Structural studies on folding and interactions of glycoconjugates of immunological interests
Structural studies on folding and interactions of glycoconjugates of immunological interests
批准号:
13470498
负责人:
KATO Koichi
金额:
$9.22万
依托单位:
依托单位国家:
日本
项目类别:
Grant-in-Aid for Scientific Research (B)
财政年份:
2001
资助国家:
日本
项目状态:
已结题
起止时间:
2001 至 2002
中文摘要
糖链是参与细胞间通讯的分子识别媒介,对糖蛋白的折叠和质量控制有重要作用。虽然糖链的生物学意义已被广泛认识,但从结构方面对其具体作用知之甚少。在本研究中,我们发展了核磁共振和多维高效液相色谱方法,用于阐明具有免疫学意义的糖偶联物的糖链生物学功能。通过使用这些技术,我们解决了以下问题:1)糖链与细胞内凝集素如钙网蛋白和血管活性肠肽-36的相互作用模式)免疫球蛋白G Fc部分的糖链在与Fcγ受体和类风湿因子相互作用中的作用。3)核磁共振和高效液相分析重组CD1糖蛋白表达的碳水化合物部分。4)各种病理条件下血清IgS的糖基化图谱。
英文摘要
Sugar chains of glycoconjugates mediate molecular recognition involved in cell-cell communication and contribute to folding and quality control of glycoproteins. Although biological significance of sugar chains were widely recognized, little was known about their specific roles from a structural aspect. In the present study, we have developed nuclear magnetic resonance (NMR) and multi-dimensional HPLC methods for the elucidation of biological functions of sugar chains of glycoconjugates of immunological interests. By use of these techniques, we have addressed the following issues :1) Modes of interactions between sugar chains and intracellular lectins such as calreticulin and VIP-36.2) Roles of the sugar chains attached to the Fc portion of immunoglobulin G (IgG) in the interactions with Fcγ receptors and rheumatoid factors.3) NMR and HPLC analyses of the carbohydrate moieties expressed by recombinant CD1 glycoproteins.4) Glycosylation profiling of serum IgGs under a variety of pathological conditions.
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山口芳樹, 加藤晃一: "免疫系糖タンパク質の構造生物学"生化学. 74. 43-46 (2002)
Yoshiki Yamaguchi、Koichi Kato:“免疫系统糖蛋白的结构生物学”生物化学 74. 43-46 (2002)。
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M.Holland et al.: "Hypogalactosylation of serum IgG in patients with ANCA-associated systemic vasculitis"Clin. Exp. Immunol.. 129. 183-190 (2002)
M.Holland 等人:“ANCA 相关系统性血管炎患者血清 IgG 的低半乳糖基化”Clin。
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N.Takahashi et al.: "N-glycan structure of squid rhodopsin : Existence of the α1-3 and α1-6 difucosylated intermost GlcNAc residue in a molluscan glycoprotein"Eur. J. Biochem.. (印刷中). (2003)
N. Takahashi 等人:“鱿鱼视紫红质的 N-聚糖结构:软体动物糖蛋白中 α1-3 和 α1-6 二岩藻糖基化的最中间 GlcNAc 残基的存在”Eur. J. Biochem.(出版中)。
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N.Takahashi et al.: "N-glycan structures from the major glycoproteins of pigeon egg white. Predominance of terminal Gal.alpha. (1-4)Gal"J. Biol. Chem.. 276. 23230-23239 (2001)
N.Takahashi 等人:“鸽子蛋清主要糖蛋白的 N-聚糖结构。末端 Gal.alpha. (1-4)Gal 的优势”J。
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作者:
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通讯作者:
N. Takahashi et al.: "N-glycan structures from the major glycoproteins of pigeon egg white. Predominance of terminal Gal. alpha. (1-4) Gal"J. Biol Chem.. 276(26). 23230-23239 (2001)
N. Takahashi 等人:“鸽子蛋清主要糖蛋白的 N-聚糖结构。末端 Gal. alpha. (1-4) Gal 的优势”J.
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