Lin F, Noyer C M, Ye Q, Courvalin J C, Worman H J
Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Hepatology. 1996 Jan;23(1):57-61. doi: 10.1002/hep.510230109.
Autoantibodies from rare patients with primary biliary cirrhosis (PBC) recognize LBR, or lamin B receptor, an integral membrane protein of the inner nuclear membrane. Human LBR has a nucleoplasmic, amino-terminal domain of 208 amino acids followed by a carboxyl-terminal domain with eight putative transmembrane segments. Autoantibodies against LBR from four patients with PBC recognized the nucleoplasmic, amino-terminal domain but not the carboxyl-terminal domain. Immunoblotting of smaller fusion proteins demonstrated that these autoantibodies recognized a conformational epitope(s) contained within the stretch of amino acids from 1 to 60. These results, combined with those of previous studies, show that autoepitopes of nuclear membrane proteins are located within their nucleocytoplasmic domains and that autoantibodies from patients with PBC predominantly react with one domain of a protein antigen. This work also provides further characterization of anti-LBR antibodies that have found utility as reagents in cell biology research.
来自罕见原发性胆汁性肝硬化（PBC）患者的自身抗体可识别LBR，即核纤层蛋白B受体，它是内核膜的一种整合膜蛋白。人LBR具有一个含208个氨基酸的核质氨基末端结构域，其后是一个带有八个推定跨膜片段的羧基末端结构域。来自四名PBC患者的抗LBR自身抗体识别核质氨基末端结构域，但不识别羧基末端结构域。对较小融合蛋白的免疫印迹表明，这些自身抗体识别位于氨基酸1至60片段内的一个构象表位。这些结果与先前研究的结果相结合，表明核膜蛋白的自身表位位于其核质结构域内，且PBC患者的自身抗体主要与蛋白质抗原的一个结构域发生反应。这项工作还进一步表征了抗LBR抗体，这些抗体已在细胞生物学研究中作为试剂发挥了作用。
