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Article ; Online: Comprehensive Cellular Glycan Profiling of Glycoproteins and Glycosphingolipids by Glycoblotting and BEP Methods.

Hanamatsu, Hisatoshi / Furukawa, Jun-Ichi

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2556, Page(s) 1–18

Abstract: The glycocalyx is a layer of glycans that covers the surface of every cell. Glycans are covalently attached to proteins and lipids, and are classified into subclasses such as N-linked glycans, glycosaminoglycans, glycosphingolipid-glycans, free ... ...

Abstract	The glycocalyx is a layer of glycans that covers the surface of every cell. Glycans are covalently attached to proteins and lipids, and are classified into subclasses such as N-linked glycans, glycosaminoglycans, glycosphingolipid-glycans, free oligosaccharides, and O-linked glycans according to their biosynthetic pathways. These complex glycans affect various biological and pathological processes, such as cell growth, differentiation, and adhesion. During infection, bacteria and viruses often use glycans to recognize and attack host cells. In this chapter, we describe detailed protocols to prepare glycans, and perform comprehensive cellular glycomic analysis using glycoblotting and β-elimination with pyrazolone methods.
MeSH term(s)	Cell Differentiation ; Glycoproteins ; Glycosaminoglycans ; Glycosphingolipids ; Pyrazolones
Chemical Substances	Glycoproteins ; Glycosaminoglycans ; Glycosphingolipids ; Pyrazolones
Language	English
Publishing date	2022-09-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2635-1_1
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Article ; Online: Comprehensive Glycan Analysis of Sphingolipids in Human Serum/Plasma.

Hanamatsu, Hisatoshi / Nishikaze, Takashi / Furukawa, Jun-Ichi

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2613, Page(s) 289–299

Abstract: Glycosphingolipids (GSLs) are glycolipids with ceramide and carbohydrate head groups that play an important role in numerous biological processes. Previously, we performed GSL-glycan analysis of various cell lines and virus-infected cells using a ... ...

Abstract	Glycosphingolipids (GSLs) are glycolipids with ceramide and carbohydrate head groups that play an important role in numerous biological processes. Previously, we performed GSL-glycan analysis of various cell lines and virus-infected cells using a glycoblotting approach. Recently, we developed several methods for sialic acid linkage-specific chemical modification to distinguish sialylated glycan isomers by mass spectrometry. In this chapter, we describe a method for analyzing GSL-glycans in human serum/plasma using glycoblotting combined with aminolysis-SALSA (sialic acid linkage-specific alkylamidation) and lactone-driven ester-to-amide derivatization (LEAD)-SALSA for comprehensive and detailed structural glycomics.
MeSH term(s)	Humans ; Sphingolipids ; N-Acetylneuraminic Acid ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Glycosphingolipids/metabolism ; Polysaccharides/chemistry
Chemical Substances	Sphingolipids ; N-Acetylneuraminic Acid (GZP2782OP0) ; Glycosphingolipids ; Polysaccharides
Language	English
Publishing date	2022-12-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2910-9_21
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Article ; Online: Comprehensive and Comparative Structural Glycome Analysis in Mouse Epiblast-like Cells.

Pecori, Federico / Hanamatsu, Hisatoshi / Furukawa, Jun-Ichi / Nishihara, Shoko

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2490, Page(s) 179–193

Abstract: Glycosylation is one of the most abundant posttranslational modifications and is involved in a wide range of cellular processes. Glycome diversity in mammals is generated by the action of over 200 distinct glycosyltransferases and related enzymes. ... ...

