PATHOBIOCHEMISTRY OF T FOETUS BOVINE TRICHOMONIASIS

Orosornucid(OMD；α-酸性糖蛋白)是一种小的(K -42,000)具有五个N-连接的复杂糖链的糖蛋白 占其质量的45%。OM[D]是一种正的急性相反应物 人类，在炎症和许多疾病状态下，多糖 成分发生了变化。糖基化模式OMD正在被 为交替基因中的正常状态和变异建立的 产品和疾病状态正在确定。的基础 糖基化模式的变异，特别是关于 刘易斯结构的表达式正在按顺序确定 要获得有关OMD与 E-选择素和OMD的生理作用。有待解决的问题 答案包括：(1)是否偏爱特定的多糖；(2) 用于糖链中的特定分支和(3)用于特定糖基化 炎症诱导系统性红斑狼疮表达的部位，以及(4)是否有 急性炎症(1)、(2)和(3)的差异 和类风湿性关节炎。在此协作之前，我们有 确定了五个组分中每一个的去唾液酸聚糖组成 糖基化位点，并记录了这些位点在 各种各样的疾病。我们还发现两个主要的基因产物 OMD的(I和11)是不同的糖基化，尽管我们是 无法确定AH站点的差异程度。 糖基化图谱分析方法的应用 不同个体的OMD类型及其与自然的关系 病程状态应该导致临床分析，可以 被用来了解疾病的状态，并增加对 糖基化对循环蛋白的作用和调控。这个 持续的Coflabation集中在两个相关领域：1)我们 纯化了基因产物I，目前H的纯度为-80% 序列。各部位糖基化程度的差异是 下定决心。OMD分析不足，将进行这些分析 关于唾液酸化形式的蛋白质，以提供分布 NeuNAc是这些网站中的一个。2)血清ONO浓度和 在疾病中，个别部位的糖类分布也会发生变化 唾液酸化的程度。特别是，唾液酸路易斯的量 OMD携带的X抗原在炎症中增加。我们会跟着去的 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作用，以及 在治疗过程中。这些数据将与 白细胞与炎症血管内皮细胞的相互作用 是通过SLeX结构和E-选择素介导的。结构性的 将对OMD的一系列亚群进行分析 根据凝集素的分级不同，它们的糖形含量也不同。在……里面 阿姆斯特丹实验室，岩藻糖基化不同的AGP糖蛋白 和二角体多糖含量现在和将来都将从 患者在各种炎症条件下。精选这些 糖型正在分析它们的总的糖链组成。 和糖基化位点，与辛辛那提和 波士顿集团。

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.