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Your search keyword '"Hinou, Hiroshi"' showing total 353 results
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353 results on '"Hinou, Hiroshi"'

20. Selective reaction monitoring approach using structure-defined synthetic glycopeptides for validating glycopeptide biomarkers pre-determined by bottom-up glycoproteomics

Author

Shiratori, Kouta, primary, Yokoi, Yasuhiro, additional, Wakui, Hajime, additional, Hirane, Nozomi, additional, Otaki, Michiru, additional, Hinou, Hiroshi, additional, Yoneyama, Tohru, additional, Hatakeyama, Shingo, additional, Kimura, Satoshi, additional, Ohyama, Chikara, additional, and Nishimura, Shin-Ichiro, additional

Published
2022
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26. Glycoblotting-assisted O-glycomics: ammonium carbamate allows for highly efficient O-glycan release from glycoproteins

Author

Miura, Yoshiaki, Kato, Kentaro, Takegawa, Yasuhiro, Kurogochi, Masaki, Furukawa, Jun-ichi, Shinohara, Yasuro, Nagahori, Noriko, Amano, Maho, Hinou, Hiroshi, and Nishimura, Shin-Ichiro

Subjects
Glycoproteins -- Chemical properties, Carbamates -- Chemical properties, Carbamates -- Composition, Ammonium chloride -- Chemical properties, Ammonium chloride -- Composition, Ammonium compounds -- Chemical properties, Ammonium compounds -- Composition, Ammonium paratungstate -- Chemical properties, Ammonium paratungstate -- Composition, Chemistry
Abstract

Glycoblotting, high throughput method for N-glycan enrichment analysis based on the specific chemical ligation between aminooxy/hydrazide-polymers/solids and reducing N-glycans released from whole serum and cellular glycoproteins, was proved to be feasible for selective enrichment analysis of O-glycans of common (mucin) glycoproteins. We established a standard protocol of glycoblotting-based O-glycomics in combination with nonenzymatic chemical treatment to release reducing Oglycans predominantly from various glycoprotein samples. It was demonstrated that the nonreductive condition employing a simple ammonium salt, ammonium carbamate, made glycoblotting-based enrichment analysis of O-glycans possible without significant loss or unfavorable side reactions. A general workflow of glycoblotting using a hydrazide bead (BlotGlyco H), on-bead chemical manipulations, and subsequent mass spectrometry allowed for rapid O-glycomics of human milk osteopontin (OPN) and urinary MUC1 glycoproteins purified from healthy donors in a quantitative manner. It was revealed that structures of O-glycans in human milk OPN were varied with habitual fucosylation and N-acetyllactosamine units. It was also suggested that purified human urinary MUC1 was modified preferentially by sialylated O-glycans (94% of total) with 7:3 ratio of core 1 to core 2 type O-glycans. Versatility of the present strategy is evident because this method was proved to be suited for the enrichment analysis of general biological and clinical samples such as human serum and urine, cultured human cancer cells, and formalin-fixed paraffin-embedded tissue sections. It is our belief that the present protocols would greatly accelerate discovery of disease-relevant O-glycans as potential biomarkers. 10.1021/ac101599p

Published
2010

28. Combinatorial synthesis of MUC1 glycopeptides: Polymer blotting facilities chemical and enzymatic synthesis of highly complicated mucin glycopeptides

Author

Fumuto, Masataka, Hinou, Hiroshi, Ohta, Takashi, Ito, Takaomi, Yamada, Kuriko, Takimoto, Akio, Kondo, Hirosato, Shimizu, Hiroki, Inazu, Toshiyuki, Nakahara, Yoshiaki, and Nishimura, Shin-Ichiro

Subjects
Enzymes -- Chemical properties, Polymers -- Chemical properties, Peptides -- Chemical properties, Chemistry
Abstract

The rapid and combinatorial synthesis of MUC1 glycopeptide derivatives by the tandem synthetic process of solid-phase chemical syntheses and solution phase enzymatic syntheses using a heterobifunctional linker that acts as a suspension bridge between two different polymer platforms is described. The two-dimensional synthetic scheme using a versatile polymer blotting strategy will accelerate both practical enzymatic syntheses using immobilized glycosyltransferases and functional identification of biologically important glycopeptides.