Abstract	Glycosylation is one of the most abundant posttranslational modifications and is involved in a wide range of cellular processes. Glycome diversity in mammals is generated by the action of over 200 distinct glycosyltransferases and related enzymes. Nevertheless, glycosylation dynamics are tightly coordinated to allow proper organismal development. Here, using mouse embryonic stem cells (mESCs) and mouse epiblast-like cells (mEpiLCs) as model systems, we describe a robust protocol that allows comprehensive and comparative structural analysis of the glycome.
MeSH term(s)	Animals ; Cell Line ; Embryonic Stem Cells ; Germ Layers ; Mammals ; Mice ; Mouse Embryonic Stem Cells ; Pluripotent Stem Cells
Language	English
Publishing date	2022-04-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2281-0_13
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Article ; Online: Articular cartilage corefucosylation regulates tissue resilience in osteoarthritis.

Homan, Kentaro / Onodera, Tomohiro / Hanamatsu, Hisatoshi / Furukawa, Jun-Ichi / Momma, Daisuke / Matsuoka, Masatake / Iwasaki, Norimasa

eLife

2024 Volume 12

Abstract: This study aimed to investigate the glycan structural changes that occur before histological degeneration in osteoarthritis (OA) and to determine the mechanism by which these glycan conformational changes affect cartilage degeneration. An OA model was ... ...

Abstract	This study aimed to investigate the glycan structural changes that occur before histological degeneration in osteoarthritis (OA) and to determine the mechanism by which these glycan conformational changes affect cartilage degeneration. An OA model was established in rabbits using mannosidase injection, which reduced high-mannose type N-glycans and led to cartilage degeneration. Further analysis of glycome in human OA cartilage identified specific corefucosylated N-glycan expression patterns. Inhibition of N-glycan corefucosylation in mice resulted in unrecoverable cartilage degeneration, while cartilage-specific blocking of corefucosylation led to accelerated development of aging-associated and instability-induced OA models. We conclude that α1,6 fucosyltransferase is required postnatally to prevent preosteoarthritic deterioration of articular cartilage. These findings provide a novel definition of early OA and identify glyco-phenotypes of OA cartilage, which may distinguish individuals at higher risk of progression.
MeSH term(s)	Humans ; Rabbits ; Animals ; Mice ; Cartilage, Articular/metabolism ; Resilience, Psychological ; Osteoarthritis/metabolism ; Aging ; Polysaccharides/metabolism ; Disease Models, Animal
Chemical Substances	Polysaccharides
Language	English
Publishing date	2024-03-11
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.92275
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Article ; Online: Simultaneous and sialic acid linkage-specific N- and O-linked glycan analysis by ester-to-amide derivatization.

Hanamatsu, Hisatoshi / Miura, Yoshiaki / Nishikaze, Takashi / Yokota, Ikuko / Homan, Kentaro / Onodera, Tomohiro / Hayakawa, Yoshihiro / Iwasaki, Norimasa / Furukawa, Jun-Ichi

Glycoconjugate journal

2023 Volume 40, Issue 2, Page(s) 259–267

Abstract: Characterization of O-glycans linked to serine or threonine residues in glycoproteins has mostly been achieved using chemical reaction approaches because there are no known O-glycan-specific endoglycosidases. Most O-glycans are modified with sialic acid ... ...

Abstract	Characterization of O-glycans linked to serine or threonine residues in glycoproteins has mostly been achieved using chemical reaction approaches because there are no known O-glycan-specific endoglycosidases. Most O-glycans are modified with sialic acid residues at the non-reducing termini through various linkages. In this study, we developed a novel approach for sialic acid linkage-specific O-linked glycan analysis through lactone-driven ester-to-amide derivatization combined with non-reductive β-elimination in the presence of hydroxylamine. O-glycans released by non-reductive β-elimination were efficiently purified using glycoblotting via chemoselective ligation between carbohydrates and a hydrazide-functionalized polymer, followed by modification of methyl or ethyl ester groups of sialic acid residues on solid-phase. In-solution lactone-driven ester-to-amide derivatization of ethyl-esterified O-glycans was performed, and the resulting sialylated glycan isomers were discriminated by mass spectrometry. In combination with PNGase F digestion, we carried out simultaneous, quantitative, and sialic acid linkage-specific N- and O-linked glycan analyses of a model glycoprotein and human cartilage tissue. This novel glycomic approach will facilitate detailed characterization of biologically relevant sialylated N- and O-glycans on glycoproteins.
MeSH term(s)	Humans ; N-Acetylneuraminic Acid/chemistry ; Esters ; Glycoproteins/chemistry ; Polysaccharides/chemistry ; Lactones
Chemical Substances	N-Acetylneuraminic Acid (GZP2782OP0) ; Esters ; Glycoproteins ; Polysaccharides ; Lactones
Language	English
Publishing date	2023-03-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	283770-5
ISSN	1573-4986 ; 0282-0080
ISSN (online)	1573-4986
ISSN	0282-0080
DOI	10.1007/s10719-023-10109-8
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Article ; Online: Characterization of galactosyltransferase and sialyltransferase genes mediating the elongation of the extracellular O-GlcNAc glycans.

