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Article ; Online: Development of M2BPGi: a novel fibrosis serum glyco-biomarker for chronic hepatitis/cirrhosis diagnostics.

Narimatsu, Hisashi

2015 Volume 12, Issue 6, Page(s) 683–693

Abstract: Many proteins in the living body are glycoproteins, which present glycans linked on their surface. Glycan structures reflect the degree of cell differentiation or canceration and are cell specific. These characteristics are advantageous in the ... ...

Abstract	Many proteins in the living body are glycoproteins, which present glycans linked on their surface. Glycan structures reflect the degree of cell differentiation or canceration and are cell specific. These characteristics are advantageous in the development of various disease biomarkers. Glycoprotein-based biomarkers (glyco-biomarkers) are developed by utilizing the specific changes in the glycan structure on a glycoprotein secreted from the diseased cells of interest. Therefore, quantification of the altered glycan structures is the key to developing a new glyco-biomarker. Glycoscience is a relatively new area of molecular science, and recent advancement of glycotechnologies is remarkable. In the author's institute, new glycoscience technologies have been designed to be efficiently utilized for the development of new diagnostic agents. This paper introduces a strategy for glyco-biomarker development, which was successfully applied in the development of Wisteria floribunda agglutinin-positive Mac-2 binding protein M2BPGi, a liver fibrosis marker now commercially available for clinical use.
MeSH term(s)	Amino Acid Sequence ; Animals ; Biomarkers/blood ; Glycomics/methods ; Glycoproteins/blood ; Glycoproteins/chemistry ; Hepatitis/blood ; Humans ; Liver Cirrhosis/blood ; Molecular Sequence Data
Chemical Substances	Biomarkers ; Glycoproteins
Language	English
Publishing date	2015
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2299100-1
ISSN	1744-8387 ; 1478-9450
ISSN (online)	1744-8387
ISSN	1478-9450
DOI	10.1586/14789450.2015.1084874
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Article ; Online: Strategy for development of clinically useful glyco-biomarkers.

Narimatsu, Hisashi

Glycoconjugate journal

2014 Volume 31, Issue 6-7, Page(s) 403–407

Abstract: Recent advancements in proteomics technology have stimulated the widespread research and development in the area of biomarker discovery using mass spectrometry (MS). The final goal of biomarker discovery and development is to establish clinically useful ... ...

Abstract	Recent advancements in proteomics technology have stimulated the widespread research and development in the area of biomarker discovery using mass spectrometry (MS). The final goal of biomarker discovery and development is to establish clinically useful and reliable diagnostic methods for various diseases. Specific alterations in the nature and composition of glycans attached to proteins are seen during the development and progression of a number of diseases and disorders. Therefore, development of glyco-biomarkers, which detect disease-specific glycoproteins and changes in glycoforms, is gaining much attention. The combined use of multiple technologies, not solely MS, is the key to the discovery of clinically significant and reliable biomarkers. We have employed the combination of quantitative real-time polymerase chain reaction (PCR), lectin microarray, liquid chromatography/mass spectrometry-based technique with isotope-coded glycosylation site-specific tagging (IGOT-LC/MS), and bioinformatics to successfully develop a novel diagnostic kit for the quantitative evaluation of liver fibrosis. Efforts to develop highly effective glyco-biomarkers for other diseases are also currently underway.
MeSH term(s)	Biomarkers/metabolism ; Glycosylation ; Mass Spectrometry ; Real-Time Polymerase Chain Reaction
Chemical Substances	Biomarkers
Language	English
Publishing date	2014-09-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	283770-5
ISSN	1573-4986 ; 0282-0080
ISSN (online)	1573-4986
ISSN	0282-0080
DOI	10.1007/s10719-014-9544-8
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Article ; Online: Chondroitin sulfate modification of CSPG4 regulates the maintenance and differentiation of glioma-initiating cells via integrin-associated signaling.