Published
2005

29. Click Synthesis of Size- and Shape-Tunable Star Polymers with Functional Macrocyclic Cores for Synergistic DNA Complexation and Delivery

Author

Carbajo-Gordillo, Ana I., primary, Jiménez Blanco, José L., additional, Benito, Juan M., additional, Lana, Hugo, additional, Marcelo, Gema, additional, Di Giorgio, Christophe, additional, Przybylski, Cédric, additional, Hinou, Hiroshi, additional, Ceña, Valentín, additional, Ortiz Mellet, Carmen, additional, Mendicuti, Francisco, additional, Tros de Ilarduya, Conchita, additional, and García Fernández, José M., additional

Published
2020
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31. Impaired O-Glycosylation at Consecutive Threonine TTX Motifs in Mucins Generates Conformationally Restricted Cancer Neoepitopes

Author

Hayakawa, Shun, primary, Matsushita, Takahiko, additional, Yokoi, Yasuhiro, additional, Wakui, Hajime, additional, Garcia-Martin, Fayna, additional, Hinou, Hiroshi, additional, Matsuoka, Koji, additional, Nouso, Kazuhiro, additional, Kamiyama, Toshiya, additional, Taketomi, Akinobu, additional, and Nishimura, Shin-Ichiro, additional

Published
2020
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32. Synthesis, conformational analysis and in vivo assays of an anti-cancer vaccine that features an unnatural antigen based on an sp2-iminosugar fragment

Author

Bermejo, Iris A., primary, Navo, Claudio D., additional, Castro-López, Jorge, additional, Guerreiro, Ana, additional, Jiménez-Moreno, Ester, additional, Sánchez Fernández, Elena M., additional, García-Martín, Fayna, additional, Hinou, Hiroshi, additional, Nishimura, Shin-Ichiro, additional, García Fernández, José M., additional, Mellet, Carmen Ortiz, additional, Avenoza, Alberto, additional, Busto, Jesús H., additional, Bernardes, Gonçalo J. L., additional, Hurtado-Guerrero, Ramón, additional, Peregrina, Jesús M., additional, and Corzana, Francisco, additional

Published
2020
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34. Correction: A straightforward approach to antibodies recognising cancer specific glycopeptidic neoepitopes

Author

Wakui, Hajime, primary, Tanaka, Yoshikazu, additional, Ose, Toyoyuki, additional, Matsumoto, Isamu, additional, Kato, Koji, additional, Min, Yao, additional, Tachibana, Taro, additional, Sato, Masaharu, additional, Naruchi, Kentaro, additional, Martin, Fayna Garcia, additional, Hinou, Hiroshi, additional, and Nishimura, Shin-Ichiro, additional

Published
2020
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37. Additional file 4: of Exploring serum and immunoglobulin G N-glycome as diagnostic biomarkers for early detection of breast cancer in Ethiopian women

Author

Abrha Gebrehiwot, Melka, Daniel, Yimenashu Kassaye, Tufa Gemechu, Wajana Lako, Hinou, Hiroshi, and Shin-Ichiro Nishimura

Abstract

Table S2. Percentage of IgG N-glycan level relative to their concentration in serum. NC = normal control group, BC = whole breast cancer group. Indicated in bold are those N-glycans whose quantity in IgG showed considerable contribution to their expression level in serum. (DOCX 11612 kb)

Published
2019
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38. Additional file 3: of Exploring serum and immunoglobulin G N-glycome as diagnostic biomarkers for early detection of breast cancer in Ethiopian women

Author

Abrha Gebrehiwot, Melka, Daniel, Yimenashu Kassaye, Tufa Gemechu, Wajana Lako, Hinou, Hiroshi, and Shin-Ichiro Nishimura