Tsukamoto, Yohei / Tsukamoto, Natsumi / Saiki, Wataru / Tashima, Yuko / Furukawa, Jun-Ichi / Kizuka, Yasuhiko / Narimatsu, Yoshiki / Clausen, Henrik / Takeuchi, Hideyuki / Okajima, Tetsuya

Biochemical and biophysical research communications

2024 Volume 703, Page(s) 149610

Abstract: O-GlcNAc is a unique post-translational modification found in cytoplasmic, nuclear, and mitochondrial proteins. In a limited number of extracellular proteins, O-GlcNAc modifications occur through the action of EOGT, which specifically modifies subsets of ...

Abstract	O-GlcNAc is a unique post-translational modification found in cytoplasmic, nuclear, and mitochondrial proteins. In a limited number of extracellular proteins, O-GlcNAc modifications occur through the action of EOGT, which specifically modifies subsets of epidermal growth factor-like (EGF) domain-containing proteins such as Notch receptors. The abnormalities due to EOGT mutations in mice and humans and the increased EOGT expression in several cancers signify the importance of EOGT pathophysiology and extracellular O-GlcNAc. Unlike intracellular O-GlcNAc monosaccharides, extracellular O-GlcNAc extends to form elongated glycan structures. However, the enzymes involved in the O-GlcNAc glycan extension have not yet been reported. In our study, we comprehensively screened potential galactosyltransferase and sialyltransferase genes related to the canonical O-GlcNAc glycan pathway and revealed the essential roles of B4GALT1 and ST3GAL4 in O-GlcNAc glycan elongation in human HEK293 cells. These findings were confirmed by sequential glycosylation of Drosophila EGF20 in vitro by EOGT, β4GalT-1, and ST3Gal-IV. Thus, the findings from our study throw light on the specific glycosyltransferases that mediate O-GlcNAc glycan elongation in human HEK293 cells.
MeSH term(s)	Humans ; Animals ; Mice ; HEK293 Cells ; Acetylglucosamine/metabolism ; Receptors, Notch/metabolism ; Galactosyltransferases/genetics ; Glycosyltransferases ; Drosophila/metabolism ; Sialyltransferases/genetics ; Polysaccharides
Chemical Substances	Acetylglucosamine (V956696549) ; Receptors, Notch ; Galactosyltransferases (EC 2.4.1.-) ; Glycosyltransferases (EC 2.4.-) ; Sialyltransferases (EC 2.4.99.-) ; Polysaccharides
Language	English
Publishing date	2024-02-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2024.149610
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Zs.A 116: Show issues

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Article ; Online: Toolbox Accelerating Glycomics (TAG): Improving Large-Scale Serum Glycomics and Refinement to Identify SALSA-Modified and Rare Glycans.

Miura, Nobuaki / Hanamatsu, Hisatoshi / Yokota, Ikuko / Akasaka-Manya, Keiko / Manya, Hiroshi / Endo, Tamao / Shinohara, Yasuro / Furukawa, Jun-Ichi

International journal of molecular sciences

2022 Volume 23, Issue 21

Abstract: Glycans are involved in many fundamental cellular processes such as growth, differentiation, and morphogenesis. However, their broad structural diversity makes analysis difficult. Glycomics via mass spectrometry has focused on the composition of glycans, ...

