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人神经病患者中一种单克隆IgM所识别的髓鞘相关糖蛋白表位的分子特征

Molecular characteristics of the epitope in myelin-associated glycoprotein that is recognized by a monoclonal IgM in human neuropathy patients.

作者信息

Frail D E, Edwards A M, Braun P E

出版信息

Mol Immunol. 1984 Aug;21(8):721-5. doi: 10.1016/0161-5890(84)90024-5.

Abstract

The antigen for the IgM monoclonal antibody from patients with IgM paraproteinemia and peripheral neuropathy is the myelin-associated glycoprotein (MAG), a minor protein component of both human PNS myelin and human CNS myelin. Sera from five patients were found to react with identical proteolytically derived fragments of MAG indicating that the monoclonal IgM from these patients is recognizing a common epitope. Furthermore, the lectin concanavalin A reacts with these fragments and deglycosylation of isolated MAG abolishes the recognition of MAG by the patient monoclonal IgM. Therefore, it appears that the monoclonal IgM from these five patients recognizes a common epitope which contains carbohydrate moieties. These data are consistent with the idea that the peripheral myelin sheath is involved in an autoimmune response directed against MAG.

摘要

来自患有IgM副蛋白血症和周围神经病变患者的IgM单克隆抗体的抗原是髓鞘相关糖蛋白(MAG),它是人类周围神经系统髓鞘和中枢神经系统髓鞘的一种次要蛋白质成分。发现五名患者的血清与MAG相同的蛋白水解衍生片段发生反应,表明这些患者的单克隆IgM识别一个共同表位。此外,凝集素伴刀豆球蛋白A与这些片段发生反应,并且分离的MAG去糖基化消除了患者单克隆IgM对MAG的识别。因此,似乎这五名患者的单克隆IgM识别一个包含碳水化合物部分的共同表位。这些数据与周围髓鞘参与针对MAG的自身免疫反应这一观点一致。

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