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  1. AU="Maeshibu, Takako"
  2. AU=Soresina Annarosa AU=Soresina Annarosa
  3. AU=Torke Alexia M
  4. AU=Sun Chuan-Bin
  5. AU="Krystal, Mark R"
  6. AU="Jiang, Yuandong"
  7. AU=Daly Roger J
  8. AU="Sorenson, Michael D"
  9. AU="Ruiqiang Li"
  10. AU="Marini, Davide"
  11. AU="Tirabassi, Jill N"
  12. AU="Song, Seok-Hwan"
  13. AU="A. Hakeem Anwer"
  14. AU="O'Connell, Jeff R"
  15. AU="Elizabeth C. Saunders"
  16. AU="Pratima Verma"
  17. AU="Nomaguchi, Masako"
  18. AU="Hutson, Alan D"
  19. AU="Jarvis, Deborah"
  20. AU="Yilmaz, Sevdican Ustun"
  21. AU="Kreisel, Wolfgang"
  22. AU="Tracy R. Nichols, Ph.D."
  23. AU="Hellal, Faycel"
  24. AU="Steffen Koschmieder"
  25. AU="Hsin-Hui Yu"
  26. AU="Watanabe, Sadanori"
  27. AU="Swarts, Benjamin M"
  28. AU="Zang, Trinity"
  29. AU="Almayahi, Basim A"
  30. AU="Lupke, Madeleine"
  31. AU="Tweed, Conor"

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  1. Artikel: Translation and Validation Testing of the Constipation-Related Quality of Life Scale for Use in Japan.

    Hamaguchi, Sugihiro / Varma, Madhulika G / Nakagawa, Hiroaki / Ozaka, Akihiro / Shimizu, Sayaka / Maeshibu, Takako / Wakita, Takafumi / Green, Joseph / Fukuhara, Shunichi

    Cureus

    2023  Band 15, Heft 11, Seite(n) e48661

    Abstract: Introduction Establishing a scale that can easily be used to appropriately measure the impact of constipation on the quality of life in Japan is a first step toward addressing this important health issue. We developed a Japanese language version of the ... ...

    Abstract Introduction Establishing a scale that can easily be used to appropriately measure the impact of constipation on the quality of life in Japan is a first step toward addressing this important health issue. We developed a Japanese language version of the Constipation-Related Quality of Life scale, which has 18 items and four subscales, and then subjected it to validation testing. Methods After translation according to a standardized and commonly used procedure, the Japanese version of the Constipation-Related Quality of Life scale was administered to people in an internet-based panel, in March 2023. The participants included 1,276 adults who had constipation (median age: 60 years, 690 {54.1%} males). The outcome measures included the Constipation-Related Quality of Life scale, the Constipation Scoring System (an index of constipation severity), and the Medical Outcomes Study (MOS) eight-item short form (a measure of generic health-related quality of life). Results Confirmatory factor analysis (four-factor model) indicated that all 18 Constipation-Related Quality of Life items had sufficiently high factor loadings (0.686-0.926). Internal consistency reliability was high (Cronbach's alpha: 0.86-0.94). Scores on the social impairment subscale and on the distress subscale of the Constipation-Related Quality of Life scale were significantly worse in the participants who had worse scores on the social functioning and mental health domains, respectively, of the MOS eight-item short form, which indicates good concurrent validity. Regarding criterion-based validity, the four subscale scores differed significantly among the four constipation-severity groups. The four subscale scores were also 1.16-4.53 times more sensitive than the MOS eight-item short form's mental component score to differences among the four constipation-severity groups (relative validity: 1.16-4.53), which indicates good discriminant validity. Conclusion The Japanese version of the Constipation-Related Quality of Life scale can be used with confidence in its factor structure, its concurrent, criterion-based, and discriminant validity, and its internal consistency reliability.
    Sprache Englisch
    Erscheinungsdatum 2023-11-11
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2747273-5
    ISSN 2168-8184
    ISSN 2168-8184
    DOI 10.7759/cureus.48661
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: A bacterial sulfoglycosidase highlights mucin O-glycan breakdown in the gut ecosystem.

