Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
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抗苏氨酰-tRNA 合成酶，第二种肌炎相关自身抗体
DOI：
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发表时间：
1984
影响因子：
15.3
通讯作者：
R. Bernstein
中科院分区：
文献类型：
--
作者：
M. Mathews;M. Reichlin;G. Hughes;Ant;R. Bernstein
在四名肌炎患者和一名系统性红斑狼疮样综合征患者的血清中发现了一种称为 PL-7 的自身抗体。 PL-7 抗原是一种 80,000 道尔顿的多肽，可与转移 RNA 共沉淀。在氨酰化反应中，PL-7 IgG 抑制苏氨酸对 tRNA 的充电，但对其他氨基酸的充电影响很小或没有影响。针对纯化的苏氨酰-tRNA 合成酶产生的实验抗体识别相同的 80,000 道尔顿多肽，但 tRNA 未共沉淀。我们得出结论，PL-7 抗体针对苏氨酰-tRNA 合成酶，并且人类和实验自身抗体可识别不同的抗原位点。我们的研究结果强调了肌炎和 tRNA 相关结构的自身免疫之间的联系。
An autoantibody known as PL-7 was found in the serum of four patients with myositis and one with a systemic lupus erythematosus-like syndrome. The PL-7 antigen is an 80,000 dalton polypeptide that coprecipitates with transfer RNA. In aminoacylation reactions, PL-7 IgG inhibited the charging of tRNA with threonine but had little or no effect on charging with other amino acids. Experimental antibodies raised against purified threonyl-tRNA synthetase recognized the same 80,000 dalton polypeptide, but tRNA was not coprecipitated. We conclude that PL-7 antibody is directed at threonyl-tRNA synthetase, and that different antigenic sites are recognized by the human and experimental autoantibodies. Our findings emphasize the link between myositis and autoimmunity to tRNA-related structures.
影响因子：
15.9
作者：
HARDIN, JA;RAHN, DR;STEITZ, JA
通讯作者：
STEITZ, JA