Niibori-Nambu, Akiko / Yamasaki, Yoshimune / Kobayashi, Daiki / Angata, Kiyohiko / Kuno, Atsushi / Panawan, Orasa / Silsirivanit, Atit / Narimatsu, Hisashi / Araki, Norie

The Journal of biological chemistry

2024 Volume 300, Issue 3, Page(s) 105706

Abstract: Glioma stem cell/glioma-initiating cell (GIC) and their niches are considered responsible for the therapeutic resistance and recurrence of malignant glioma. To clarify the molecular mechanisms of GIC maintenance/differentiation, we performed a unique ... ...

Abstract	Glioma stem cell/glioma-initiating cell (GIC) and their niches are considered responsible for the therapeutic resistance and recurrence of malignant glioma. To clarify the molecular mechanisms of GIC maintenance/differentiation, we performed a unique integrated proteogenomics utilizing GIC clones established from patient tumors having the potential to develop glioblastoma. After the integration and extraction of the transcriptomics/proteomics data, we found that chondroitin sulfate proteoglycan 4 (CSPG4) and its glycobiosynthetic enzymes were significantly upregulated in GICs. Glyco-quantitative PCR array revealed that chondroitin sulfate (CS) biosynthetic enzymes, such as xylosyltransferase 1 (XYLT1) and carbohydrate sulfotransferase 11, were significantly downregulated during serum-induced GIC differentiation. Simultaneously, the CS modification on CSPG4 was characteristically decreased during the differentiation and also downregulated by XYLT1 knockdown. Notably, the CS degradation on CSPG4 by ChondroitinaseABC treatment dramatically induced GIC differentiation, which was significantly inhibited by the addition of CS. GIC growth and differentiation ability were significantly suppressed by CSPG4 knockdown, suggesting that CS-CSPG4 is an important factor in GIC maintenance/differentiation. To understand the molecular function of CS-CSPG4, we analyzed its associating proteins in GICs and found that CSPG4, but not CS-CSPG4, interacts with integrin αV during GIC differentiation. This event sequentially upregulates integrin-extracellular signal-regulated kinase signaling, which can be inhibited by cyclic-RGD (Arg-Gly-Asp) integrin αV inhibitor. These results indicate that CS-CSPG4 regulates the GIC microenvironment for GIC maintenance/differentiation via the CS moiety, which controls integrin signaling. This study demonstrates a novel function of CS on CSPG4 as a niche factor, so-called "glyco-niche" for GICs, and suggests that CS-CSPG4 could be a potential target for malignant glioma.
MeSH term(s)	Humans ; Chondroitin Sulfate Proteoglycans/metabolism ; Chondroitin Sulfates/metabolism ; Glioma/metabolism ; Glioma/pathology ; Integrin alphaV ; Membrane Proteins/metabolism ; Tumor Microenvironment
Chemical Substances	Chondroitin Sulfate Proteoglycans ; Chondroitin Sulfates (9007-28-7) ; CSPG4 protein, human ; Integrin alphaV ; Membrane Proteins
Language	English
Publishing date	2024-02-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2024.105706
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Article ; Online: Serum O-glycosylated hepatitis B surface antigen levels in patients with chronic hepatitis B during nucleos(t)ide analog therapy.

Murata, Ayato / Angata, Kiyohiko / Sogabe, Maki / Sato, Shunsuke / Ichida, Takafumi / Narimatsu, Hisashi / Genda, Takuya

BMC gastroenterology

2022 Volume 22, Issue 1, Page(s) 270

Abstract: Background: Serum hepatitis B surface antigen (HBsAg) is a component of both hepatitis B virus (HBV) virions and non-infectious subviral particles (SVPs). Recently, O-glycosylation of the PreS2 domain of middle HBsAg protein has been identified as a ... ...

