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针对阿片受体的人抗独特型抗体。

Human antiidiotypic antibody against opiate receptors.

作者信息

Roy B F, Bowen W D, Frazier J S, Rose J W, McFarland H F, McFarlin D E, Murphy D L, Morihisa J M

机构信息

Department of Psychiatry, Georgetown University School of Medicine, Washington, DC 20007.

出版信息

Ann Neurol. 1988 Jul;24(1):57-63. doi: 10.1002/ana.410240111.

Abstract

Sera containing antibodies to beta-endorphin from 2 patients with major depressive disorder were shown to have antidiotypic antibodies that specifically inhibited reactivity between anti-beta-endorphin IgG and beta-endorphin. Autologous and homologous antiidiotypic anti-anti-beta-endorphin IgG antibodies were isolated by affinity chromatography. The purified antiidiotypic antibody did not bind beta-endorphin but competed with [125I]beta-endorphin for rat brain opiate receptors. Normal IgG that was similarly treated had negligible competitive effects. The antibody bound to the membrane preparation; such binding was inhibited by opiate receptor ligands. Binding of the antiidiotype to a 60,000-dalton protein from rat brain was detected by Western immunoblot analysis. This protein corresponds in molecular weight to proteins proposed to be components of opiate receptors. These findings imply that immune reactivity to neuropeptides could contribute to psychiatric impairment.

摘要

研究表明,来自2名重度抑郁症患者的含有β-内啡肽抗体的血清具有抗独特型抗体,该抗体能特异性抑制抗β-内啡肽IgG与β-内啡肽之间的反应性。通过亲和层析分离出了自体和同源抗独特型抗抗β-内啡肽IgG抗体。纯化后的抗独特型抗体不与β-内啡肽结合,但能与[125I]β-内啡肽竞争大鼠脑阿片受体。经过类似处理的正常IgG的竞争作用可忽略不计。该抗体与膜制剂结合;这种结合可被阿片受体配体抑制。通过Western免疫印迹分析检测到抗独特型与大鼠脑60000道尔顿蛋白的结合。该蛋白的分子量与被认为是阿片受体组成成分的蛋白相对应。这些发现表明,对神经肽的免疫反应性可能导致精神障碍。

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