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Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes.

Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes. Research Abstract Details 

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  • Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes. Abstract Text:

    naofumi itohNaofumi Itoh,shinji sakaueShinji Sakaue,hiroaki nakagawaHiroaki Nakagawa,masaki kurogochiMasaki Kurogochi,hiroshi ohiraHiroshi Ohira,kisaburo deguchiKisaburo Deguchi,shin-ichiro nishimuraShin-Ichiro Nishimura,masaharu nishimuraMasaharu Nishimura,naofumi itohNaofumi Itoh,shinji sakaueShinji Sakaue,hiroaki nakagawaHiroaki Nakagawa,masaki kurogochiMasaki Kurogochi,hiroshi ohiraHiroshi Ohira,kisaburo deguchiKisaburo Deguchi,shin-ichiro nishimuraShin-Ichiro Nishimura,masaharu nishimuraMasaharu Nishimura,

    Glycosylation has an important role in regulating properties of proteins and is associated with many diseases. To examine the alteration of serum N-glycans in type 2 diabetes, we used the db/db mouse model. Serum N-glycans were fluorescence labeled and applied to HPLC. There were reproducible differences in N-glycan profiles between the db/db mouse model and the db/+ control. The structures of the oligosaccharides, which had changed in their amounts, were analyzed by a two-dimensional mapping method, matrix-assisted laser desorption ionization-time-of-flight mass spectrometry, and exoglycosidase digestion. Those analyses revealed an increase in the N-glycans possessing alpha1,6-fucose in the serum of db/db mice. The level of alpha1,6-fucosyltransferase mRNA was increased in the liver of the db/db mice. The ratio of a biantennary N-glycan with alpha1,6-fucose to that without alpha1,6-fucose in the liver tissue of the db/db mouse was increased relative to the db/+ control. Next, we analyzed the serum N-glycan profile in human subjects with type 2 diabetes and found an increased amount of a biantennary N-glycan that had an alpha1,6-fucose with a bisecting N-acetylglucosamine. In conclusion, the increase in alpha1,6-fucosylation is a striking change in the serum N-glycans of the db/db mice, whereas the change in the fucosylation in humans with type 2 diabetes was small, albeit statistically significant. It is likely that the change is caused, at least partially, by the increase in the alpha1,6-fucosyltransferase mRNA level in the liver. The increased alpha1,6-fucosylation may affect protein properties associated with the pathophysiology of type 2 diabetes.

    Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes. Publishing Authors By Initials

    n itohN Itoh,s sakaueS Sakaue,h nakagawaH Nakagawa,m kurogochiM Kurogochi,h ohiraH Ohira,k deguchiK Deguchi,s nishimuraS Nishimura,m nishimuraM Nishimura,n itohN Itoh,s sakaueS Sakaue,h nakagawaH Nakagawa,m kurogochiM Kurogochi,h ohiraH Ohira,k deguchiK Deguchi,s nishimuraS Nishimura,m nishimuraM Nishimura,

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    Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: American journal of physiology. Endocrinology and

    VOLUME: 293

    Page Numbers: E1069-77

    Journal Abbreviation: Am. J. Physiol. Endocrinol. Me

    ISSN: 0193-1849

    DAY: 31

    MONTH: 07

    YEAR: 2007

    Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes. Information

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    LANGUAGE: eng

    NlmUniqueID: 100901226

    Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes. Keywords Mesh Terms:

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    Grant and Affiliation Information for Analysis of N-glycan in serum glycoproteins from db/db mice and humans with type 2 diabetes.

    AFFILIATION: First Dept. of Medicine, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Am J Physiol Endocrinol Metab

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