mapping method for detailed identification of O-glycans including neutral, sialylated, and sulfated oligosaccharides. Furthermore, using this method, we were able to quantitatively identify isomeric products from an in vitro reaction catalyzed by N-acetylglucosamine-6O-sulfotransferases and obtain O-glycosylation profiles of serum IgA as a model glycoprotein.

Published
2011
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2. Comparison of Methods for Profiling O-Glycosylation

Author

Carlito B. Lebrilla, Naoyuki Taniguchi, Anne Dell, Erina Ohno, Akihiro Kondo, Malin Bäckström, Kazuaki Kakehi, Kay-Hooi Khoo, Michiko Tajiri, Elizabeth Palaima, Hiromi Ito, Yoshiyuki Hiki, Bérangère Tissot, Catherine E. Costello, Jan Novak, Milos V. Novotny, Hirokazu Yagi, Miyako Nakano, Parastoo Azadi, Nana Kawasaki, Koichi Kato, Mayumi Ishihara, Nicolle H. Packer, Catherine A. Hayes, Kevin Canis, Daniel Kolarich, Stuart M. Haslam, Gunnar C. Hansson, Hisashi Narimatsu, Kunihiko Kobayashi, Matthew B. Renfrow, Kristina A. Thomsson, Yoshinao Wada, Niclas G. Karlsson, and Shin-Yi Yu

Subjects
human serum iga1, Glycosylation, Computational biology, Biology, Proteomics, Bioinformatics, Biochemistry, Analytical Chemistry, Glycomics, chemistry.chemical_compound, Human disease, resonance mass-spectrometry, Human proteome project, Metabolome, antibodies, Profiling (information science), hinge region, Molecular Biology, electron-capture dissociation, chemistry, Proteome, peptides, nephropathy, glycans, heterogeneity, immunoglobulin
Abstract

The Human Proteome Organisation Human Disease Glycomics/Proteome Initiative recently coordinated a multiinstitutional study that evaluated methodologies that are widely used for defining the N-glycan content in glycoproteins. The study convincingly endorsed mass spectrometry as the technique of choice for glycomic profiling in the discovery phase of diagnostic research. The present study reports the extension of the Human Disease Glycomics/ Proteome Initiative's activities to an assessment of the methodologies currently used for O-glycan analysis. Three samples of IgA1 isolated from the serum of patients with multiple myeloma were distributed to 15 laboratories worldwide for O-glycomics analysis. A variety of mass spectrometric and chromatographic procedures representative of current methodologies were used. Similar to the previous N-glycan study, the results convincingly confirmed the pre-eminent performance of MS for O-glycan profiling. Two general strategies were found to give the most reliable data, namely direct MS analysis of mixtures of permethylated reduced glycans in the positive ion mode and analysis of native reduced glycans in the negative ion mode using LC-MS approaches. In addition, mass spectrometric methodologies to analyze O-glycopeptides were also successful. Molecular & Cellular Proteomics 9: 719-727, 2010.

Published
2010

3. Development and Application of High Performance Liquid Chromatography Map of Glucuronyl N-glycans

Author

Hirokazu Yagi, Kenzo Yamada, Erina Ohno, Maho Utsumi, Yoshiki Yamaguchi, Eiji Kurimoto, Noriko Takahashi, Shogo Oka, Toshisuke Kawasaki, and Koichi Kato

Subjects
chemistry.chemical_classification, Glycan, Glycosylation, Chromatography, biology, Oligosaccharide, digestive system, High-performance liquid chromatography, Enzyme catalysis, Glycomics, chemistry.chemical_compound, Enzyme, Sulfation, chemistry, Biochemistry, biology.protein
Abstract

Although the multi-dimensional HPLC maps of neutral, sialyl, and sulfated N-glycans have been reported and widely used for glycosylation profiling, those of glucuronyl oligosaccharides have not yet been available. In the present study, by in vitro enzymatic reactions, we prepared 55 different glucuronyl PA-oligosaccharides that include 6 kinds of HNK-1-containing N-glycans, and established their HPLC map. Furthermore, we applied this map to the characterization of branch specificity in glucuronylation reaction catalyzed by human GlcAT-S, revealing that this enzyme transfers the glucuronyl residues preferentially onto the Gal 1�4GlcNAc 1�4Man 1�3 and Gal 1�4GlcNAc 1�2Man 1�3 branches of a galactose-terminated tri-antennary oligosaccharide. The HPLC map developed in the present study will be a useful glycomics tool for identification and profiling of glucuronyl N-glycans expressed in the neural and other biological systems.

Published
2008

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