Abstract	Background: Serum hepatitis B surface antigen (HBsAg) is a component of both hepatitis B virus (HBV) virions and non-infectious subviral particles (SVPs). Recently, O-glycosylation of the PreS2 domain of middle HBsAg protein has been identified as a distinct characteristic of genotype C HBV virions versus SVPs. This study aimed to evaluate serum O-glycosylated HBsAg levels in patients with chronic hepatitis B (CHB) treated with nucleos(t)ide analogs (NAs). Methods: Forty-seven treatment-naïve patients with genotype C CHB were retrospectively enrolled. Serum O-glycosylated HBsAg levels at baseline and after 48 weeks of NA therapy were quantified by immunoassay using a monoclonal antibody against the O-glycosylated PreS2 domain of middle HBsAg, and their correlations with conventional HBV marker levels were analyzed. Results: At baseline, the serum O-glycosylated HBsAg levels were significantly correlated with the HBV DNA (P = 0.004), HBsAg (P = 0.005), and hepatitis B-core related antigen (HBcrAg, P = 0.001) levels. Both HBV DNA and O-glycosylated HBsAg levels were decreased after 48 weeks of NA therapy. The significant correlation of the O-glycosylated HBsAg level with the HBsAg or HBcrAg level was lost in patients who achieved undetectable HBV DNA (HBsAg, P = 0.429; HBcrAg, P = 0.065). Immunoprecipitation assays demonstrated that HBV DNA and RNA were detected in the O-glycosylated HBsAg-binding serum fraction, and the proportion of HBV RNA increased during NA therapy (P = 0.048). Conclusion: Serum O-glycosylated HBsAg levels change during NA therapy and may reflect combined levels of serum HBV DNA and RNA virions. An O-glycosylated HBsAg-based immunoassay may provide a novel means to monitor viral kinetics during NA therapy.
MeSH term(s)	DNA, Viral ; Glycosylation ; Hepatitis B Surface Antigens ; Hepatitis B, Chronic/drug therapy ; Humans ; RNA ; Retrospective Studies
Chemical Substances	DNA, Viral ; Hepatitis B Surface Antigens ; RNA (63231-63-0)
Language	English
Publishing date	2022-05-31
Publishing country	England
Document type	Journal Article
ZDB-ID	2041351-8
ISSN	1471-230X ; 1471-230X
ISSN (online)	1471-230X
ISSN	1471-230X
DOI	10.1186/s12876-022-02352-4
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Article ; Online ; Conference proceedings: 8th HUPO World Congress: the Human Disease Glycomics/Proteomics Initiative (HGPI) Session 26 September 2009, Toronto, Canada.

Narimatsu, Hisashi

Proteomics

2010 Volume 10, Issue 10, Page(s) 1899–1902

Abstract: The Human Disease Glycomics/Proteomics Initiative (HGPI) Session at the HUPO World Congress was held in Toronto on 26 September 2009. In this report, we summarize the presentation of the HGPI workshop as follows: (i) The results of the past HGPI pilot ... ...

Abstract	The Human Disease Glycomics/Proteomics Initiative (HGPI) Session at the HUPO World Congress was held in Toronto on 26 September 2009. In this report, we summarize the presentation of the HGPI workshop as follows: (i) The results of the past HGPI pilot studies (first and second) in which we analyzed N- and O-linked glycans using standard glycoproteins (i.e. first: N-linked glycan analysis of transferrin and IgG; second: O-linked glycan analysis of IgA). (ii) The recent progresses of the current HGPI third pilot study. The third analytical pilot study is in progress to perform the two tasks, which are glycan structural analysis and identification of proteins which carry specific carbohydrate antigen (Lewis X antigen) using cancer cells (i.e. L428, U937, and SK-N-SH), under the theme of "Glyco-Biomarker Discovery". Finally, recently advanced glycomic and glycoproteomic analyses were also reported.
MeSH term(s)	Animals ; Canada ; Glycomics ; Humans ; Proteomics ; Societies, Scientific ; Time Factors
Language	English
Publishing date	2010-05
Publishing country	Germany
Document type	Congresses
ZDB-ID	2032093-0
ISSN	1615-9861 ; 1615-9853
ISSN (online)	1615-9861
ISSN	1615-9853
DOI	10.1002/pmic.201090035
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Zs.A 5386: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.A 1868: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Wisteria floribunda agglutinin positive glycobiomarkers: a unique lectin as a serum biomarker probe in various diseases.

