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抗髓鞘少突胶质细胞糖蛋白抗体的脱髓鞘潜能与其补体固定能力有关。

The demyelinating potential of antibodies to myelin oligodendrocyte glycoprotein is related to their ability to fix complement.

作者信息

Piddlesden S J, Lassmann H, Zimprich F, Morgan B P, Linington C

机构信息

Department of Medical Biochemistry, University of Wales, College of Medicine, Cardiff.

出版信息

Am J Pathol. 1993 Aug;143(2):555-64.

Abstract

A panel of 13 monoclonal antibodies (mAbs) has been raised to the central nervous system-specific glycoprotein, myelin oligodendrocyte glycoprotein; five of these mAbs recognize a carbohydrate epitope on the molecule. Although all of the mAbs recognized surface epitopes on cultured oligodendrocytes and stained central nervous system tissue sections in a similar manner, marked differences were seen in their ability to induce demyelination in experimental allergic encephalomyelitis in the Lewis rat. This variation in pathogenic potential was not related to the specificity of a given mAb for carbohydrate or peptide epitopes of myelin oligodendrocyte glycoprotein, but correlated with its ability to fix complement.

摘要

已制备出一组针对中枢神经系统特异性糖蛋白——髓鞘少突胶质细胞糖蛋白的13种单克隆抗体(mAb);其中5种mAb识别该分子上的一个碳水化合物表位。尽管所有mAb均识别培养的少突胶质细胞上的表面表位,并以类似方式对中枢神经系统组织切片进行染色,但在Lewis大鼠实验性变应性脑脊髓炎中,它们诱导脱髓鞘的能力存在显著差异。这种致病潜力的差异与特定mAb对髓鞘少突胶质细胞糖蛋白碳水化合物或肽表位的特异性无关,而是与其补体固定能力相关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/06f0/1887024/636edcab31f8/amjpathol00068-0241-a.jpg

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