Subjects
carbohydrates (lipids)
Abstract

Table S1. List of serum N-glycans statistically differed between whole cancer patients and normal controls. All glycan peaks except m/z 1915 showed increased abundance (p ≤ 0.05) in the BC patients compared to NC. Peak numbers (peak #) are according to the list of detected glycans as shown in Table 2. (DOCX 15 kb)

Published
2019
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41. The Use of Fluoroproline in MUC1 Antigen Enables Efficient Detection of Antibodies in Patients with Prostate Cancer

Author

Somovilla, Víctor J, Bermejo, Iris A., Albuquerque, Inês S, Martínez-Sáez, Nuria, Castro-López, Jorge, García-Martín, Fayna, Compañón, Ismael, Hinou, Hiroshi, Nishimura, Shin-Ichiro, Jiménez-Barbero, Jesús, Asensio, Juan L., Avenoza, Alberto, Busto, Jesús H., Hurtado-Guerrero, Ramón, Peregrina, Jesús M., Bernardes, Gonçalo J L, Corzana, Francisco, and Chemical Biology and Drug Discovery

Abstract

A structure-based design of a new generation of tumor-associated glycopeptides with improved affinity against two anti-MUC1 antibodies is described. These unique antigens feature a fluorinated proline residue, such as a (4S)-4-fluoro-l-proline or 4,4-difluoro-l-proline, at the most immunogenic domain. Binding assays using biolayer interferometry reveal 3-fold to 10-fold affinity improvement with respect to the natural (glyco)peptides. According to X-ray crystallography and MD simulations, the fluorinated residues stabilize the antigen-antibody complex by enhancing key CH/π interactions. Interestingly, a notable improvement in detection of cancer-associated anti-MUC1 antibodies from serum of patients with prostate cancer is achieved with the non-natural antigens, which proves that these derivatives can be considered better diagnostic tools than the natural antigen for prostate cancer.

Published
2017

42. Glycopeptides as Targets for Dendritic Cells: Exploring MUC1 Glycopeptides Binding Profile toward Macrophage Galactose-Type Lectin (MGL) Orthologs

Author

Artigas, Gerard, Monteiro, João T., Hinou, Hiroshi, Nishimura, Shin-Ichiro, Lepenies, Bernd, and Garcia-Martin, Fayna

Subjects
Mice, Glycosylation, Mucin-1, Glycopeptides, Animals, Humans, Lectins, C-Type, Dendritic Cells, Protein Binding
Abstract

The macrophage galactose-type lectin (MGL) recognizes glycan moieties exposed by pathogens and malignant cells. Particularly, mucin-1 (MUC1) glycoprotein presents an altered glycosylation in several cancers. To estimate the ability of distinct MGL orthologs to recognize aberrant glycan cores in mucins, we applied evanescent-field detection to a versatile MUC1-like glycopeptide microarray platform. Here, as binding was sequence-dependent, we demonstrated that not only sugars but also peptide region impact the recognition of murine MGL1 (mMGL1). In addition, we observed for all three MGL orthologs that divalent glycan presentation increased the binding. To assess the utility of the glycopeptide binders of the MGL orthologs for MGL targeting, we performed uptake assays with fluorescein-MUC1 using murine dendritic cells. A diglycosylated MUC1 peptide was preferentially internalized in an MGL-dependent fashion, thus showing the utility for divalent MGL targeting. These findings may be relevant to a rational design of antitumor vaccines targeting dendritic cells via MGL.

