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PATHOBIOCHEMISTRY OF T FOETUS BOVINE TRICHOMONIASIS

PATHOBIOCHEMISTRY OF T FOETUS BOVINE TRICHOMONIASIS
胎牛滴虫病的病原生物化学
批准号:
6478978
负责人:
BIBHUTI N. SINGH
金额:
$5.36万
依托单位国家:
美国
项目类别:
财政年份:
2000
资助国家:
美国
项目状态:
已结题
起止时间:
2000-07-01 至 2002-06-30

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中文摘要
翻译
Orosornucoid(OMD;糖醛酸糖蛋白)是一种小的(K -42,000)糖蛋白,具有五个N-连接的复合聚糖链, 包括其质量的约45%。 OM[D]是一种阳性急性期反应物, 在炎症和许多疾病状态下, 组成变化。 糖基化模式OMD正在被 建立了交替基因的正态和方差 产品和疾病状态正在建立。 的基础 糖基化模式的变化,特别是关于 刘易斯结构的表达式,正在确定, 为了获得关于OMD与 E-选择素和OMD的生理作用。 疑问待 回答包括:(1)是否存在对特定聚糖的偏好,(2) 对于聚糖中的特定分支和(3)对于特定糖基化 炎症诱导的Sle表达的位点,以及(4)是否存在 急性炎症之间(1)、(2)和(3)的差异 和类风湿性关节炎。 在这次合作中,我们 建立了五种去唾液酸聚糖的组成, 糖基化位点,并记录了这些如何在一个 各种疾病。 我们还发现两种主要的基因产物 (I和11)OMD的糖基化差异,虽然我们 无法确定aH位点差异的程度。 糖基化分析方法的应用 不同个体的OMD模式及其与自然的关系 和病程状态应该导致临床测定, 用于了解疾病状态,并增加对 糖基化对循环蛋白的作用和控制。 的 持续的合作集中在两个相关的领域:1)我们 已经纯化了基因产物I,目前通过PCR检测具有约80%纯度的H, 顺序 每个位点糖基化的差异将是 测定 OMD唾液酸化不足,将进行这些分析 对唾液酸化形式的蛋白质,以提供分布 NeuNAc在研究中心中。 2)血清ONO浓度及 在疾病中,单个位点的糖型分布发生变化, 唾液酸化的程度。 特别地,唾液酸刘易斯的量 OMD携带的X抗原在炎症中增加。 我们将遵循 SLex在每个糖基化位点的发生过程, 炎症在急性和慢性阶段的功能,以及 在治疗期间。 这些数据将与 白细胞与炎症内皮细胞的相互作用,因为 通过SLex结构和E-选择素介导。 结构性 将对一系列OMD亚群进行分析, 基于凝集素分级,它们的糖型含量不同。 在 阿姆斯特丹实验室,岩藻糖基化不同的AGP糖型 和双触角聚糖含量是,并将从血清中分离, 各种炎症条件下的患者。 其中的一个选择 糖型”正在分析它们的总聚糖组成 和全糖基化位点,与辛辛那提和 波士顿集团
英文摘要
Orosornucoid (OMD; alphal-acid glycoprotein) is a small (K -42,000) glycoprotein with five N-linked complex glycan chains that comprise -45% of its mass. OM[D is a positive acute phase reactant in humans, and during inflammation and many disease states, the glycan composition changes. The glycosylation patterns OMD are being established for the normal state and the variance in thealternate gene product and in disease states are being established. The basis for variation in the glycosylation patterns, particularly with regard to the expression of the Lewis' structure, is being determined in order to gain further information about the interaction of OMD with E-selectin and the physiological role of OMD. Questions to be answered include: (1) is there a preference for specific glycans, (2) for specific branches in glycans and (3) for specific glycosylation sites for the inflammation-induced expression of SLe, and (4) is there a difference in (1), (2) and (3) between acute inflammation andrheumatoid arthritis. Previously in this collaboration, we have established the asialoglycan compositions at each of the five glycosylation sites, and documented how these have changed in a vaiiety of diseases. We also found that the two major gene products (I and 11) of OMD were differentially glycosylated, although we were not able to determine the extent of the differences at aH sites. Applications of the methods developed for profiling the glycosylation patterns of OMD in different individuals and in relation to the nature and course of disease states should lead to clinical assays that can be used to foHow disease states and to increased understanding of the role and control of glycosylation on circulating proteins. The continuing coflaboration concentrates on two related areas: 1) We have purified gene product I and presently have H at -80% purity by sequence. The differences in glycosylation at each site wiH be determined. OMD is under-sialylated, and these analyses will be done on the sialylated forms of the proteins to provide the distribution of NeuNAc among the sites. 2) The serum concentration of ONO and the glycoform distribution at individual sites change in disease, as does the extent of sialylation. In particular, the amount of sialyl Lewis X antigen carried by OMDincreases in inflarnmation. We shall follow the course of occurrence of SLex at each glycosylation site as a function of inflammation through the acute and chronic stages, and during treatment. These data will be compared with the extent of interaction of leucocytes with the inflamed endothelium, since tl~iis is mediated via the SLex structure and E-selectin. The structural analyses will be performed on a series of subpopulations of OMD that differ in their glycoform content based on lectin fractionation. In the Amsterdam laboratory, glycofon-ns of AGP differing in fucosylation and diantennary glycan content are and will be isolated from sera of patients under various inflammatory conditions. A selection of these glycoforms is" being analyzed for their glycan composition in total and perglycosylation sites, in collaboration with the Cincinnati and Boston groups.
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CHARACTERIZATION OF TRICHOMONAD LIPOPHOSPHOGLYCAN
  • 批准号:
    8365543
  • 项目类别:
  • 资助金额:
    $1.7万
  • 财政年份:
    2011
  • 负责人:
    BIBHUTI N. SINGH
  • 依托单位:
CHARACTERIZATION OF TRICHOMONAD LIPOPHOSPHOGLYCAN
  • 批准号:
    8170911
  • 项目类别:
  • 资助金额:
    $1.02万
  • 财政年份:
    2010
  • 负责人:
    BIBHUTI N. SINGH
  • 依托单位:
CHARACTERIZATION OF TRICHOMONAD LIPOPHOSPHOGLYCAN
  • 批准号:
    7955945
  • 项目类别:
  • 资助金额:
    $0.99万
  • 财政年份:
    2009
  • 负责人:
    BIBHUTI N. SINGH
  • 依托单位:
IDENTIFICATION & CHARACTERIZATION OF TRICHOMONAD CYSTEINE PROTEASES
  • 批准号:
    7955896
  • 项目类别:
  • 资助金额:
    $0.25万
  • 财政年份:
    2009
  • 负责人:
    BIBHUTI N. SINGH
  • 依托单位:
海外基金