Abstract	Glycans are involved in many fundamental cellular processes such as growth, differentiation, and morphogenesis. However, their broad structural diversity makes analysis difficult. Glycomics via mass spectrometry has focused on the composition of glycans, but informatics analysis has not kept pace with the development of instrumentation and measurement techniques. We developed Toolbox Accelerating Glycomics (TAG), in which glycans can be added manually to the glycan list that can be freely designed with labels and sialic acid modifications, and fast processing is possible. In the present work, we improved TAG for large-scale analysis such as cohort analysis of serum samples. The sialic acid linkage-specific alkylamidation (SALSA) method converts differences in linkages such as α2,3- and α2,6-linkages of sialic acids into differences in mass. Glycans modified by SALSA and several structures discovered in recent years were added to the glycan list. A routine to generate calibration curves has been implemented to explore quantitation. These improvements are based on redefinitions of residues and glycans in the TAG List to incorporate information on glycans that could not be attributed because it was not assumed in the previous version of TAG. These functions were verified through analysis of purchased sera and 74 spectra with linearity at the level of R2 > 0.8 with 81 estimated glycan structures obtained including some candidate of rare glycans such as those with the N,N’-diacetyllactosediamine structure, suggesting they can be applied to large-scale analyses.
MeSH term(s)	Humans ; Glycomics/methods ; N-Acetylneuraminic Acid ; Polysaccharides/chemistry ; Sialic Acids/chemistry ; Mass Spectrometry
Chemical Substances	N-Acetylneuraminic Acid (GZP2782OP0) ; Polysaccharides ; Sialic Acids
Language	English
Publishing date	2022-10-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms232113097
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Article ; Online: Simultaneous determination of heparan sulfate, chondroitin/dermatan sulfates, and hyaluronan glycosaminoglycan disaccharides by high-performance liquid chromatography using a reverse-phase column with adamantyl groups.

Hanamatsu, Hisatoshi / Makino, Satoshi / Ohara, Masatsugu / Suda, Goki / Yokota, Ikuko / Nishihara, Shoko / Sakamoto, Naoya / Furukawa, Jun-Ichi

Journal of chromatography. A

2022 Volume 1689, Page(s) 463748

Abstract: Glycosaminoglycans (GAGs), which are one of the major components of proteoglycans, play a pivotal role in physiological processes such as signal transduction, cell adhesion, growth, and differentiation. Characterization of GAGs is challenging due to the ... ...

Abstract	Glycosaminoglycans (GAGs), which are one of the major components of proteoglycans, play a pivotal role in physiological processes such as signal transduction, cell adhesion, growth, and differentiation. Characterization of GAGs is challenging due to the tremendous structural diversity of heteropolysaccharides with numerous sulfate or carboxyl groups. In this present study, we examined the analysis of 2-aminobenzamide (2-AB) labeled GAG disaccharides by high-performance liquid chromatography (HPLC) using a reverse-phase (RP)-column with adamantyl groups. Under the analytical conditions, 17 types of 2-AB labeled GAG disaccharides derived from heparan sulfate, chondroitin/dermatan sulfates, and hyaluronan were sequentially separated in a single analysis. The analysis time was fast with high retention time reproducibility. Moreover, the RP-HPLC column with adamantyl groups allowed the quantification of GAGs in various biological samples, such as serum, cultured cells, and culture medium.
MeSH term(s)	Glycosaminoglycans/chemistry ; Chondroitin Sulfates/chemistry ; Hyaluronic Acid/analysis ; Hyaluronic Acid/chemistry ; Dermatan Sulfate/analysis ; Dermatan Sulfate/chemistry ; Dermatan Sulfate/metabolism ; Chromatography, High Pressure Liquid/methods ; Disaccharides/chemistry ; Reproducibility of Results ; Heparitin Sulfate/analysis
Chemical Substances	Glycosaminoglycans ; Chondroitin Sulfates (9007-28-7) ; Hyaluronic Acid (9004-61-9) ; Dermatan Sulfate (24967-94-0) ; Disaccharides ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2022-12-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1171488-8
ISSN	1873-3778 ; 0021-9673
ISSN (online)	1873-3778
ISSN	0021-9673
DOI	10.1016/j.chroma.2022.463748
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Zs.A 813: Show issues