Published
2017

45. Chemical Synthesis Demonstrates That Dynamic O-Glycosylation Regulates the Folding and Functional Conformation of a Pivotal EGF12 Domain of the Human NOTCH1 Receptor

Author

Hayakawa, Shun, Yokoi, Yasuhiro, Hinou, Hiroshi, and Nishimura, Shin-Ichiro

Abstract

The interaction of the human NOTCH1 receptor and its ligands is a crucial step in initiating the intracellular signal transductions, in which O-glycosylation of the extracellular EGF-like domain strongly affects multiple aspects of cell differentiation, development, and cancer biology. However, consequences of biosynthetic O-glycosylation processes in the endoplasmic reticulum (ER) and Golgi on the folding of EGF domains remain unclear. Synthetic human NOTCH1 EGF12 modules allow for new insight into the crucial roles of O-glycosylation in the folding and conformation of this pivotal domain. Here, we show for the first time that predominant O-glucosylation at Ser458 facilitates proper folding of the EGF12 domain in the presence of calcium ion, while the nonglycosylated linear EGF12 peptide affords large amounts of misfolded products (>50%) during in vitrooxidative folding. Strikingly, O-fucosylation at Thr466 prior to O-glucosylation at Ser458 totally impedes folding of EGF12 independent of calcium ion, whereas modification of the Fucα1→ moiety with β-linked GlcNAc dramatically enhances folding efficiency. In addition, we elicit that extension of the Glcβ1→ moiety with xyloses is a negative-regulation mechanism in the folding of EGF12 when synthesis of a trisaccharide (Xylα1→3Xylα1→3Glcβ1→) dominates over the posttranslational modification at Thr466. Comprehensive nuclear magnetic resonance studies of correctly folded EGF12 modules demonstrate that noncovalently bonded bridges between sugars and peptide moieties, namely sugar bridges, contribute independently to the stabilization of the antiparallel β-sheet in the ligand-binding region. Our results provide evidence that the dynamic O-glycosylation status of the EGF12 domain elaborated in the ER and Golgi strongly affects folding and trafficking of the human NOTCH1 receptor.

Published
2024
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46. An Efficient Approach to the Discovery of Potent Inhibitors against Glycosyltransferases

Author

Hosoguchi, Kensaku, Maeda, Takahiro, Furukawa, Jun-ichi, Shinohara, Yasuro, Hinou, Hiroshi, Sekiguchi, Mitsuaki, Togame, Hiroko, Takemoto, Hiroshi, Kondo, Hirosato, and Nishimura, Shin-Ichiro

Abstract

We describe a standardized approach for searching potent and selective inhibitors of glycosyltransferases by high throughput quantitative MALDI-TOFMS-based screening of focused compound libraries constructed by 1,3-dipolar cycloaddition of the desired azidosugar nucleotides with various alkynes. An aminooxy-functionalized reagent with a stable isotope was conjugated with oligosaccharides to afford glycopeptides as acceptor substrates with improved ion sensitivity. Enhanced ionization potency of new substrates allowed for MALDI-TOFMS-based facile and quantitative analysis of enzymatic glycosylation in the presence of glycosyl donor substrates. A non-natural synthetic sugar nucleotide was identified to be the first highly specific inhibitor for rat recombinant α2,3-(N)-sialyltransferase (α2,3ST, IC50= 8.2 μM), while this compound was proved to become a favorable substrate for rat recombinant α2,6-(N)-sialyltransferase (α2,6ST, Km= 125 μM). Versatility of this strategy was demonstrated by identification of two selective inhibitors for human recombinant α1,3-fucosyltransferase V (α1,3-FucT, Ki= 293 nM) and α1,6-fucosyltransferase VIII (α1,6-FucT, Ki= 13.8 μM).

Published
2024
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47. Synthesis, conformational analysis and in vivo assays of an anti-cancer vaccine that features an unnatural antigen based on an sp2-iminosugar fragment.

Author

Bermejo, Iris A., Navo, Claudio D., Castro-López, Jorge, Guerreiro, Ana, Jiménez-Moreno, Ester, Sánchez Fernández, Elena M., García-Martín, Fayna, Hinou, Hiroshi, Nishimura, Shin-Ichiro, García Fernández, José M., Mellet, Carmen Ortiz, Avenoza, Alberto, Busto, Jesús H., Bernardes, Gonçalo J. L., Hurtado-Guerrero, Ramón, Peregrina, Jesús M., and Corzana, Francisco

Published
2020
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