    Katoh, Toshihiko / Yamada, Chihaya / Wallace, Michael D / Yoshida, Ayako / Gotoh, Aina / Arai, Moe / Maeshibu, Takako / Kashima, Toma / Hagenbeek, Arno / Ojima, Miriam N / Takada, Hiromi / Sakanaka, Mikiyasu / Shimizu, Hidenori / Nishiyama, Keita / Ashida, Hisashi / Hirose, Junko / Suarez-Diez, Maria / Nishiyama, Makoto / Kimura, Ikuo /
    Stubbs, Keith A / Fushinobu, Shinya / Katayama, Takane

    Nature chemical biology

    2023  Band 19, Heft 6, Seite(n) 778–789

    Abstract: Mucinolytic bacteria modulate host-microbiota symbiosis and dysbiosis through their ability to degrade mucin O-glycans. However, how and to what extent bacterial enzymes are involved in the breakdown process remains poorly understood. Here we focus on a ... ...

    Abstract Mucinolytic bacteria modulate host-microbiota symbiosis and dysbiosis through their ability to degrade mucin O-glycans. However, how and to what extent bacterial enzymes are involved in the breakdown process remains poorly understood. Here we focus on a glycoside hydrolase family 20 sulfoglycosidase (BbhII) from Bifidobacterium bifidum, which releases N-acetylglucosamine-6-sulfate from sulfated mucins. Glycomic analysis showed that, in addition to sulfatases, sulfoglycosidases are involved in mucin O-glycan breakdown in vivo and that the released N-acetylglucosamine-6-sulfate potentially affects gut microbial metabolism, both of which were also supported by a metagenomic data mining analysis. Enzymatic and structural analysis of BbhII reveals the architecture underlying its specificity and the presence of a GlcNAc-6S-specific carbohydrate-binding module (CBM) 32 with a distinct sugar recognition mode that B. bifidum takes advantage of to degrade mucin O-glycans. Comparative analysis of the genomes of prominent mucinolytic bacteria also highlights a CBM-dependent O-glycan breakdown strategy used by B. bifidum.
    Mesh-Begriff(e) Mucins/metabolism ; Ecosystem ; Polysaccharides/metabolism ; Bacteria/metabolism
    Chemische Substanzen Mucins ; Polysaccharides
    Sprache Englisch
    Erscheinungsdatum 2023-03-02
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-023-01272-y
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel: Identification and characterization of a sulfoglycosidase from Bifidobacterium bifidum implicated in mucin glycan utilization

    Katoh, Toshihiko / Maeshibu, Takako / Kikkawa, Kei-ichi / Gotoh, Aina / Tomabechi, Yusuke / Nakamura, Motoharu / Liao, Wei-Hsiang / Yamaguchi, Masanori / Ashida, Hisashi / Yamamoto, Kenji / Katayama, Takane

    Bioscience, biotechnology, and biochemistry. 2017 Oct. 3, v. 81, no. 10

    2017  

    Abstract: Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-glycan degradation by ... ...

    Abstract Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-glycan degradation by bifidobacteria remains fragmentary, especially regarding how they decompose sulfated glycans, which are abundantly found in mucin sugar-chains. Here, we examined the abilities of several Bifidobacterium strains to degrade a sulfated glycan substrate and identified a 6-sulfo-β-d-N-acetylglucosaminidase, also termed sulfoglycosidase, encoded by bbhII from Bifidobacterium bifidum JCM 7004. A recombinant BbhII protein showed a substrate preference toward 6-sulfated and 3,4-disulfated N-acetylglucosamines over non-sulfated and 3-sulfated N-acetylglucosamines. The purified BbhII directly released 6-sulfated N-acetylglucosamine from porcine gastric mucin and the expression of bbhII was moderately induced in the presence of mucin. This de-capping activity may promote utilization of sulfated glycans of mucin by other bacteria including bifidobacteria, thereby establishing the symbiotic relationship between human and gut microbes.
    Schlagwörter Bifidobacterium bifidum ; N-acetylglucosamine ; biotechnology ; carbon ; humans ; intestines ; mucins ; polysaccharides ; substrate specificity ; swine ; symbionts ; symbiosis
    Sprache Englisch
    Erscheinungsverlauf 2017-1003
    Umfang p. 2018-2027.
    Erscheinungsort Taylor & Francis
    Dokumenttyp Artikel
    Anmerkung NAL-light
    ZDB-ID 1106450-x
    ISSN 1347-6947 ; 0916-8451
    ISSN (online) 1347-6947
    ISSN 0916-8451
    DOI 10.1080/09168451.2017.1361810
    Datenquelle NAL Katalog (AGRICOLA)

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  4. Artikel ; Online: A bacterial sulfoglycosidase highlights mucin O-glycan breakdown in the gut ecosystem