Narimatsu, Hisashi / Sato, Takashi

Expert review of proteomics

2017 Volume 15, Issue 2, Page(s) 183–190

Abstract: Introduction: Serum proteins are generally glycosylated and solubilized, and are thus present as glycoproteins. The glycan structure of glycoproteins reflects cell differentiation status; glycan structures generated by diseased cells are distinguishable ...

Abstract	Introduction: Serum proteins are generally glycosylated and solubilized, and are thus present as glycoproteins. The glycan structure of glycoproteins reflects cell differentiation status; glycan structures generated by diseased cells are distinguishable from those produced by healthy cells. Proteins may therefore serve as markers of tissues that secrete them. Several strategies for the identification of novel serum biomarkers using a combination of glycoscience-based technologies have been recently proposed. The selection of lectins for use as probes for identification of altered glycan structures represents a critical step. Areas covered: This review describes the identification of Wisteria floribunda agglutinin (WFA) as a probe that recognizes the altered glycan structure of glycoproteins secreted by diseased cells. WFA may be employed as a probe for several diseases, e.g., liver fibrosis, liver cirrhosis, prostate cancer, ovarian cancer, and IgA nephropathy. The advantage of employing WFA as a serum biomarker probe is that only very small amounts of WFA-positive glycoproteins are present in serum; therefore, WFA background in serum is very low. Expert commentary: Based on the findings to date, several WFA-positive serum biomarkers may be measured without pre-purification of target glycoproteins, indicating their utility as serum biomarkers in patients with various diseases.
MeSH term(s)	Biomarkers/blood ; Glomerulonephritis, IGA/blood ; Glycomics/methods ; Humans ; Liver Cirrhosis/blood ; Plant Lectins/immunology ; Receptors, N-Acetylglucosamine/immunology
Chemical Substances	Biomarkers ; Plant Lectins ; Receptors, N-Acetylglucosamine ; wisteria lectin
Language	English
Publishing date	2017-12-21
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2299100-1
ISSN	1744-8387 ; 1478-9450
ISSN (online)	1744-8387
ISSN	1478-9450
DOI	10.1080/14789450.2018.1419066
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Article ; Online: Association between the expression of core 3 synthase and survival outcomes of patients with cholangiocarcinoma.

Boottanun, Patcharaporn / Ino, Yoshinori / Shimada, Kazuaki / Hiraoka, Nobuyoshi / Angata, Kiyohiko / Narimatsu, Hisashi

Oncology letters

2021 Volume 22, Issue 5, Page(s) 760

Abstract: Cholangiocarcinoma (CCA) is a highly aggressive and metastatic type of malignant carcinoma that is associated with high mortality rates and is difficult to detect at early stages. Core 3 structure is a mucin- ... ...

Abstract	Cholangiocarcinoma (CCA) is a highly aggressive and metastatic type of malignant carcinoma that is associated with high mortality rates and is difficult to detect at early stages. Core 3 structure is a mucin-type
Language	English
Publishing date	2021-09-03
Publishing country	Greece
Document type	Journal Article
ZDB-ID	2573196-8
ISSN	1792-1082 ; 1792-1074
ISSN (online)	1792-1082
ISSN	1792-1074
DOI	10.3892/ol.2021.13021
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Book: Rinshō tōsa baiomākā no kaihatsu

Narimatsu, Hisashi

tōsa kinō no kaimei to sono ōyō

(Idenshi igaku mook, ; 11)

2008

Abstract: This book, written by leading researchers in the world, can be used as a guide to carbohydrate function research and their application, including carbohydrate structure analysis, clinical biomarker discoveries by advanced technology in glycosylation, ... ...

