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人抗神经丝自身抗体的特异性

Specificity of human anti-neurofilament autoantibodies.

作者信息

Braxton D B, Williams M, Kamali D, Chin S, Liem R, Latov N

机构信息

Department of Neurology, Columbia University, College of Physicians and Surgeons, New York, NY 10032.

出版信息

J Neuroimmunol. 1989 Feb;21(2-3):193-203. doi: 10.1016/0165-5728(89)90175-6.

DOI:10.1016/0165-5728(89)90175-6
PMID:2492307
Abstract

The specificities and isotypes of human antibodies that react with neurofilament (NF) proteins were examined by Western blot analysis. Two-thirds of the subjects tested had antibodies to the 200 kDa high molecular weight neurofilament protein (NF-H), and fewer had antibodies to the low and middle molecular weight neurofilament proteins (NF-L and NF-M respectively). Human autoantibodies bound to both native and dephosphorylated NF-H, but some antibodies bound to dephosphorylated NF-H only, indicating the presence of at least two target epitopes. They also recognized a fusion protein containing a segment of the NF-H protein produced by a cDNA clone in Escherichia coli, indicating that they bind to unmodified peptide epitopes. The anti-NF-H antibodies were mostly IgG, but were frequently complexed to IgA or IgM antibodies, possibly with rheumatoid factor or anti-idiotypic activity. These characteristics of anti-NF-H antibodies are most consistent with a secondary immune response that is antigen driven and T-cell dependent.

摘要

通过蛋白质免疫印迹分析检测了与神经丝(NF)蛋白发生反应的人抗体的特异性和亚型。三分之二的受试对象具有针对200 kDa高分子量神经丝蛋白(NF-H)的抗体,而针对低分子量和中分子量神经丝蛋白(分别为NF-L和NF-M)的抗体较少。人自身抗体可与天然和去磷酸化的NF-H结合,但有些抗体仅与去磷酸化的NF-H结合,这表明至少存在两个靶表位。它们还识别一种包含由大肠杆菌中的cDNA克隆产生的NF-H蛋白片段的融合蛋白,这表明它们与未修饰的肽表位结合。抗NF-H抗体大多为IgG,但常与IgA或IgM抗体形成复合物,可能具有类风湿因子或抗独特型活性。抗NF-H抗体的这些特性与由抗原驱动且依赖T细胞的二次免疫反应最为一致。

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Specificity of human anti-neurofilament autoantibodies.人抗神经丝自身抗体的特异性
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