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多发性骨髓瘤中多克隆和副蛋白IgG的糖基化

Glycosylation of polyclonal and paraprotein IgG in multiple myeloma.

作者信息

Farooq M, Takahashi N, Arrol H, Drayson M, Jefferis R

机构信息

Department of Immunology, The Medical School, Edgbaston, Birmingham, UK.

出版信息

Glycoconj J. 1997 Jun;14(4):489-92. doi: 10.1023/a:1018555619519.

Abstract

It has previously been shown that in multiple myeloma (MM) each IgG paraprotein exhibits a unique oligosaccharide profile. It has been assumed that this results from a clone specific glycosylation machinery. However, the abnormal physiological environment of the bone marrow in this disease may also affect normal plasma cells producing polyclonal IgG. We present data to show that this is so and that, in two cases, the oligosaccharide profile of the polyclonal IgG reflected that of the paraprotein from the same patient rather than that of normal polyclonal IgG.

摘要

此前已有研究表明,在多发性骨髓瘤(MM)中,每种IgG副蛋白都呈现出独特的寡糖谱。人们认为这是由克隆特异性糖基化机制导致的。然而,这种疾病中骨髓异常的生理环境也可能影响产生多克隆IgG的正常浆细胞。我们提供的数据表明确实如此,并且在两个病例中,多克隆IgG的寡糖谱反映的是同一患者副蛋白的寡糖谱,而非正常多克隆IgG的寡糖谱。

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