Author's details	henshū Narimatsu Hisashi
Series title	Idenshi igaku mook, ; 11
Abstract	This book, written by leading researchers in the world, can be used as a guide to carbohydrate function research and their application, including carbohydrate structure analysis, clinical biomarker discoveries by advanced technology in glycosylation, functional analysis of carbohydrate with applications with advanced technology, and clinical applications to drug discovery and medicine.
MeSH term(s)	Carbohydrates/genetics ; Biomarkers ; Glycosylation
Language	Japanese
Size	304 p. :, ill. ;, 26 cm.
Publisher	Medikaru Dū
Publishing place	Ōsaka
Document type	Book
ISBN	9784944157419 ; 494415741X
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: GGDonto ontology as a knowledge-base for genetic diseases and disorders of glycan metabolism and their causative genes.

Solovieva, Elena / Shikanai, Toshihide / Fujita, Noriaki / Narimatsu, Hisashi

Journal of biomedical semantics

2018 Volume 9, Issue 1, Page(s) 14

Abstract: Background: Inherited mutations in glyco-related genes can affect the biosynthesis and degradation of glycans and result in severe genetic diseases and disorders. The Glyco-Disease Genes Database (GDGDB), which provides information about these diseases ... ...

Abstract	Background: Inherited mutations in glyco-related genes can affect the biosynthesis and degradation of glycans and result in severe genetic diseases and disorders. The Glyco-Disease Genes Database (GDGDB), which provides information about these diseases and disorders as well as their causative genes, has been developed by the Research Center for Medical Glycoscience (RCMG) and released in April 2010. GDGDB currently provides information on about 80 genetic diseases and disorders caused by single-gene mutations in glyco-related genes. Many biomedical resources provide information about genetic disorders and genes involved in their pathogenesis, but resources focused on genetic disorders known to be related to glycan metabolism are lacking. With the aim of providing more comprehensive knowledge on genetic diseases and disorders of glycan biosynthesis and degradation, we enriched the content of the GDGDB database and improved the methods for data representation. Results: We developed the Genetic Glyco-Diseases Ontology (GGDonto) and a RDF/SPARQL-based user interface using Semantic Web technologies. In particular, we represented the GGDonto content using Semantic Web languages, such as RDF, RDFS, SKOS, and OWL, and created an interactive user interface based on SPARQL queries. This user interface provides features to browse the hierarchy of the ontology, view detailed information on diseases and related genes, and find relevant background information. Moreover, it provides the ability to filter and search information by faceted and keyword searches. Conclusions: Focused on the molecular etiology, pathogenesis, and clinical manifestations of genetic diseases and disorders of glycan metabolism and developed as a knowledge-base for this scientific field, GGDonto provides comprehensive information on various topics, including links to aid the integration with other scientific resources. The availability and accessibility of this knowledge will help users better understand how genetic defects impact the metabolism of glycans as well as how this impaired metabolism affects various biological functions and human health. In this way, GGDonto will be useful in fields related to glycoscience, including cell biology, biotechnology, and biomedical, and pharmaceutical research.
MeSH term(s)	Databases, Genetic ; Disease/genetics ; Gene Ontology ; Internet ; Knowledge Bases ; Mutation ; Polysaccharides/biosynthesis ; Polysaccharides/metabolism ; User-Computer Interface
Chemical Substances	Polysaccharides
Language	English
Publishing date	2018-04-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2548651-2
ISSN	2041-1480 ; 2041-1480
ISSN (online)	2041-1480
ISSN	2041-1480
DOI	10.1186/s13326-018-0182-0
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Article ; Online: Correction to: Renal involvement of monoclonal immunoglobulin deposition disease associated with an unusual monoclonal immunoglobulin A glycan profile.

Kaneko, Shuzo / Usui, Joichi / Narimatsu, Yoshiki / Ito, Hiromi / Narimatsu, Hisashi / Hagiwara, Masahiro / Tsuruoka, Shuichi / Nagata, Michio / Yamagata, Kunihiro

Clinical and experimental nephrology

2022 Volume 26, Issue 7, Page(s) 733

Language	English
Publishing date	2022-03-18
Publishing country	Japan
Document type	Published Erratum
ZDB-ID	1338768-6
ISSN	1437-7799 ; 1342-1751
ISSN (online)	1437-7799
ISSN	1342-1751
DOI	10.1007/s10157-022-02212-1
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