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Article ; Online: Glycosphingolipid GM3 prevents albuminuria and podocytopathy induced by anti-nephrin antibody.

Kawashima, Nagako / Naito, Shokichi / Hanamatsu, Hisatoshi / Nagane, Masaki / Takeuchi, Yasuo / Furukawa, Jun-Ichi / Iwasaki, Norimasa / Yamashita, Tadashi / Nakayama, Ken-Ichi

Scientific reports

2022 Volume 12, Issue 1, Page(s) 16058

Abstract: Podocytopathy, which is characterized by injury to podocytes, frequently causes proteinuria or nephrotic syndrome. There is currently a paucity of effective therapeutic drugs to treat proteinuric kidney disease. Recent research suggests the possibility ... ...

Abstract	Podocytopathy, which is characterized by injury to podocytes, frequently causes proteinuria or nephrotic syndrome. There is currently a paucity of effective therapeutic drugs to treat proteinuric kidney disease. Recent research suggests the possibility that glycosphingolipid GM3 maintains podocyte function by acting on various molecules including nephrin, but its mechanism of action remains unknown. Here, various analyses were performed to examine the potential relationship between GM3 and nephrin, and the function of GM3 in podocytes using podocytopathy mice, GM3 synthase gene knockout mice, and nephrin injury cells. Reduced amounts of GM3 and nephrin were observed in podocytopathy mice. Intriguingly, this reduction of GM3 and nephrin, as well as albuminuria, were inhibited by administration of valproic acid. However, when the same experiment was performed using GM3 synthase gene knockout mice, valproic acid administration did not inhibit albuminuria. Equivalent results were obtained in model cells. These findings indicate that GM3 acts with nephrin in a collaborative manner in the cell membrane. Taken together, elevated levels of GM3 stabilize nephrin, which is a key molecule of the slit diaphragm, by enhancing the environment of the cell membrane and preventing albuminuria. This study provides novel insight into new drug discovery, which may offer a new therapy for kidney disease with albuminuria.
MeSH term(s)	Albuminuria/metabolism ; Animals ; Glycosphingolipids/metabolism ; Mice ; Podocytes/metabolism ; Proteinuria/metabolism ; Valproic Acid/metabolism ; Valproic Acid/pharmacology
Chemical Substances	Glycosphingolipids ; Valproic Acid (614OI1Z5WI)
Language	English
Publishing date	2022-09-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-20265-w
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Article ; Online: Establishment of the removal method of undifferentiated induced pluripotent stem cells coexisting with chondrocytes using R-17F antibody.

Miyazaki, Takuji / Hanamatsu, Hisatoshi / Onodera, Tomohiro / Furukawa, Jun-Ichi / Xu, Liang / Homan, Kentaro / Baba, Rikiya / Kawasaki, Toshisuke / Iwasaki, Norimasa

Regenerative medicine

2022 Volume 17, Issue 11, Page(s) 793–803

Abstract: Aim: ...

Abstract	Aim:
MeSH term(s)	Animals ; Antibodies ; Cell Differentiation ; Chondrocytes ; Glycosphingolipids ; Induced Pluripotent Stem Cells ; Mice ; Teratoma
Chemical Substances	Antibodies ; Glycosphingolipids
Language	English
Publishing date	2022-09-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2274500-2
ISSN	1746-076X ; 1746-0751
ISSN (online)	1746-076X
ISSN	1746-0751
DOI	10.2217/rme-2022-0010
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Zs.A 6627: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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