    Katoh, Toshihiko / Yamada, Chihaya / Wallace, Michael D. / Yoshida, Ayako / Gotoh, Aina / Arai, Moe / Maeshibu, Takako / Kashima, Toma / Hagenbeek, Arno / Ojima, Miriam N. / Takada, Hiromi / Sakanaka, Mikiyasu / Shimizu, Hidenori / Nishiyama, Keita / Ashida, Hisashi / Hirose, Junko / Suarez-Diez, Maria / Nishiyama, Makoto / Kimura, Ikuo /
    Stubbs, Keith A. / Fushinobu, Shinya / Katayama, Takane

    Nature Chemical Biology

    2023  Band 19

    Abstract: Mucinolytic bacteria modulate host–microbiota symbiosis and dysbiosis through their ability to degrade mucin O-glycans. However, how and to what extent bacterial enzymes are involved in the breakdown process remains poorly understood. Here we focus on a ... ...

    Abstract Mucinolytic bacteria modulate host–microbiota symbiosis and dysbiosis through their ability to degrade mucin O-glycans. However, how and to what extent bacterial enzymes are involved in the breakdown process remains poorly understood. Here we focus on a glycoside hydrolase family 20 sulfoglycosidase (BbhII) from Bifidobacterium bifidum, which releases N-acetylglucosamine-6-sulfate from sulfated mucins. Glycomic analysis showed that, in addition to sulfatases, sulfoglycosidases are involved in mucin O-glycan breakdown in vivo and that the released N-acetylglucosamine-6-sulfate potentially affects gut microbial metabolism, both of which were also supported by a metagenomic data mining analysis. Enzymatic and structural analysis of BbhII reveals the architecture underlying its specificity and the presence of a GlcNAc-6S-specific carbohydrate-binding module (CBM) 32 with a distinct sugar recognition mode that B. bifidum takes advantage of to degrade mucin O-glycans. Comparative analysis of the genomes of prominent mucinolytic bacteria also highlights a CBM-dependent O-glycan breakdown strategy used by B. bifidum. [Figure not available: see fulltext.].
    Schlagwörter Life Science
    Sprache Englisch
    Erscheinungsland nl
    Dokumenttyp Artikel ; Online
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  5. Artikel ; Online: Identification and characterization of a sulfoglycosidase from Bifidobacterium bifidum implicated in mucin glycan utilization.

    Katoh, Toshihiko / Maeshibu, Takako / Kikkawa, Kei-Ichi / Gotoh, Aina / Tomabechi, Yusuke / Nakamura, Motoharu / Liao, Wei-Hsiang / Yamaguchi, Masanori / Ashida, Hisashi / Yamamoto, Kenji / Katayama, Takane

    Bioscience, biotechnology, and biochemistry

    2017  Band 81, Heft 10, Seite(n) 2018–2027

    Abstract: Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-glycan degradation by ... ...

    Abstract Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-glycan degradation by bifidobacteria remains fragmentary, especially regarding how they decompose sulfated glycans, which are abundantly found in mucin sugar-chains. Here, we examined the abilities of several Bifidobacterium strains to degrade a sulfated glycan substrate and identified a 6-sulfo-β-d-N-acetylglucosaminidase, also termed sulfoglycosidase, encoded by bbhII from Bifidobacterium bifidum JCM 7004. A recombinant BbhII protein showed a substrate preference toward 6-sulfated and 3,4-disulfated N-acetylglucosamines over non-sulfated and 3-sulfated N-acetylglucosamines. The purified BbhII directly released 6-sulfated N-acetylglucosamine from porcine gastric mucin and the expression of bbhII was moderately induced in the presence of mucin. This de-capping activity may promote utilization of sulfated glycans of mucin by other bacteria including bifidobacteria, thereby establishing the symbiotic relationship between human and gut microbes.
    Mesh-Begriff(e) Acetylglucosaminidase/chemistry ; Acetylglucosaminidase/genetics ; Acetylglucosaminidase/metabolism ; Amino Acid Sequence ; Bifidobacterium bifidum/enzymology ; Bifidobacterium bifidum/genetics ; Bifidobacterium bifidum/metabolism ; Gene Expression Regulation, Bacterial ; Mucins/metabolism ; Polysaccharides/metabolism
    Chemische Substanzen Mucins ; Polysaccharides ; Acetylglucosaminidase (EC 3.2.1.52)
    Sprache Englisch
    Erscheinungsdatum 2017-10
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1106450-x
    ISSN 1347-6947 ; 0916-8451
    ISSN (online) 1347-6947
    ISSN 0916-8451
    DOI 10.1080/09168451.2017.1361810
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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